MXPA99010661A - Grapevine leafroll virus (type 2) proteins and their uses - Google Patents

Abstract

The present invention relates to isolated proteins or polypeptides of grapevine leafroll virus (type 2). The encoding DNA molecules either alone in isolated form or in an expression system, a host cell, or a transgenic grape plant are also disclosed. Other aspects of the present invention relates to a method of imparting grapevine leafroll resistance to grape and tobacco plants by transforming them with the DNA molecules of the present invention, a method of imparting beet yellows virus resistance to a beet plant, a method of imparting tristeza virus resistance to a citrus plant, and a method of detecting the presence of a grapevine leafroll virus, such as GRLaV-2, in a sample.

Description

PROTEINS, AND THEIR USES, OF THE VIRUS (TYPE 2) OF THE VINE LEAF ROLL This application claims the benefit of United States Provisional Patent Application Serial No. 60 / 047,194, filed May 20, 1997. This work was supported by the United States Department of Agriculture, Cooperative Grant Number 58- 2349-9-01. The Government of the United States can have certain rights in the invention. Field of the Invention The present invention relates to vine leaf winding virus proteins (Type 2), to DNA molecules that encode these proteins, and to their uses. Background of the Invention The most widely cultivated fruit crop, the grape (Vitis sp.), Is grown on all continents, except Antarctica. However, the largest grape production centers are in European countries (including Italy, Spain and France), which account for approximately 70 percent of world grape production (Mullins et al., Bioloay of the Grapevine), Cambridge, United Kingdom: University Press (1992)). The United States, with 300,000 hectares of vines, is the eighth largest grower of grapes in the world, although grapes have many uses, a larger portion of grape production (approximately 80 percent) is used for wine production Unlike most cereal crops, most of the world's vineyards are planted with traditional vine crops, which have been perpetuated for centuries by vegetative propagation, several important vine viruses and virus-like diseases, such as such as winding vine leaf, cork bark, and Rupestris stem sting, are transmitted and spread through the use of vegetatively propagated infected materials.Therefore, the propagation of certified virus-free materials is one of the measures of most important disease control Traditional breeding for disease resistance is difficult due to the highly heterozygous nature and behavior of crosses of different types of vines, and due to the polygenic patterns of the inheritance. Moreover, the introduction of a new crop may be prohibited by custom or by law. Recent biotechnological developments have made possible the introduction of special traits, such as resistance to diseases, in an established crop, without altering its horticultural characteristics. Many plant pathogens, such as fungi, bacteria, phytoplasmas, viruses, and nematodes, can infect grapes, and the resulting diseases can cause substantial losses in production (Pearson et al., Compendium of Grape Diseases, American Phytopathological Society Press (1988)). Among these, viral diseases are a major impediment to the lucrative cultivation of vines. Approximately 34 viruses of the vines have been isolated and characterized. The major virus diseases are grouped into: (1) the degeneration of the vine caused by the fan leaf nepovirus, other European nepoviruses, and American nepoviruses, (2) the leaf rolling complex, and (3) the complex of rough wood (Martelli, ed., Graft Transmissible Diseases of Grapevi-nes, Handbook for Detecting and Diagnosis, FAO, UN, Rome, Italy (1993)). Of the major virus diseases, the vine leaf winding complex is the largest entity distributed throughout the world. According to Goheen ("Grape Leafroll", in Frazier et al., Eds., Diseases of Small Fruits and Grapevines Virus (A Handbook), University of California, Division of Agricultural Sciences, Berkeley, Calif., USA, page 209-212 (1970) ("Goheen (1970)"), vine leaf curl type disease was described as early as in the 1850s in German and French literature, however, the viral nature of the disease was demonstrated first by Scheu (Scheu, "Die Rollkrankheit des Rebstockes (Leafroll of grapevine)", D. D. Weinbau 14: 222-358 (1935) ("Scheu (1935)")). In 1946, Harmon and Snyder (Harmon et al., "Investigations on the Occurrence, Transmission, Spread and Effect of 'White' Fruit Color in the Emperor Grape," Proc. Am. Soc. Hort. Sci. 74: 190-194 ( 1946)) determined the viral nature of White Emperor disease in California. It was subsequently tested by Goheen et al., (Goheen et al, "Leafroll (White Emperor Disease) of Grapes in California", Phvtopatholoav, 48: 51-54 (1958) ("Goheen (1958)"), which both the curl of Leaf like the "White Emperor" disease were the same, and only the name "leaf curl" was retained.The leaf curl is a serious viral disease of the grapes, and occurs whenever grapes are grown. The disease has been caused by the spread of diseased vines, affecting almost all cultivated varieties and the rhizome of Vitis, although the disease is not lethal, results in yield losses and a reduction in the sugar content, Scheu estimated in 1936 that 80 percent of all vines planted in Germany were infected (Scheu, Mein Winzerbuch, Berlin: Reichsnahrstand-Verlags (1936)). In many grape vineyards in California, the incidence of leaf curl (basal A study of field symptoms conducted in 1959) agrees with Scheu's initial observation in the German vineyards (Goheen et al., "Studies of Grape Leafroll in California", Amer. J. Enol. Vitic, 10: 78-84 (1959)). The current situation on leaf curl disease does not seem to be better (Goheen, "Diseases Caused by Viruses and Viruslike Agents", The American Phytopatholoqical Societv, St. Paul, Minnesota: APS Press, 1: 47-54 (1988) ( "Goheen (1988)").

Goheen also estimated that the disease causes an annual loss of about 5 to 20 percent of total grape production (Goheen (1970) and Goheen (1988)). The amount of sugar in the individual berries of the infected vines is only about 1/2 to 2/3 of the berries of uninfected vines (Goheen (1958)). The symptoms of leaf rolling disease vary considerably, depending on the crop, the environment and the time of year. In red or dark fruit varieties, the typical downward curl and interveinal reddening of mature basal leaves is most prevalent in autumn; but not in primary or early summer. However, in light colored fruit varieties, the symptoms are less conspicuous, usually with downward curl accompanied by interveinal chlorosis. Moreover, many infected rhizome cultures do not develop the symptoms. In these cases, the disease is usually diagnosed with a woody indicator marker test using Vitis viviera variety Cabernet Franc (Goheen (1988)). Since Scheu showed that leaf curl was transmissible by grafting, it has always been suspected of a viral etiology (Scheu (1935)). Several types of virus particles have been isolated from diseased leaf curl vines. These include the type potivirus (Tanne et al., "Purification and Characterization of a Virus Associated with the Grapevine Leafroll Disease", Phytopatholoav, 67: 442-447 (1977)), the type of isometric virus (Castilian and collaborators, "Viruslike Particles and Ultrastructural Modifications in the Phloem of Leafroll-affected Grapevines ", Vitis, 22: 23-39 (1983) (" Spanish (1983) "), and Namba et al," A Small Spherical Virus Associated with the Ajinashika Disease of Koshu Grapevine ", Ann. Phytopathol, Soc. Japan, 45: 70-73 (1979)), and closterovirus type (Namba," Grapevine Leafroll Virus, a Possible Member of Closteroviruses, Ann. Phytopathol. Soc. Japan, 45: 497- 502 (1979)). However, in recent years, long flexo closteroviruses, from 1,400 to 2,200 nanometers, have been associated more consistently with leaf rolling disease (Figure 1) (Castellano (1983), Faoro et al. , Association of a Possible Closterovirus with Grapevine Leafroll in Northern Italy ", Riv. Patol. See . Ser IV, 17: 183-189 (1981), Gugerli et al., "L 'enroulement de la vigne: mise en évidence de particules virales et développement d'une méthode immuno-enzymatigue pour le diagnostic rapide (Grapevine Leafroll: Presence of Virus Particles and Development of an Immuno-enzyme method for Diagnosis and Detection), "Rev. Suisse Viticult. Arboricult. Hort., 16: 299-304 (1984) ("Gugerli (1984)"), Hu et al., "Characterization of Closterovirus-like Particles Associated with Grapevine Leafroll Disease", J. Phytopathol. , 128: 1-14 (1990) ("Hu (1990)"), Milne et al., "Closterovirus-like Particles of Two Types Associated with Grapevine Diseases", Phytopathol. Z., 110: 360-368 (1984), Zee et al., "Cytopathology of Leafroll-diseased Grapevines and the Purification and Serology of Associated Closterovirus-like Particles," Phvtopatholoav, 77: 1427-1434 (1987) ("Zee (1987) "), and Zimmermann et al.," Characterization and Serological Detection of Four Closterovirus-like Particles Associated with Leafroll Disease on Grapevine ", J. Phytopathol., 130: 205-218 (1990) (" Zimmermann (1990) "). These closteroviruses are referred to as viruses associated with vine leaf curl ("GLRaV"). At least six serologically distinct types of GLRaVs (GLRaV-1 to -6) have been detected from diseased leaf curl vines (Table 1) (Boscia et al., "Nomenclature of Grapevine Leafroll-associated Putative Closer-viruses, Vitis , 34: 171-175 (1995) ("Boscia (1995)") and (Martelli, "Leafroll", pages 37-44 in Martelli, editor, Graft Transmissi-ble Diseases of Grapevines, Handbook for Detection and Diagnosis, FAO, Rome, Italy (1993) ("Martelli I")) The first five were confirmed at the 10th Meeting of the International Council for the Study of Virus and Virus Diseases of the Grapevine ("ICVG") (Volos, Greece, 1990) .

TABLE 1 However, through the use of monoclonal antibodies, it has been shown that the original GLRaV II described in Gugerli (1984) is an apparent mixture of at least two components, lia and Ilb (Gugerli et al., "Grapevine Leafroll Associated Virus II Analyzed by Monoclonal Antibodies ", llth Meeting of the International Council for the Study of Viruses and Viruses Diseases of the Grapevine, Montreux, Switzerland, pages 23-24 (1993) (" Gugerli (1993) "). Recent research with comparative serological assays (Boscia (1995)) showed that the Ilb component of the Chasselas variety 8/22 is the same as the GLRaV-2 isolate from France (Zimmermann (1990)), which also includes closterovirus isolates associated with vine cork bark. from Italy (GCBaV-BA) (Boscia (1995)) and from the United States (GCBaV-NY) (Namba et al., "Purification and Properties of Closterovirus-like Particles Associated with Grapevine Corky Bark Disease", Phytopatholoqy, 81: 964 -970 (1991) ("Namba (1991)")). The lia component of the Chasselas 8/22 variety was provisionally named as the virus associated with vine leaf roll 6 (GLRaV-6). In addition, the antiserum for the CA-5 isolate of GLRaV-2 produced by Boscia et al. (Boscia et al., "Characterization of Grape Leafroll Associated Closterovirus (GLRaV) Serotype II and Comparison with GLRaV Serotype III", Phytopathology, 80: 117 (1990)) showed to contain antibodies for both GLRaV-2 and GLRaV-1, with a prevalence of the latter (Boscia (1995)). The GLRaV-2 virions are flexuous filamentous particles of approximately 1,400 to 1,800 nanometers in length (Gugerli et al., "L1 enroulement de la Vigne: Mise en Evidence de Particles Virales et Development d'une Methode Immuno-enzymatique Pour le Diagnostic Rapide" (Grapevine Leafroll: Presence of Virus Particles and Development of an Immuno-enzyme Method for Diagnosis and Detection) (Vine Leaf Curl: Presence of Virus Particles and Development of an Immunoenzymatic Method for Diagnosis and Detection), Rev. Suisse Viticult, Arboricult, Horticult 16: 299-304 (1984)). A double-stranded RNA (dsRNA) of approximately 15 kb was consistently isolated from tissues infected with GLRaV-2 (Goszcynski et al., "Detection of Two Strains of Grapevine Leafroll-Associated Virus 2", Vitis 35: 133-35 (nineteen ninety six)) . The coating protein of GLRaV-2 is approximately 22 to 26 kDa (Zimmermann et al., Characterization and Serological Detection of Four Closterovirus-like Particles Associated with Leafroll Disease on Grapevine ", J. Phytopathology 130: 205-18 (1990); Gugerli and Ramel, extended abstracts: "Grapevine Leafroll Associated Virus II Analyzed by Monoclonal Antibodies", llth ICVG in Montreux, Switzerland, Gugerli, editor, Federal Agricultural Research Station of Changins, CH-1260 Nyon, Switzerland, pages 23-24 (1993) ), Boscia et al, "Nomenclatu-re of Grapevine Leafroll-Associated Putative Closteroviruses", Vitis 34: 171-75 (1995)), which is considerably more similar than other GLRaVs (from 35 to approximately 43 kDa) (Zee et al. , "Cytopathology of Leafroll-Diseased Grapevines and the Purification and Serology of Associated Closterovirus Like Particles", Phytopatholoqy 77: 1427-34 (1987); Hu et al., "Characterization of Closterovirus-Like Particles Associa ted with Grapevine Leafroll Disease ", J. of Phytopathology 128: 1-14 (1990); Ling et al., "The Coat Protein Gene of Grapevine Leafroll Associated Closterovirus-3: Cloning, Nucleotide Sequencing and Expression in Transgenic Plants", Arch. Of Viroloqy 142: 1101-16 (1997)). Although GLRaV-2 has been classified as a member of the genus Closterovirus, based on the morphology and cytopathology of the particles (Martelli, Circular of ICTV-Plant Virus Subcommittee Study Group on Closterolike Viruses (1996)), its molecular and biochemical properties In the group of closteroviruses, several viruses have recently been sequenced: the partial or complete genome sequences of yellow beet virus (BYV) (Agranovsky et al., "Nucleotide Seguence of the 3 '-Terminal Half of Beet Yellows Closterovirus RNA Genome Unique Arrangement of Eight Virus Genes ", J. General Virology 72: 15-24 (1991); Agranovsky et al., "Beet Yellows Closterovirus: Complete Genome Structure and Identification of a Papain-like Thiol Protease", Virology 198: 311-24 (1994)), yellow beetle wilt virus (BYSV) (Karasev et al., "Orgapization of the 3'-Terminal Half of Beet Yellow Stunt Virus Genome and Implications for the Evolution of Closteroviruses ", Viroloqy 221: 199-207 (1996)); Citrus tristeza virus (CTV) (Pappu et al., "Nucleotide Sequence and Organization of Eight 3 'Open Reading Frames of the Citrus Tristeza Closterovirus Genome", Virology 199: 35-46 (1994); Karasev et al., "Complete Sequence of the Citrus Tristeza Virus RNA Genome ", Viroloqy 208: 511-20 (1995)), yellow infectious lettuce virus (LIYV) (Klaassen et al.," Partial Characterization of the Lettuce Infectious Yellows Virus Genomic RNAs, Identification of the Coat Protein Gene and Comparison of its amino acid Sequence With Those of Other Filamentous RNA Plant Viruses ", J. General Viroloqy 75: 1525-33 (1995)), small cherry virus (LChV) (Keim and Jelkmann," Genome Analysis of the 3 '-Terminal Part of the Little Cherry Disease Associated dsRNA Reveal Monopartite Clostero-Like Virus, "Arch. Virology 141: 1437-51 (1996); Jelkmann et al.," Complete Genome Structure and Phylogenetic Analysis of Little Cherry Virus, " Mealybug-Transmissible Closteroviru s ", J. General Virology 78: 2067-71 (1997)), and GLRaV-3 (Ling et al.," Nucleotide Sequence of the 3 'Terminal Two-Thirds of the Grapevine Leafroll Associated Virus-3 Genome Reveal Typical Monopartite Closterovirus ", J. Gen. Virology 79 (5): 1289-1301 (1998)) revealed some common features of closteroviruses, including the presence of the HSP70 chaperone heat shock protein, and a duplicate of the protein coating (Agranovsky, "Principles of Molecular Organization, Expression, and Evolution of Closteroviruses: Over the Barriers", Adv. in Virus Res. 47: 119-218 (1996); Dolja et al., "Molecular Biology and Evolution of Closter Viruses: Sophisticated Build-up of Large RNA Genomes", Annual Rev. Photopathology 32: 261-85 (1994); Boyko et al., "Coat Protein Gene Duplication in a Filamentous RNA Virus of Plants", Proc. Nat. Acad. Sci. USA 89: 9156-60 (1992)). The characterization of the genome organization of the GLRaVs would provide molecular information on serologically distinct closteroviruses that cause symptoms of similar leaf curl in the vine. Several shorter closteroviruses (800 nanometer long particle length) have also been isolated from vines. One of these, called Grapevine Virus A ("GVA") has also been found associated, albeit inconsistently, with leaf curl disease (Agran et al., "Ocurrence of Grapevine Virus A (GVA) and Other Closterovi-ruses in Tunisian Grapevines Affected by Leafroll Disease ", Vitis, 29: 43-48 (1990), Conti et al, Closterovirus Associated with Leafroll and Stem Pitting in Grapevine", Phvtopathol. Mediterr., 24: 110-113 (1985 ), and Conti et al, "A Closterovirus from a Stem-pitting-diseased Grapevine", Phvtopathology, 70: 394-399 (1980).) The etiology of GVA is not really known, however, it seems to be more consistently associated with The sensu is made of rough wood (Rosciglione et al., "Maladies de 1 'enroulement et du bois strie de la vigne: analyze microscopique et seologique (Leafroll and Stem Pitting of Grapevine: Microscopical and Serological Analysis) Vine Stem: Analysis M icroscopic and Serological) ", Rev. Suisse Vitic Arboric. Hortic , 18: 207-211 (1986) ("Rosciglione (1986)"), and Zimmermann (1990)). Furthermore, another short closterovirus (800 nanometers long) known as B vine virus ("GVB") has been isolated and characterized from vines affected by cork bark (Boscia et al., "Properties of a Filamentous Virus Isolated from Grapevines Affected by Corky Bark ", Arch. Virol., 130: 109-120 (1993) and Namba (1991)).

As suggested by Martelli I, leaf roll symptoms may be induced by more than one virus, or may simply be a general physiological response of the plant to invasion by a set of viruses that inhabit the phloem. The evidence accumulated in the last 15 years greatly favors the idea that vine leaf curl is induced by a (or a complex of) long closterovirus (particle length from 1,400 to 2,200 nanometers). The winding of the vine leaf is transmitted primarily by contaminated shoots and rhizomes. However, under field conditions, several species of cocci have been shown to be the vector of leaf curl (Engelbrecht et al., "Transmission of Grapevine Leafroll Disease and Associated Closteroviruses by the Vine Mealybug Planococcus-ficus", Phytophylactica, 22: 341-346 (1990), Rosciglione et al., "Transmission of Grapevine Leafroll Disease and an Associated Closterovirus to Healthy Grapevine by the Mealybug Planococcus ficus" (Abstract), Phytoparasitica, 17: 63-63 (1989), and Tanne, "Evidence for the Transmission by Mealybugs to Healthy Grapevines of a Closter-like Particle Associated with Grapevine Leafroll Disease ", Phvtoparasitica, 16: 288 (1988)). The natural extension of leaf curl by insect vectors is rapid in different parts of the world. In New Zealand, observations from three vineyards showed that the number of infected vines almost doubled in a single year (Jordan et al., "Spread of Grapevine Leafroll and its Associated Virus in New Zealand Vineyards", llth Meeting of the International Council for the Study of Viruses and Viruses Diseases of the Grapevine, Montreux, Switzerland, pages 113-114 (1993)). A vineyard became infected 90 percent five years after GLRaV-3 was first observed. The prevalence of global leaf roll may increase as chemical control of the coconuts becomes more difficult, due to the lack of availability of effective insecticides. In view of the serious risk presented by vine leaf roll virus to vineyards, and the absence of an effective treatment for it, there continues to be a need to prevent this affliction. The present invention is directed to overcoming this deficiency in the art. SUMMARY OF THE INVENTION The present invention relates to an isolated protein or polypeptide corresponding to a protein or polypeptide of a vine leaf winding virus (Type 2). The RNA and DNA molecules of coding are also disclosed, either in isolation, or incorporated in an expression system, in a host cell, in a culture of the shoot or rhizomes of Vi tis or Ci trus transgénicos, or in a Nicotiana transgenic plant, or in a beet plant. Another aspect of the present invention relates to a method for imparting resistance to vine leaf winding virus (Type 2), to shoot cultures or Vitis rhizomes, or to Nicotiana plants, by transforming it with a molecule of DNA encoding the protein or polypeptide corresponding to a protein or polypeptide of a vine leaf winding virus (Type 2). Other aspects of the present invention relate to a method for imparting resistance to yellow beetle virus to beet plants, and a method for imparting resistance to the Tristeza virus, to the cultures of suckers or citrus rhizomes, both by transforming plants or cultures with a DNA molecule that encodes the protein or polypeptide corresponding to a protein or polypeptide of a vine leaf winding virus (Type 2). The present invention also relates to an antibody or binding portion thereof, or to a probe that recognizes the protein or polypeptide. Transgenic variants resistant to vine leaf winding virus of the present commercial grape crops and rhizomes, allow to have a more complete control of the virus, while retaining the characteristics of specific crop varieties. In addition, these variants allow controlling the GLRaV-2 transmitted by contaminated shoots or rhizomes, or by an insect vector currently not characterized. With respect to the last mode of transmission, the present invention circumvents the greater restriction of the use of pesticides that has made increasingly difficult the chemical control of the insect infeion. In this way, by means of the present invention, the interests of the environment and the economy of grape cultivation and wine making are followed. Brief Description of the Drawings Figures IA and IB are a comparison of a double stranded RNA (dsRNA) profile (Figure IA) of GLRaV-2 and its Northern hybridization assay (Figure IB). In Figure IA: Track M, DNA marker Hind III lambda; and lane 1, pattern of dsRNA in a 1 percent agarose gel stained with ethidium bromide. Figure IB is a Northern hybridization of the high molecular weight isolated dsRNA of GLRaV-2 with a probe prepared with the 32 P-labeled cDNA insert [a-dATP] from clone TC-1 of the GLRaV-2 specific cDNA. Lane 1, high molecular weight ARNds of GLRaV-2. Lane 2, total RNA extracted from healthy vines. Figure 2 shows the genome organization of GLRaV-2 and its sequencing strategy. The tables represent the open reading frames encoded by the deduced amino acid sequences of GLRaV-2; the numbered lines represent the nucleotide coordinates, starting from 5 '-terminal of the RNA in kilobases (kb). The lines below the GLRaV-2 RNA genome represent the cDNA clones used to determine the nucleotide sequences. Figures 3A-3D are comparisons between ORFla / ORFlb of GLRaV-2 and BYV. Figures 3A-3D show the conserved domains of two proteases of the papain type (P-PRO), methyltransferase (MT / MTR), helicase (HEL), and RNA polymerase dependent on the RNA (RdRP), respectively. The exclamation marks indicate the predicted catalytic residues of the leading papain type protease; the diagonals indicate the predicted dissociation sites. The conserved motifs of the MT, HEL and RdRP domains are highlighted with lines highlighted with the respective letters. The alignment is built using the MegAlign program in DNASTAR. Figures 4A and 4B are alignments of the nucleotide (Figure 4A) and deduced amino acid (Figure 4B) sequences of the ORFla / ORFlb overlapped region of GLRaV-2, BYV, BYSV and CTV. The nucleotides and identical amino acids are shown in consensus. The frame shift site of GLRaV-2 plus 1 (TAGC) and its corresponding sites of BYV (TAGC) and BYSV (TAGC) and CTV (CGGC) in the nucleotide and amino acid sequences are highlighted with underlining. Figure 5 is an alignment of the amino acid sequence of the HSP70 protein of GLRaV-2 and BYV. The conserved motifs (A to H) are indicated by bold lines with the respective letters. The alignment was conducted with the MegAlign program of DNASTAR. Figure 6A is a comparison with the coating protein (CP) and the duplication of the coat protein (CPd) of GLRaV-2 with other closteroviruses. The amino acid sequence of the CP and CPd of GLRaV-2 is aligned with the CP and the CPd of BYV, BYSV and CTV. The conserved amino acid residues are in bold letters, and the consensus sequences are indicated. The sequence alignment and the phylogenetic tree were constructed using the Clustal Method in the MegAlign Program of DNASTAR. Figure 6B is a tentative phylogenetic tree of the CP and CPd of GLRaV-2 with BYV, BYSV, CTV, LIYV, LChV and GLRaV-3. To facilitate alignment, only the C-terminal 250 amino acids of CP and CPd of LIYV, LChV and GLRaV-3 were used. The scale below the phylogenetic tree represents the distance between the sequences. Units indicate the number of substitution events. Figure 7 is a comparison of the genome organization of GLRaV-2, BYV, BYSV, CTV, LIYV, LChV and GLRaV-3. P-PRO, protease of the papain type; MT / MTR, methyltransferase; HEL, helicase; RdRP, RNA-dependent RNA polymerase; HSP70, heat-chogue protein 70; CP, coating protein; CPd, duplicate coating protein. Figure 8 is a tentative phylogenetic tree showing the RdRP ratio of GLRaV-2 with respect to BYV, BYSV, CTV and LIYV. The phylogenetic tree was constructed using the Clustal method with the MegAlign program in DNASTAR. Figure 9 is an alignment of the amino acid sequence of the HSP90 protein of GLRaV-2 with respect to other closteroviruses, BYS, BYSV and CTV. The most conserved motifs (I to II) are indicated with the highlighted lines, and are marked with the respective letters. Figure 10 is an alignment of the nucleotide sequence of the 3 '-terminal region of GLRaV-2 with respect to the BYV closteroviruses (Agranovsky et al., "Beet Yellows Closterovirus: Complete Genome Structure and Identification of a Papain-like Thiol Protease", Virology 198: 311-24 (1994), which is incorporated herein by reference) BYSV (Karasev et al., "Organization of the 3 '-Terminal Half of Beet Yellow Stunt Virus Genome and Implications for the Evolution of Closteroviruses', Virology 221: 199-207 (1996), which is incorporated herein by reference), and CTV (Karasev et al., "Complete Sequence of the Citrus Tristeza Virus RNA Genome ", Virology 208: 511-20 (1995), which is incorporated herein by reference). The consensus sequences are shown, and the distance to end 3 is indicated. A complementary region capable of forming a "hair pin" structure is underlined. Figures HA and 11B are genetic maps of the transformation vectors pGA482GG / EPT8CP-GLRaV-2 and pGA482G / EPT8CP-GLRaV-2, respectively. As shown in Figures HA and 11B, the expression cassette in plants (EPT8CP-GLRaV-2), which consists of a 35S enhancer of double cauliflower mosaic virus (CaMV), a 35S promoter of CaMV, a leader sequence 5 'of alfalfa mosaic virus RNA4 (ALMV), a GLRaV-2 coat protein gene (CP-GLRaV-2), and a 3' untranslated region of the CaMV 35S, was cloned into the vector of transformation by the EcoR I restriction site. The GLRaV-2 coat protein was cloned into the plant expression vector by the Neo I restriction site. Figure 12 is a reaction analysis in the polymerase chain of molecules of DNA extracted from the leaves of putative transgenic plants, using both the GLRaV-2 coat protein gene, and the specific primers of the NPT II gene. A gel stained with ethidium bromide shows an amplified DNA fragment of 720 base pairs for the NPT II gene, and a DNA fragment of 653 base pairs for the entire coding sequence of the coat protein gene. Track 1, DNA Marker F174 / Hae III; tracks 2-6, transgenic plants of different lines; lane 7, the positive control GLRaV-2 coat protein gene; and lane 8, the positive control NPT II gene. Figure 13 is a comparison of resistant transgenic Nicotiana benthamiana plants (the 3 plants on the right side) and susceptible plants (the 3 plants on the left side). Plants are shown 48 days after inoculation with GLRaV-2. Figure 14 is a Northern blot analysis of transgenic Nicotiana Benthamiana plants. An aliquot of 10 grams of the total RNA extracted from opposite transgenic plants was denatured and loaded on a 1 percent agarose gel containing formaldehyde. The separated RNAs were transferred to a Gene Screen Plus membrane, and hybridized with a 32 P-labeled DNA probe containing one third of the 3d coat protein gene sequence. Tracks 1, 3 and 4 represent non-control plants. transformed without RNA expression. The remaining tracks represent transgenic plants of different lines: lanes 2, 14-17, and 22-27 represent plants with a high level of RNA expression, which are susceptible to GLRaV-2; all other clues represent plants with an undetectable or low level of RNA expression, which are resistant to GLRaV-2. Detailed Description of the Invention The present invention relates to isolated DNA molecules that code for the proteins or polypeptides of a vine leaf winding virus (Type 2). A substantial portion of the genome of vine leaf winding virus (Type 2) ("GLRaV-2") has been sequenced. Within the genome there is a plurality of open reading frames ("ORFs"), and a 3 'nontranscribed region ("UTR"), each containing DNA molecules according to the present invention. The DNA molecule that constitutes a substantial portion of the GLRaV-2 genome comprises the nucleotide sequence corresponding to SEQ. ID. No .: 1 as follows: TAAACATTGC GAGAGAACCC CATTAGCGTC TCCGGGGTGA ACTTGGGAAG GTCTGCCGCC 60 GCTCAGGTTA TTTATTTCGG CAGTTTCACG CAGCCCTTCG CGTTGTATCC GCGCCAAGAG 120 AGCGCGATCG TAAAAACGCA ACTTCCACCG GTCAGTGTAG TGAAGGTGGfl GTGCGTAGCT 180 GCGGAGGTAG CTCCCGACAG GGGCGTGGTC GACAAGAAAC CTACGTCTGT TGGCGTTCCC 240 CCGCAGCGCG GTGTGCTTTC TTTTCCGACG GTGGTTCGGA ACCGCGGCGA CGTGAT? ATC 300 ACAGGGGTGG TGCATGAAGC CCTGAAGAAA ATTAAAGACG GGCTCTTACG CTTCCGCGT? 360 GGCGGTGACA TGCGTTTTTC GAGATTTTTC TCATCGAACT ACGGCTGCAG ATTCGTCGCG 420 AGCGTGCGTA CGAACACTAC AGTTTGGCTA AATTGCACGA AAGCGAGTGG TGAGAAATTC 480 TCACTCGCCG CCGCGTGCAC GGCGGATTAC GTGGCGATGC TGCGTTATGT GTGTGGCGGG 540 AAATTTCCAC TCGTCCTCAT GAGTAGAGTT ATTTACCCGG ATGGGCGCTG TTACTTGGCC 600 CATATGAGGT ATTTGTGCGC CTTTTACTGT CGCCCGTTTA GAGAGTCGGA TTATGCCCTC 660 GGAATGTGGC CTACGGTGGC GCGTCTCAGG GCATGCGTTG AGAAGAACTT CGGTGTCGAA 720 GCTTGTGGCA TAGCTCTTCG TGGCTATTAC ACCTCTCGCA ATGTTTATCA CTGTGATTAT 780 GACTCTGCTT ATGTAAAATA TTTTAGAAAC CTTTCCGGCC GCATTGGCGG TGGTTCGTTC 840 GATCCGACAT CTTTAACCTC CGTAATA? CG GTGAAGATTA GCGGTCTTCC AGGTGGTCTT 900 CCTAAAAATA TAGCGTTTGG TGCCTTCCTG TGCGATATAC GTTACGTCGA ACCGGTAGAC 960 TCGGGCGGCA TTCAATCGAG CGTTAAGACG AAACGTGAAG ATGCGCACCG AACCGTAGAG 1020 GAACGGGCGG CCGGCGGATC CGTCGAGCAA CCGCGACAAA AGAGGATAGA TGAGAAAGGT 1080 TGCGGCAGAG TTCCTAGTGG AGGTTTTTCG CATCTCCTGG TCGGCAACCT TAACGAAGTT 1140 AGGAGGAAGG TAGCTGCCGG ACTTCTACGC TTTCGCGTTG GCGGTGATAT GGATTTTCAT 1200 CGCTCGTTCT CCACCCAAGC GGGCCACCGC TTGCTGGTGT GGCGCCGCTC GAGCCGGAGC 1260 GTGTGCCTTG AACTTTACTC ACCATCTAAA AACTTTTTGC GTTACGATGT CTTGCCCTGT 1320 TCTGGAGACT ATGCAGCGAT GTTTTCTTTC GCGGCGGGCG GCCGTTTCCC TTTAGTTTTG 1380 ATGACTAGAA TTAGATACCC GAACGGGTTT TGTTACTTGG CTCACTGCCG GTACGCGTGC 1440 GCGTTTCTCT TAAGGGGTTT TGATCCGAAG CGTTTCGACA TCGGTGCTTT CCCCACCGCG 1500 GCCAAGCTCA GAAACCGTAT GGTTTCGGAG CTTGGTGAAA GAAGTTTAGG TTTGAACTTG 1560 TACGGCGCAT ATACGTCACG CGGCGTCTTT CACTGCGATT ATGACGCTAA GTTTATAAAG 1620 GATTTGCGTC TTATGTCAGC AGTTATAGCT GGAAAGGACG GGGTGGAAGA GGTGGTACCT 1680 TCTGACATAA CTCCTGCCAT GAAGCAGAAA ACGATCGAAG CCGTGTATGA TAGATTATAT 1740 GGCGGCACTG ACTCGTTGCT GAAACTGAGC ATCGAGAAAG ACTTAATCGA TTTCAAAAAT 1800 GACGTGCAGA GTTTGAAGAA AGATCGGCCG ATTGTCAAAG TGCCCTTTTA CATGTCGGAA 1860 GCAACACAGA ATTCGCTGAC GCGTTTCTAC CCTCAGTTCG AACTTAAGTT TTCGCACTCC 1920 TCGCATTCAG? TCATCCCGC CGCCGCCGCT TCTAG? CTGC TGG? A? TGA AACGTTAGTG 1980 CGCTTATGTG GTAATAGCGT TTCAGATATT GGAGGTTGTC CTCTTTTCCA TTTGCATTCC 2040 AAGACGCAAA GACGGGTTCA CGTATGTAGG CCTGTGTTGG ATGGCAAGGA TGCGC? GCGT 2100 CGCGTGGTGC GTGATTTGCA GTATTCCAAC GTGCGTTTGG GAGACGATGA TAAAATTTTG 2160 GAAGGGCCAC GCAATATCGA CATTTGCCAC TATCCTCTGG GCGCGTGTGA CCACGAAAGT 2220 AGTGCTATGA TGATGGTGCA GGTGTATGAC GCGTCCCTTT ATGAGA ATG TGGCGCCATG 2280 ATCAAGAAGA AAAGCCGCAT AACGTACTTA ACCATGGTCA CGCCCGGCGA GTTTCTTGAC 2340 GGACGCGAAT GCGTCTACAT GGAGTCGTTA GACTGTGAGA TTGAAGTTGA TGTGCACGCG 2400 GACGTCGTAA TGTACAAATT CGGTAGTTCT TGCTATTCGC ACAAGCTTTC AATCATCAAG 2460 GACATCATGA CCACTCCGTA CTTGACACTA GGTGGTTTTC TATTCAGCGT GGAGATGTAT 2520 GAGGTGCGTA TGGGCGTGAA TTACTTCAAG ATTACGAAGT CCGAAGTATC GCCTAGCATT 2580 AGCTGCACCA AGCTCCTGAG ATACCGAAGA GCTAATAGTG ACGTGGTTAA AGTTAAACTT 2640 CCACGTTTCG ATAAGAAACG TCGCATGTGT CTGCCTGGGT ATGACACCAT ATACCTAGAT 2700 TCGAAGTTTG TGAGTCGCGT TTTCGATTAT GTCGTGTGTA ATTGCTCTGC CGTGAACTCA 2760 AAAACTTTCG AGTGGGTGTG GAGTTTCATT AAGTCTAGTA AGTCGAGGGT GATTATTAGC 2820 GGTAAAATAA TTCACAAGGA TGTGAATTTG GACCTCAAGT ACGTCGAGAG TTTCGCCGCG 2880 GTTATGTTGG CCTCTGGCGT GCGCAGTAGA CTAGCGTCCG AGTACCTTGC TAAGAACCTT 2940 AGTCATTTTT CGGGAGATTG CTCCTTTATT GAAGCCACGT CTTTCGTGTT GCGTGAGAAA 3000 ATCAGAAACA TGACTCTGAA TTTTAACGAA AGACTTTTAC AGTTAGTGAA GCGCGTTGCC 3060 TTTGCGACCT TGGACGTGAG TTTTCTAGAT TTAGATTCAA CTCTTGAATC AATAACTGAT 3120 TTTGCCGAGT GTAAGGTAGC GATTGAACTC GACGAGTTGG GTTGCTTGAG AGCGGAGGCC 3180 GAGAATGAAA AAATCAGGAA TCTGGCGGGA GATTCGATTG CGGCTAAACT CGCGAGCGAG 3240 ATAGTGGTCG ATATTGACTC TAAGCCTTCA CCGAAGCAGG TGGGTAATTC GTCATCCGAA 3300 AACGCCGATA AGCGGGAAGT TCAGAGGCCC GGTTTGCGTG GTGGTTCTAG AAACGGGGTT 3360 GTTGGGGAGT TCCTTCACTT CGTCGTGGAT TCTGCCTTGC GTCTTTTCAA ATACGCGACG 3420 GATCAACAAC GGATCAAGTC TTACGTGCGT TTCTTGGACT CGGCGGTCTC ATTCTTGGAT 3480 TACAACTACG ATAATCTATC GTTTATACTG CGAGTGCTTT CGGAAGGTTA TTCGTGTATG 3540 TTCGCGTTTT TGGCGAATCG CGGCGACTTA TCTAGTCGTG TCCGTAGCGC GGTGTGTGCT 3600 GTGAAAGAAG TTGCTACCTC ATGCGCGAAC GCGAGCGTTT CTAAAGCCAA GGTTATGATT 3660 ACCTTCGCAG CGGCCGTGTG TGCTATGATG TTTAATAGCT GCGGTTTTTC AGGCGACGGT 3720 CGGGAGTATA AATCGTATAT ACATCGTTAC ACGCAAGTAT TGTTTGACAC TATCTTTTTT 3780 GAGGACAGCA GTTACCTACC CATAGAAGTT CTGAGTTCGG CGATATGCGG TGCTATCGTC 3840 ACACTTTTCT CCTCGGGCTC GTCCATAAGT TTAAACGCCT TCTTACTTCA AATTACCAAA 3900 GGATTCTCCC TAGAGGTTGT CGTCCGGAAT GTTGTGCGAG TCACGCATGG TTTGAGCACC 3960 ACAGCGACCG ACGGCGTCAT ACGTGGGGTT TTCTCCCAAA TTGTGTCTCA CTTACTTGTT 4 020 GGAAATACGG GTAATGTGGC TT? CCAGTCA GCTTTCATTG CCGGGGTGGT GCCTCTTTTA 4080 GTTAAAAAGT GTGTGAGCTT AATCTTCATC TTGCGTGAAG ATACTTATTC CGGTTTTATT 4 140 AAGCACGGAA TCAGTGAATT CTCTTTCCTT AGTAGTATTC TGAAGTTCTT GAAGGGTAAG 4200 CTTGTGGACG AGTTGAAATC GATTATTCAA GGGGTTTTTG ATTCCAACAA GCACGTGTTT 4260 AAAGAAGCTA CTCAGGAAGC GATTCGTACG ACGGTCATGC AAGTGCCTGT CGCTGTAGTG 4320 GATGCCCTTA AGAGCGCCGC GGGAAAAATT TATAACAATT TTACTAGTCG ACGTACCTTT 4380 GGTAAGGATG AAGGCTCCTC TAGCGACGGC GCATGTGAAG AGTATTTCTC ATGCGACGAA 4440 GGTGAAGGTC CGGGTCTGAA AGGGGGTTCC AGCTATGGCT TCTCAATTTT AGCGTTCTTT 4500 TCACGCATTA TGTGGGGAGC TCGTCGGCTT ATTGTTAAGG TGAAGCATGA GTGTTTTGGG 4 560 AAACTTTTTG AATTTCTATC GCTCAAGCTT CACGAATTCA GGACTCGCGT TTTTGGGAAG 4 620 AATAGAACGG ACGTGGGAGT TTACGATTTT TTGCCCACGG GCATCGTGGA AACGCTCTCA 4 680 TCGATAGAAG AGTGCGACCA AATTGAAGAA CTTCTCGGCG ACGACCTGAA AGGTGACAAG 4740 GATGCTTCGT TGACCGATAT GAATTACTTT GAGTTCTCAG AAGACTTCTT AGCCTCTATC 4800 GAGGAGCCGC CTTTCGCTGG ATTGCGAGGA GGTAGCAAGA ACATCGCGAT TTTGGCGATT 4860 TTGGAATACG CGCATAATTT GTTTCGCATT GTCGCAAGCA AGTGTTCGAA ACGACCTTTA 4920 TTTCTTGCTT TCGCCGAACT CTCAAGCGCC CTTATCGAGA AATTTAAGGA GGTTTTCCCT 4 980 CGTAAGAGCC AGCTCGTCGC TATCGTGCGC GAGTATACTC AGAGATTCCT CCGAAGTCGC 5040 ATGCGTGCGT TGGGTTTGAA TAACGAGTTC GTGGTAAAAT CTTTCGCCGA TTTGCTACCC 5100 GCATTAATGA AGCGGAAGGT TTCAGGTTCG TTCTTAGCTA GTGTTTATCG CCCACTTAGA 5160 GGTTTCTCAT ATATGTGTGT TTCAGCGGAG CGACGTGAAA AGTTTTTTGC TCTCGTGTGT 5220 TTAATCGGGT TAAGTCTCCC TTTCTTCGTG CGCATCGTAG GAGCGAAAGC GTGCGAAGAA 5280 CTCGTGTCCT CAGCGCGTCG CTTTTATGAG CGTATTAAAA TTTTTCTAAG GCAGAAGTAT 5340 GTCTCTCTTT CTAATTTCTT TTGTCACTTG TTTAGCTCTG ACGTTGATGA CAGTTCCGCA 5400 TCTGCAGGGT TGAAAGGTGG TGCGTCGCGA ATGACGCTCT TCCACCTTCT GGTTCGCCTT 5460 GCTAGTGCCC TCCTATCGTT AGGGTGGGAA GGGTTAAAGC TACTCTTATC GCACCACAAC 5520 TTGTTATTTT TGTGTTTTGC ATTGGTTGAC GATGTGAACG TCCTTATCAA AGTTCTTGGG 5580 GGTCTTTCTT TCTTTGTGCA ACCAATCTTT TCCTTGTTTG CGGCGATGCT TCTACAACCG 5640 GACAGGTTTG TGGAGTATTC CGAGAAACTT GTTACAGCGT TTGAATTTTT CTTAAAATGT 5700 TCGCCTCGCG CGCCTGCACT ACTCAAAGGG TTTTTTGAGT GCGTGGCGAA CAGCACTGTG 5760 TCAAAAACCG TTCGAAGACT TCTTCGCTGT TTCGTGAAGA TGCTCAAACT TCGAAAAGGG 5820 CGAGGGTTGC GTGCGGATGG TAGGGGTCTC CATCGGCAGA AAGCCGTACC CGTCATACCT 5880 TCTAATCGGG TCGTGACCGA CGGGGTTGAA AGACTTTCGG TAAAGATGCA AGGAGTTGAA 5940 GCGTTGCGTA CCGAATTGAG AATCTTAGAA GATTTAGATT CTGCCGTGAT CGAAAAACTC 6000 AATAGACGCA GAAATCGTGA CACTAATGAC GACGAATTTA CGCGCCCTGC TCATGAGCAG 6060 ATGCAAGAAG TCACCACTTT CTGTTCGAAA GCCAACTCTG CTGGTTTGGC CCTGGAAAGG 6120 GCAGT GCTTG TGGAAGACGC TATAAAGTCG GAGAAACTTT CTAAGACGGT TAATGAGATG 6180 GTGAGGAAAG GGAGTACCAC CAGCGAAGAA GTGGCCGTCG CTTTGTCGGA CGATGAAGCC 6240 GTGGAAGAAA TCTCTGTTGC TGACGAGCGA GACGATTCGC CTAAGACAGT CAGGATAAGC 6300 GAATACCTAA ATAGGTTAAA CTCAAGCTTC GAATTCCCGA AGCCTATTGT TGTGGACGAC 6360 AACAAGGATA CCGGGGGTCT AACGAACGCC GTGAGGGAGT TTTATTATAT GCAAGAACTT 6420 GCTCTTTTCG AAATCCACAG CAAACTGTGC ACCTACTACG ATCAACTGCG CATAGTCAAC 6480 TTCGATCGTT CCGTAGCACC ATGCAGCGAA GATGCTCAGC TGTACGTACG GAAGAACGGC 6540 • TCAACGATAG TGCAGGGTAA AGAGGTACGT TTGCACATTA AGGATTTCCA CGATCACGAT 6600 TTCCTGTTTG ACGGAAAAAT TTCTATTAAC AAGCGGCGGC GAGGCGGAAA TGTTTTATAT 6660 CACGACAACC TCGCGTTCTT GGCGAGTAAT TTGTTCTTAG CCGGCTACCC CTTTTCAAGG 6720 AGCTTCGTCT TCACGAATTC GTCGGTCGAT ATTCTCCTCT ACGAAGCTCC ACCCGGAGGT 6780 GGTAAGACGA CGACGCTGAT TGACTCGTTC TTGAAGGTCT TCAAGAAAGG TGAGGTTTCC 6840 ACCATGATCT TAACCGCCAA CAAAAGTTCG CAGGTTGAGA TCCTAAAGAA AGTGGAGAAG 6900 GAAGTGTCTA ACATTGAATG CCAGAAACGT AAAGACAAAA GATCTCCGAA AAAGAGCATT 6960 TACACCATCG ACGCTTATTT AATGCATCAC CGTGGTTGTG ATGCAGACGT TCTTTTCATC 7020 GATGAGTGTT TCATGGTTCA TGCGGGTAGC GTACTAGCTT GCATTGAGTT CACGAGGTGT 7080 CATAAAGTAA TGATCTTCGG GGATAGCCGG CAGATTCACT ACATTGAAAG GAACGAATTG 7140 GACAAGTGTT TGTATGGGGA TCTCGACAGG TTCGTGGACC TGCAGTGTCG GGTTTATGGT 7200 AATATTTCGT ACCGTTGTCC ATGGGATGTG TGCGCTTGGT TAAGCACAGT GTATGGCAAC 7260 CTAATCGCCA CCGTGAAGGG TGAAAGCGAA GGTAAGAGCA GCATGCGCAT TAACGAAATT 7320 AATTCAGTCG ACGATTTAGT CCCCGACGTG GGTTCCACGT TTCTGTGTAT GCTTCAGTCG 7380 GAGAAGTTGG AAATCAGCAA GCACTTTATT CGCAAGGGTT TGACTAAACT TAACGTTCTA 7440 ACGGTGCATG AGGCGCAAGG TGAGACGTAT GCGCGTGTGA ACCTTGTGCG ACTTAAGTTT 7500 CAGGAGGATG AACCCTTTAA ATCTA TCAGG CACATAACCG TCGCTCTTTC TCGTCACACC 7560 GACAGCTTAA CTTATAACGT CTTAGCTGCT CGTCGAGGTG ACGCCACTTG CGATGCCATC 7620 CAGAAGGCTG CGGAATTGGT GAACAAGTTT CGCGTTTTTC CTACATCTTT TGGTGGTAGT 7680 GTTATCAATC TCAACGTGAA GAAGGACGTG GAAGATAACA GTAGGTGCAA GGCTTCGTCG 7740 GCACCATTGA GCGTAATCAA CGACTTTTTG AACGAAGTTA ATCCCGGTAC TGCGGTGATT 7800 GATTTTGGTG ATTTGTCCGC GGACTTCAGT ACTGGGCCTT TTGAGTGCGG TGCCAGCGGT 7860 ATTGTGGTGC GGGACAACAT CTCCTCCAGC AAC? TCACTG ATCACGATAA GCAGCGTGTT 7920 TAGCGTAGTT CGGTCGCAGG CGATTCCGCG TAGAAAACCT TCTCTACAAG AAAATTTGTA 7980 TTCGTTTGAA GCGCGGAATT ATAACTTCTC GACTTGCGAC CGTAACACAT CTGCTTCAAT 8040 GTTCGGAGAG GCTATGGCGA TGAACTGTCT TCGTCGTTGC TTCGACCTAG ATGCCTTTTC 8100 GTCCCTGCGT GATGATGTGA TTAGTATCAC ACGTTCAGGC ATCGAACAAT GGCTGGAGAA 8160 ACGTACTCCT AGTCAGATTA AAGCATTAAT GAAGGATGTT GAATCGCCTT TGGAAATTGA 8220 CGATGAAATT TGTCGTTTTA AGTTGATGGT GAAGCGTGAC GCTAAGGTGA AGTTAGACTC 8280 TTCTTGTTTA ACTAAACACA GCGCCGCTCA AAATATCATG TTTCATCGCA AGAGCATTAA 8340 TGCTATCTTC TCTCCTATCT TTAATGAGGT GAAAAACCGA ATAATGTGCT GTCTTAAGCC 8400 TAACATAAAG TTTTTTACGG AGATGACTAA CAGGGATTTT GCTTCTGTTG TCAGCAACAT 8460 GCTTGGTGAC GACGATGTGT ACCATATAGG TGAAGTTGAT TTCTCAAAGT ACGACAAGTC 8520 TCAAGATGCT TTCGTGAAGG CTTTTGAAGA AGTAATGTAT AAGGAACTCG GTGTTGATGA 8580 AGAGTTGCTG GCTATCTGGA TGTGCGGCGA GCGGTTATCG ATAGCTAACA CTCTCGATGG 8640 TCAGTTGTCC TTCACGATCG AGAATCAAAG GAAGTCGGGA GCTTCGAACA CTTGGATTGG 8700 TAACTCTCTC GTCACTTTGG GTATTTTAAG TCTTTACTAC GACGTTAGAA ATTTCGAGGC 8760 GTTGTACATC TCGGGCGATG ATTCTTTAAT TTTTTCTCGC AGCGAGATTT CGAATTATGC 8820 CGACGACATA TGCACTGACA TGGGTTTTGA GACAAAATTT ATGTCCCCAA GTGTCCCGTA 8880 CTTTTGTTCT AAATTTGTTG TTATGTGTGG TCATAAGACG TTTTTTGTTC CCGACCCGTA 8940 CAAGCT TTTT GTCAAGTTGG GAGCAGTCAA AGAGGATGTT TCAATGGATT TCCTTTTCGA 9000 GACTTTTACC TCCTTTAAAG ACTTAACCTC CGATTTTAAC GACGAGCGCT TAATTCAAAA 9060 GCTCGCTGAA CTTGTGGCTT TAAAATATGA GGTTCAAACC GGCAACACCA CCTTGGCGTT 9120 AAGTGTGATA CATTGTTTGC GTTCGAATTT CCTCTCGTTT AGCAAGTTAT ATCCTCGCGT 9180 GAAGGGATGG CAGGTTTTTT ACACGTCGGT TAAGAAAGCG CTTCTCAAGA GTGGGTGTTC 9240 TCTCTTCGAC AGTTTCATGA CCCCTTTTGG TCAGGCTGTC ATGGTTTGGG ATGATGAGTA 9300 GCGCTAACTT GTGCGCAGTT TCTTTGTTCG TGACATACAC CTTGTGTGTC ACCGTGCGTT 9360 TATAATGAAT CAGGTTTTGC AGTTTGAATG TTTGTTTCTG CTGAATCTCG CGGTTTTTGC 9420 TGTGACTTTC ATTTTCATTC TTCTGGTCTT CCGCGTG? TT AAGTCTTTTC GCCAGAAGGG 9480 TCACGAAGCA CCTGTTCCCG TTGTTCGTGG CGGGGGTTTT TCAACCGTAG TGTAGTCAAA 9540 AGACGCGCAT ATGGTAGTTT TCGGTTTGGA CTTTGGCACC ACATTCTCTA CGGTGTGTGT 9600 GTACAAGGAT GGACGAGTTT TTTCATTCAA GCAGAATAAT TCGGCGTACA TCCCCACTTA 9660 CCTCTATCTC TTCTCCGATT CTAACCACAT GACTTTTGGT TACGAGGCCG AATCACTGAT 9720 GAGTAATCTG AAAGTTAAAG GTTCGTTTTA TAGAGATTTA AAACGTTGGG TGGGTTGCGA 9780 TTCGAGTAAC C TCGACGCGT ACCTTGACCG TTTAAAACCT CATTACTCGG TCCGCTTGGT 9840 TAAGATCGGC TCTGGCTTGA ACGAAACTGT TTCAATTGGA AACTTCGGGG GCACTGTTAA 9900 GTCTGAGGCT CATCTGCCAG GGTTGATAGC TCTCTTTATT AAGGCTGTCA TTAGTTGCGC 9960 GGAGGGCGCG TTTGCGTGCA CTTGCACCGG GGTTATTTGT TCAGTACCTG CCAATTATGA 10020 TAGCGTTCAA AGGAATTTCA CTGATCAGTG TGTTTCACTC AGCGGTTATC AGTGCGTATA 10080 TATGATCAAT GAACCTTCAG CGGCTGCGCT ATCTGCGTGT AATTCGATTG GAAAGAAGTC 10140 CGCAAATTTG GCTGTTTACG ATTTCGGTGG TGGGACCTTC GACGTGTCTA TCATTTCATA 10200 CCGCAACAAT ACTTTTGTTG TGCGAGCTTC TGGAGGCGAT CTAAATCTCG GTGGAAGGGA 10260 TGTTGATCGT GCGTTTCTCA CGCACCTCTT CTCTTTAACA TCGCTGGAAC CTGACCTCAC 10320 TTTGGATATC TCGAATCTGA AAGAATCTTT ATCAAAAACG GACGCAGAGA TAGTTTACAC 10380 TTTGAGAGGT GTCGATGGAA GAAAAGAAGA CGTTAGAGTA AACAAAAACA TTCTTACGTC 10440 GGTGATGCTC CCCTACGTGA ACAGAACGCT TAAGATATTA GAGTCAACCT TAAAATCGTA 10500 TGCTAAGAGT ATGAATGAGA GTGCGCGAGT TAAGTGCGAT TTAGTGCTGA TAGGAGGATC 10560 TTCATATCTT CCTGGCCTGG CAGACGTACT AACGAAGCAT CAGAGCGTTG ATCGTATCTT 10620 AAGAGTT TCG GATCCTCGGG CTGCCGTGGC CGTCGGTTGC GCATTATATT CTTCATGCCT 10680 CTCAGGATCT GGGGGGTTGC TACTGATCGA CTGTGCAGCT CACACTGTCG CTATAGCGGA 10740 CAGAAGTTGT CATCAAATCA TTTGCGCTCC AGCGGGGGCA CCGATCCCCT TTTCAGGAAG 10800 CATGCCTTTG TACTTAGCCA GGGTCAACAA GAACTCGCAG CGTGAAGTCG CCGTGTTTGA 10860 AGGGGAGTAC GTTAAGTGCC CTAAGAACAG AAAGATCTGT GG? GCAAATA TAAGATTTTT 10920 TGATATAGGA GTGACGGGTG ATTCGTACGC ACCCGTTACC TTCTATATGG ATTTCTCCAT 10980 TTCAAGCGTA GGAGCCGTTT CATTCGTGGT GAGAGGTCCT GAGGGTA? GC A? GTGTCACT 11040 CACTGGAACT CCAGCGTATA ACTTTTCGTC TGTGGCTCTC GGATCACGCA GTGTCCGAGA 11100 ATTGCATATT AGTTTAAATA ATAAAGTTTT TCTCGGTTTG CTTCTACATA GAAAGGCGGA 11160 TCGACGAATA CTTTTCACTA AGGATGAAGC GATTCGATAC GCCGATTCAA TTGATATCGC 11220 GGATGTGCTA AAGGAATATA AAAGTTACGC GGCCAGTGCC TTACCACCAG ACGAGGATGT 11280 CGAATTACTC CTGGGAAAGT CTGTTCAAAA AGTTTTACGG GGAAGCAGAC TGGAAGAAAT 11340 ACCTCTCTAG GAGCATAGCA GCACACTCAA GTGAAATTAA AACTCTACCA GACATTCGAT 11400 TGTACGGCGG TAGGGTTGTA AAGA ? GTCCG AATTCGAATC AGCACTTCCT AATTCTTTTG 1146 0AGGACTGTTC ATACTGAGCG AACGGGAAGT GGGATGGAGC AAATTATGCG 11520 GAATAACGGT GGAAGAAGCA GCATACGATC TTACGAATCC CAAGGCTTAT AAATTCACTG 11580 CCGAGACATG TAGCCCGGAT GTAAAAGGTG AAGGACAAAA ATACTCTATG GAAGACGTGA 11640 TGAATTTCAT GCGTTTATCA AATCTGGATG TTAACGACAA GATGCTGACG GAACAGTGTT 11700 GGTCGCTGTC CAATTCATGC GGTGAATTGA TCAACCCAGA CGACAAAGGG CGATTCGTGG 11760 CTCTCACCTT TAAGGACAGA GACACAGCTG ATGACACGGG TGCCGCCAAC GTGGAATGTC 11820 GCGTGGGCGA CTATCTAGTT TACGCTATGT CCCTGTTTGA GCAGAGGACC CAAAAATCGC 11880 AGTCTGGCAA CATCTCTCTG TACGAAAAGT ACTGTGAATA CATCAGGACC TACTTAGGGA 11940 GTACAGACCT GTTCTTCACA GCGCCGGACA GGATTCCGTT ACTTACGGGC ATCCTATACG 12000 ATTTTTGTAA GGAATACAAC GTTTTCTACT CGTCATATAA GAGAAACGTC GATAATTTCA 12060 GATTCTTCTT GGCGAATTAT ATGCCTTTGA TATCTGACGT CTTTGTCTTC CAGTGGGTAA 12120 AACCCGCGCC GGATGTTCGG CTGCTTTTTG AGTTAAGTGC AGCGGAACTA ACGCTGGAGG. 12180 TTCCCACACT GAGTTTGATA GATTCTCAAG TTGTGGTAGG TCATATCTTA AGATACGTAG_12240_AATCCTACAC ATCAGATCCA GCCATCGACG CGTTAGAAGA CAAACTGGAA GCGATACTGA 12300 AAAGTAGCAA TCCCCGTCTA TCGACAGCGC AACTATGGGT TGGTTTCTTT TGTTACTATG 12360 GTGAGTTTCG TACGGCTCAA AGTAGAGTAG TGCAAAGACC AGGCGTATAC AAAACACCTG 12420 ACTCAGTGGG TGGATTTGAA ATAAACATGA AAGATGTTGA GAAATTCTTC GATAAACTTC 12480 AGAGAGAATT GCCTAATGTA TCTTTGCGGC GTCAGTTTAA CGGAGCTAGA GCGCATGAGG 12540 CTTTCAAAAT ATTTAAAAAC GGAAATATAA GTTTCAGACC TATATCGCGT TTAAACGTGC 12600 CTAGAGAGTT CTGGTATCTG AACATAGACT ACTTCAGGCA CGCGAATAGG TCCGGGTTAA 12660 CCGAAGAAGA AATACTCATC CTAAACAACA TAAGCGTTGA TGTTAGGAAG TTATGCGCTG 12720CAATACCCTA CCTAGCGCGA AGCGCTTTAG TAAAAATCAT AAGAGTAATA 12780 TACAATCATC ACGCCAAGAG CGGAGGATTA AAGACCCATT GGTAGTCCTG AAAGACACTT 128 0 TATATGAGTT CCAACACAAG CGTGCCGGTT GGGGGTCTCG AAGCACTCGA G? CCTCGGGA 12900 GTCGTGCTGA CCACGCGAAA GGAAGCGGTT GATAAGTTTT TTA? TGAACT A? AAAACGAA 12960 AATTACTCAT CAGTTGACAG CAGCCGATTA AGCGATTCGG AAGTAAAAGA AGTGTTAGAG 13020 AAAAGTAAAG AAAGTTTCAA AAGCGAACTG GCCTCCACTG ACGAGCACTT CGTCTACC? C 13080 ATTATATTTT TCTTAATCCG ATGTGCTAAG ATATCGACAA GTGAAAAGGT GAAGTACGTT 13140 GGTAGTCATA CGTACGTGGT CGACGGAAAA ACGTACACCG TTCTTGACGC TTGGGTATTC 13200 AACATGATGA AAAGTCTCAC GAAGAAGTAC AAACGAGTGA ATGGTCTGCG TGCGTTCTGT 13260 TGCGCGTGCG AAGATCTATA TCTAACCGTC GCACC ?? TAA TGTCAGAACG CTTTAAGACT 13320 AAAGCCGTAG GGATGAAAGG TTTGCCTGTT GGAAAGGAAT ACTTAGGCGC CGACTTTCTT 13380 TCGGGAACTA GCAAACTGAT GAGCGATCAC GACAGGGCGG TCTCCATCGT TGCAGCGAAA 134 4 0 AACGCTGTCG ATCGTAGCGC TTTCACGGGT GGGGAGAGAA AGATAGTTAG TTTGTATGAT 13500 CTAGGGAGGT ACTAAGCACG GTGTGCTATA GTGCGTGCTA TAATAATAAA CACTAGTGCT 13560 TAAGTCGCGC AGAAGAAAAC GCTATGGAGT TGATGTCCGA CAGCAACCTT AGCAACCTGG 13620 TGATAACCGA CGCCTCTAGT CTAAATGGTG TCGACAAGAA GCTTTTATCT GCTGAAGTTG 13680 AAAAAATGTT GGTGCAGAAA GGGGCTCCTA ACGAGGGTAT AGAAGTGGTG TTCGGTCT? C 13740 TCCTTTACGC ACTCGCGGCA AGAACCACGT CTCCTAAGGT TCAGCGCGCA GATTCAGACG 13800 TTATATTTTC AAATAGTTTC GGAGAGAGGA ATGTGGTAGT AACAGAGGGT GACCTTAAGA 13860 AGGTACTCGA CGGGTGTGCG CCTCTCACTA GGTTCACTAA TAAACTTAGA ACGTTCGGTC 13920 GTACTTTCAC TGAGGCTTAC GTTGACTTTT GTATCGCGTA TAAGCACAAA TTACCCCAAC 13980 TCAACGCCGC GGCGGAATTG GGGATTCCAG CTGAAGATTC GTACTTAGCT GCAGATTTTC 14040 TGGGTACTTG CCCGAAGCTC TCTGAATTAC AGCAAAGTAG GAAGATGTTC GCGAGTATGT 1 100 ACGCTCTAAA AACTGAAGGT GGAGTGGTAA ATACACCAGT GAGCAATCTG CGTCAGCTAG_14160_GTAGAAGGGA AGTTATGTAA TGGAAGATTA CGAAGAAAAA TCCGAATCGC TCATACTGCT 14220 ACGCACGAAT CTGAACACTA TGCTTTTAGT GGTCAAGTCC GATGCTAGTG TAGAGCTGCC 14280 TAAACTACTA ATTTGCGGTT ACTTACGAGT GTCAGGACGT GGGGAGGTGA CGTGTTGCAA 14340 CCGTGAGGAA TTAACAAGAG ATTTTGAGGG CAATCATCAT ACGGTGATCC GTTCTAGAAT 14400 CATACAATAT GACAGCGAGT CTGCTTTTGA GGAATTCAAC AACTCTGATT GCGTAGTGAA 144 60 GTTTTTTCCTA GAGACTGGTA GTGTCTTTTG GTTTTTTCCTT CGAAGTGAAA CCAAAGGTAG_14520_? GCGGTGCG? CATTTGCGC? CCTTCTTCGA? GCT? AC ?? T TTCTTCTTTG G? TCGC? TTG 14580 CGGT? CC? TG GAGT? TTGTT TGAAGCAGGT ACTAACTGAA? CTG ?? TCTA T ?? TCG? TTC 14640 TTTTTGGGAGA GA ?? GAA? TC GTT? AGATGA GGGTT? TAGT GTCTCCTT? TG? AGCTG? AG 14700 ACATTCTGAA AAG? TCG? CT G? C? TGTTAC GAAAC? TAGA CAGTGGGGTC TTG? GC? CT? 14760 AAGAATGT? T C? AGGCATTC TCG? CGATAA CGCG? GACCT ACATTGTGCG A? GGCTTCCT 14820? CCAGTGGG? TGTTGACACT GGGTTATATC AGCGT ?? TTG CGCTGAAAAA CGT? TAATTG 14880 ACACGGTGGA GTC? AACATA CGGTTGGCTC A? CCTCTCGT GCGTG? AAAA GTGGCGGTTC 14940? TTTTTGT ?? GGATGAACCA AAAGAGCT? G T? GCATTC? T C? CGCGAAAG TACGTGGA? C 15000 TCACGGGCGT GGG? GTG? GA G? AGCGGTG? ? GAGGGAAAT GCGCTCTCTT? CC ??? ACAG 15060 TTTTAAATAA A? TGTCTTTG GAAATGGCGT TTTACATGTC ACC? CGAGCG TGG? A? ACG 15120 CTGAATGGTT AGAACT? AAA TTTTCACCTG TGA? AATCTT TAGAGATCTG CT? TT? G? CG 15180 TGGAAACGCT C? CGAATTG TGCGCCGA? G ATG? TGTTCA CGTCGAC? AA GTAAATGAG? 15240 ATGGGGACG? AAATCACGAC CTCGAACTCC AAGACGAATG TTAAAC? TTG GTTAAGTTTA 15300 ACG? AA? TGA TTAGT? A? TA AT ??? TCGA? CGTGGGTGT? TCTACCTG? C GT? TC? ACTT 15360 AAGCTGTTAC TGAGTAATTA A? CCAACAAG TGTTGGTGTA ATGTGTATGT TGATGTAGAG 15420 AAAAATCCGT TTGTAGA? CG GTGTTTTTCT CTTCTTTATT TTTAAAAAAA AAATAAA? AA 15480 AAAAAAAAAA AAGCGGCCCCC 15500 Another DNA molecule of the present invention (GLRaV-2 ORFla) includes nucleotides 4-7923 of SEQ. ID. DO NOT. 1 and is believed to encode a large polyprotein of the vine leaf roll virus containing the conserved domains characteristic of two papain-like proteases, a methyltransferase, and a helicase. This DNA molecule comprises the nucleotide sequence corresponding to SEQ. ID. DO NOT. 2, as follows: ACT ACATTGCGAG AGAACCCCAT TAGCGTCTCC GGGGTG TGGGAAGGTC TGCCGCCGCT 60 CAG6TTATTT ATTTCGGCAG TTTCACGCAG CCCTTCGCGT TGTATCCGCG CCAAG GAGC 120 GCGATCGTAA AAACGCAACT TCCACCGGTC AGTGT GTGA AGGTGGAGTG CGTAGCTGCG 180 G GGTAGCTC CCG C AG GGGG CGTGGTCG C ?? ACCTA CGTCTGTTGG CGTTCCCCCG??????? 2 0 CAGCGCGGTG TGCTTTCTTT TCCGACGGTG GTTCGGAACC GCGGCG? CGT GATAATCACA 300 GGGGTGGTGC? TGA? GCCCT GAAGA? TAs AAAG? CGGGC TCTTACGCTT CCGCGT? GGC 360 GGTGACATGC GTTTTTCGAG ATTTTTCTCA TCGAACTACG GCTGCAGATT CGTCGCGAGC 420 GTGCGTACGA ACACTACAGT TTGGCTAAAT TGCACGAAAG CGAGTGGTGA GAAATTCTCA 480 CTCGCCGCCG CGTGCACGGC GG? TT? GSEE GCGATGCTGC GTT ? TGTGTG TGGCGGG ??? 540 TTTCCACTCG TCCTCATGAG TAG? GTTATT T? CCCGGATG GGCGCTGTT? CTTGGCCC? T 600 ? TGAGGT? TT TGTGCGCCTT TT? CTGTCGC CCGTTT? G? G AG-rCGGATI? TGCCC1CGG? 660 ATGTGGCCTA CGGTGGCGCG TCTCAGGGCA TGCGTTG? GA AG ?? CTTCGG TGTCGA? GCT 720 TGTGGCATAG CTCTTCGTGG CT? TT? C? CC TCTCGCA? TG TTT? TC? CTG TG? TT? TGAC 780 TCTGCTT? TG T ???? TATTT TAGAAACCTT TCCGGCCGC? TTGGCGGTGG TTCGTTCG? T 840 CCGACATCTT TAACCTCCGT AATA? CGGTG ?? GATTAGCG GTC11CCAGG TGGTCTTCCT 900 AAAAAT? TAG CGTTTGGTGC CTTCCTGTGC G? T? TACGTT ACGTCGAACC GGT? G? CTCG 960 GGCGGC? TTC A? TCG? GCGT T? GACGAAA CGTG ?? G? TG CGC? CCGA? C CGTAG? GG ?? 1020 CGGGCGGCCG GCGGATCCGT CG? GC? CCG CG? C ?? AAGA GGATAGATGA G ??? GGTTGC 1080 GGC? G? GTTC CT? GTGGAGG TTTTTCGCAT CTCCTGGTCG GC? ACCTT ?? CG? AGTT? GG 11 0 ? GG? AGGTAG CTGCCGG? CT TCT? CGCTTT CGCGTTGGCG GTGATATGGA TTTTCATCGC 1200 TCGTTCTCCA CCC ?? GCGGG CCACCGCTTG CTGGTGTGGC GCCGCTCGAG CCGGAGCGTG 1260 TGCCTTG? AC TTT? CTCACC? TCTA? A ?? C TTTTTGCGTT? CGATGTCTT GCCCTGTTCT 1320 GGAG? CTATG C? GCG? TGTT TTCTTTCGCG GCGGGCGGCC GTTTCCCTTT? GTTTTGATG 1380 ? CTAG ?? TTA GATACCCGAA CGGGTTTTGT TACTTGGCTC? CTGCCGGT? CGCGTGCGCG 1140 TTTCTCTTAA GGGGTTTTGA TCCG? GCGT TTCG? CATCG GTGCTTTCCC CACCGCGGCC 1500 ? AGCTC? G ?? ACCGT? TGGT TTCGG? GCTT GGTG ??? G ?? GTTT? GGTTT G ?? CTTGTAC 1560 GGCGCAT? TA CGTC? CGCGG CGTCTTTCAC TGCGATTATG? CGCTAAGTT TAT ??? GGAT 1620 TTGCGTCTTA TOTCAGCAGT TAT? GCTGGA ?? GG? CGGGG TGG? AG? GGT GGT? CCTTCT 1680 GACATAACTC CTGCC? TGAA GCAGAAAACG ATCG? AGCCG TGT? TGATAG? TTATATGGC 1740 GGCACTGACT CGTTGCTGA? ACTGAGCATC G? GAA? GACT TAATCGATTT C? A ?? ATGAC 1800 GTGCAG? GTT IG ?? G ??? GA? CGGCCGATT GTC ??? GTGC CCTTTT? CAT GTCGGA? GCA 1860 ACACAGAATT CGCTGACGCG TTTCT? CCCT CAGTTCG? AC TT ?? GTTTTC GC? CTCCTCG 1920 «MTCAG? TC ATCCCGCCGC CGCCGCTTCT? GACTGCTGG AA ?? TGAAAC GTTAGTGCGC 1980 TTATGTGGTA ATAGCGTTTC? GAT? TTGGA GGTTGTCCTC TTTTCC? TTT GCATTCC ?? G 2040 ACGCAAAGAC GGGTTCACGT ATGTAGGCCT GTGTTGG? TG GC? AGGATGC GCAGCGICGC 2100 GTGGTGCGTG ATTTGC? GT? TTCt ^ l? CGTß CGTTTGGGAG ACGATG? TAA? ATTTTGGAA 2160 GGGCCACGCA ATATCG? CAT TTGCC? CTAT CCTCTGGGCG CGTGTGACC? CGAA? GTAGT 2220 GCTATGATG? TGGTGCAGGT GTATGACGCG TCCCTTTATG? G? TATGTGG CGCC? TG? TC 2280 ?? G ?? GAAAA GCCGCAT ?? C GT? CTT? ACC? TGGTCACGC CCGGCGAGTT TCTTG? CGG? 2340 CGCGA? TGCG TCTACATGG? GTCGTTAG? C TGTG? GATTG? GTTG? TGT GCACGCGG? C 2400 GTCGTAATGT? C? A? TTCGG T? GTTCTTGC T? TTCGCACA? GCTTTCA? T C? TCA? GG? C 2460 ? TCATGACCA CTCCGTACTT G? CACT? GGT GGTTTTCT? T TC? GCGTGG? GATGTATGAG 2520 GTGCGT? TGG GCGTG ?? TTA CTTC ?? G? TT ACGAAGTCCG A? GTATCGCC TAGC? TT? GC 2580 TGC? CCAAGC TCCTG? GATA CCGAAGAGCT? ATAGTG? CG TGGTTAAAGT T ??? CTTCC? 2640 CGTTTCGAT? ? GA? ACGTCG CATGTGTCTG CCTGGGTATG ACACCAT? T? CCT? GATTCG 2700 ?? GTTTGTG? ' GTCGCGTTTT CGATTATGTC GTGTGTA? TT GCTCTGCCGT G ?? CTC? A ?? 2760 ? CTTTCG? GT GGGTGTGG? G TTTC? TT ?? G TCT? GTA? GT CG? GGGTG? T? TT? GCGGT 2820 AAAATA? TTC AC? AGGATGT GA? TTTGG? CTC? GT? CG TCG? G? GTTT CGCCGCGGTT 2800 ATGTTGGCCT CTGGCGTGCG C? GTAG? CT? GCGTCCGAGT? CCTTGCTAA G? ACCTIAGT 2940 C? TTTTTCGG GAGATTGCTC CTTT? TTGA? GCCACGTCTT TCGTGTTGCG TG? G? AAATC 3000 AOAA? C? TG? CTCTG ?? TTT T? ACG ??? G? CTTTTAC? GT TAGTGAAGCG CGTTGCCTTT 3060 GCG? CCTTGG? CGTGAGTTT TCT? G? TTTA GATTCAACTC TTGAATC ?? T AACTGATTTT 3120 GCCGAGTGTA AGGTAGCGAT TG? ACTCG? C G? GTTGGGTT GCTTG? GAGC GGAGGCCGAG 3180 AATGAA? A ?? TC? GGA? TCT GGCGGG? G? T TCG? TTGCGG CTAAACTCGC G? GCGAGAT? 3240 GTGGTCGATA TTGACTCTAA GCCTTCACCG? AGCAGGTGG GTAATTCGTC? TCCGAA? AC 3300 GCCG? TAAGC GGGAAGTTCA G? GGCCCGGT TTGCGTGGTG GTTCTAG ??? CGGGGTTGTT 3360 GGGGAGTTCC TTCACTTCGT CGTGGATTCT GCCTTGCGTC TTTTCAAATA CGCG? CGGAT 3420 C? CA? CGGA TC? AGTCTTA CGTGCGTTTC TTGGACTCGG CGGTCTCATT CTTGG? TTAC 3480 AACT? CG? TA ATCTATCGTT TATACTGCG? GTGCTTTCGG AAGGTT? TTC GTGT? TGTTC 3540 -33- TTGCGTACCG AATTGAGAAT CTTAGAAGAT TTAGATTCTG CCGTGATCGA AAAACTCAAT 6000 AGACGCAGAA ATCGTGACAC TAATGACGAC GAATTTACGC GCCCTGCTCA TGAGCAGATG 6060 CAAGAAGTCA CCACTTTCTG TTCGAAAGCC AACTCTGCTG GTTTGGCCCT GGAAAGGGCA 6120 GTGCTTGTGG AAGACGCTAT AAAGTCGGAG AAACTTTCTA AGACGGTT? A TG? GATGGTG 6180 AGGAAAGGGA GTACCACCAG CGAAGAAGTG GCCGTCGCTT TGTCGGACGA TGAAGCCGTG 6240CTGTTGCTGA CGAGCGAGAC GATTCGCCTA AGACAGTCAG GATAAGCGAA 6300 TACCTAAATA GGTTAAACTC AAGCTTCGAA TTCCCGAAGC CTATTGTTGT GGACGACAAC 6360 AAGGATACCG GGGGTCTAAC GAACGCCGTG AGGGAGTTTT ATTAT? TGCA AGAACTTGCT 6420 CTTTTCGAAA TCCACAGCAA ACTGTGCACC TACTACGATC AACTGCGCAT AGTCAACTTC 6480 GATCGTTCCG TAGCACCATG CAGCGAAGAT GCTCAGCTGT ACGTACGGAA GAACGGCTC? 6540 ACGATAGTGC AGGGTAAAGA GGTACGTTTG CAC? TTAAGG ATTTCCACGA TCACGATTTC 6600 CTGTTTGACG GAAAAATTTC TATTAACAAG CGGCGGCGAG GCGGAAATGT TTTATATCAC 6660 GACAACCTCG CGTTCTTGGC GAGTAATTTG TTCTTAGCCG GCTACCCCTT TTCAAGGAGC 6720 TTCGTCTTCA CGAATTCGTC GGTCGATATT CTCCTCTACG AAGCTCCACC CGGAGGTGGT 6780 AAGACGACGA CGCTGATTGA CTCGTTCTTG AAGGTCTTCA AGAAAGGTGA GGTTTCCACC 6840 ATGATCTTAA CCGCCAACAA AAGTTCGCAG GTTGAGATCC TAAAGAAAGT GGAGAAGGAA 6900 GTGTCTAACA TTGAATGCCA GAAACGTAAA GACAAAAGAT CTCCGAAAAA GAGCATTTAC 6960 ACCATCGACG CTTATTTAAT GCATCACCGT GGTTGTGATG CAGACGTTCT TTTCATCGAT 7020 GAGTGTTTCA TGGTTCATGC GGGTAGCGTA CTAGCTTGCA TTGAGTTCAC GAGGTGTCAT 7080 AAAGTAATGA TCTTCGGGGA TAGCCGGCAG ATTCACTACA TTGAAAGGAA CGAATTGGAC 7140 AAGTGTTTGT ATGGGGATCT CGACAGGTTC GTGGACCTGC AGTGTCGGGT TTATGGTAAT 7200 ATTTCGTACC GTTGTCCATG GGATGTGTGC GCTTGGTTAA GCACAGTGTA TGGCAACCTA 7260 ATCGCCACCG TGAAGGGTGA AAGCGAAGGT AAGAGCAGCA TGCGCATTAA CGAAATTAAT 7320 TCAGTCGACG ATTTAGTCCC CGACGTGGGT TCCACGTTTC TGTGTATGCT TCAGTCGGAG 7380 AAGTTGGAAA TCAGCAAGCA CTTTATTCGC AAGGGTTTGA CTAAACTTAA CGTTCTAACG 7440 GTGCATGAGG CGCAAGGTGA GACGTATGCG CGTGTGAACC TTGTGCGACT TAAGTTTCAG 7500 GAGGATGAAC CCTTTAAATC TATCAGGCAC ATAACCGTCG CTCTTTCTCG TCACACCGAC 7560 AGCTTAACTT ATAACGTCTT AGCTGCTCGT CGAGGTGACG CCACTTGCGA TGCCATCCAG 7620 AAGGCTGCGG AATTGGTGAA CAAGTTTCGC GTTTTTTCCTA CATCTTTTGG TGGTAGTGTT 7680 ATCAATCTCA ACGTGAAGAA GGACGTGGAA GATAACAGTA GGTGCAAGGC TTCGTCGGCA 7740 CCATTGAGCG TAATCAACGA CTTTTTGAAC GAAGTTAATC CCGGTACTGC GGTGATTGAT 7800 TTTGGTGATT TGTCCGCGGA CTTCAGTACT GGGCCTTTTG AGTGCGGTGC CAGCGGTATT 7860 GTGGTGCGGG ACAACATCTC CTCCAGCAAC ATCACTGATC ACGATAAGCA GCGTGTTTAG_7920_The large polyprotein (papain type proteases, methyltransferase, and helicase) has a sequence of amino acids corresponding to SEQ. ID. No .: 3, as follows: Thr Leu Arg Glu Asn Pro lie Ser Val Ser Gly Val? Sn Leu Gly Arg 1 5 10 15 Be Ala Ala Ala Gln Val He Tyr Phe Gly Ser Phe Thr Gln Pro Phe 20 25 30 Ala Leu Tyr Pro Arg Gln Glu Ser Ala lie Val Lys Thr Gln Leu Pro 35 40 45 Pro Val Ser Val Val Lys Val Glu Val Val Clu Ala Ala Val Val Wing Pro 50 55 60 Asp Arg Val Val Valve Asp Lys Pro Thr Ser Val Val Val Val Pro Pro 65 70 75 80 Gln Arg Gly Val Leu Ser Phe Pro Thr Val Val Arg Asn Arg Gly Asp 85 90 95 Val lie lie Thr Gly Val Val His Glu Ala Leu Lys Lys lie Lys Asp 100 105 110 Gly Leu Leu Arg Phe Arg Val Gly Gly Asp Met Arg Phe Ser Arg Phe 115 120 125 Phe Ser Asn Tyr Gly Cys Arg Phe Val Wing Ser Val Arg Thr Asn 130 135 140 Thr Thr Val Trp Leu Asn Cys Thr Lys Wing Ser Gly Glu Lys Phe Ser 145 150 155 160 Leu Ala Ala Ala Cys Thr Ala Asp Tyr Val Ala Met Leu Arg Tyr Val 165 170 175 Cys Gly Gly Lys Phe Pro Leu Val Leu Met Ser Arg Val He Tyr Pro 180 185 190 Asp Gly Arg Cys Tyr Leu Ala His Met Arg Tyr Leu Cys Ala Phe Tyr 195 200 205 Cys Arg Pro Phe Arg Glu As Asp Tyr Ala Leu Gly Met Trp Pro Thr 210 215 220 Val Wing Arg Leu Arg Wing Cys Val Glu Lys Asn Phe Gly Val Glu Wing 225 230 235 240 Cys Gly He Ala Leu Arg Gly Tyr Tyr Thr Ser Arg Asn Val Tyr His 245 250 255 Cys Asp Tyr Asp Ser Wing Tyr Val Lys Tyr Phe Arg Asn Leu Ser Gly 260 265 270 Arg He Gly Gly Gly Ser Phe Asp Pro Thr Ser Leu Thr Ser Val He 275 280 285 Thr Val Lys He Ser Gly Leu Pro Gly Gly Leu Pro Lys Asn He Ala 290 295 300 Phe Gly Wing Phe Leu Cys Asp He Arg Tyr Val Glu Pro Val Asp Ser 305 310 315 320 Gly Gly He Gln Ser Ser Val Lys Thr Lys Arg Glu Asp Ala His Arg 325 330 335 Thr Val Glu Glu Arg Wing Wing Gly Gly Ser Val Glu Gln Pro Arg Gln 340 345 350 Lys Arg He Asp Glu Lys Gly Cys Gly Arg Val Pro Ser Gly Gly Phe 355 360 365 Ser His Leu Leu Val Gly Asn Leu Asn Glu Val Arg Arg Lys Val Wing 370 375 380 Wing Gly Leu Leu Arg Phe Arg Val Gly Gly Asp Met Asp Phe His Arg 385 390 395 400 Ser Phe Ser Thr Gln Wing Gly His Arg Leu Leu Val Trp Arg Arg Ser 405 410 415 Ser Arg Ser Val Cys Leu Glu Leu Tyr Ser Pro Ser Lys Asn Phe Leu 420 425 430 Arg Tyr Asp Val Leu Pro Cys Ser Gly Asp Tyr Wing Wing Met Phe Ser 435 440 445 Phe Wing Wing Gly Gly Arg Phe Pro Leu Val Leu Met Thr Arg He Arg 450 455 460 Tyr Pro Asn Gly Phe Cys Tyr Leu Wing His Cys Arg Tyr Wing Cys Wing 465 470 475 480 Phe Leu Leu Arg Gly Phe Asp Pro Lys Arg Phe Asp He Gly Wing Phe 485 490 495 Pro Thr Wing Wing Lys Leu Arg Asn Arg Met Val Ser Glu Leu Gly Glu 500 505 510 Arg Ser Leu Gly Leu Asn Leu Tyr Gly Wing Tyr Thr Ser Arg Gly Val 515 520 525 Phe His Cys Asp Tyr Asp Wing Lys Phe He Lys Asp Leu Arg Leu Met 530 535 540 Ser Wing Val He Wing Gly Lys Asp Gly Val Val Glu Val Val Val Pro Ser 545 550 555 560 Asp He Thr Pro Wing Met Lys Gln Lys Thr He Glu Wing Val Tyr Asp 565 570 575 Arg Leu Tyr Gly Gly Thr Asp Ser Leu Leu Lys Leu Ser He Glu Lys 580 585 590 Asp Leu He Asp Phe Lys Asn Asp Val Gln Ser Leu Lys Lys Asp Arg 595 600 605 Pro He Val Lys Val Pro Phe Tyr Met Ser Glu Ala Thr Gln Asn Ser 610 615 620 Leu Thr Arg Phe Tyr Pro Gln Phe Glu Leu Lys Phe Ser His Ser Ser 625 630 635 640 His Ser Asp His Pro Ala Ala Ala Ala Ser Arg Leu Leu Glu Asn Glu 645 650 655 Thr Leu Val Arg Leu Cys Gly Asn Ser Val Ser Asp He Gly Gly Cys 660 665 670 Pro Leu Phe His Leu His Ser Lys Thr Gln Arg Arg Val His Val Cys 675 680 685 Arg Pro Val Leu Asp Gly Lys Asp Ala Gln Arg Arg Val Val Arg? Sp 690 695 700 Leu Gln Tyr Ser Asn Val Arg Leu Gly Asp Asp Asp Lys He Leu Glu 705 710 715 720 Gly Pro Arg Asn He Asp He Cys His Tyr Pro Leu Gly Ala Cys Aso 725 730 735 His Glu Being Ser Wing Met Met Met Val Gln Val Tyr Asp Wing Ser Leu 740 745 750 Tyr Glu lie Cys Gly Wing Met He Lys Lys Lys Ser Arg He Thr Tyr 755 760 765 Leu Thr Met Val Thr Pro Gly Glu Phe Leu Asp Gly Arg Glu Cys Val 770 775 780 Tyr Met Glu Ser Leu Asp Cys Glu He Glu Val Asp Val His Ala Asp 785 790 795 800 Val Val Met Tyr Lys Phe Gly Ser Ser Cys Tyr Ser His Lys Leu Ser 805 810 815 He He Lys Asp He Met Thr Thr Pro Tyr Leu Thr Leu Gly Gly Phe 820 825 830 Leu Phe Ser Val Glu Met Tyr Glu Val Arg Met Gly Val Asn Tyr Phe 835 840 845 Lys He Thr Lys Ser Glu Val Ser Pro Ser He Ser Cys Thr Lys Leu 850 855 860 Leu Arg Tyr Arg Arg Ala Asn Ser Asp Val Val Lys Val Lys Leu Pro 865 870 875 880 Arg Phe Asp Lys Lys Arg Arg Met Cys Leu Pro Gly Tyr Asp Thr He 885 890 895 Tyr Leu Asp Ser Lys Phe Val Ser Arg Val Phe Asp Tyr Val Val Cys 900 905 910 Asn Cys Ser Wing Val Asn Ser Lys Thr Phe Glu Trp Val Trp Ser Phe 915 920 925 lie Lys Ser Ser Lys Ser Arg Val He He Ser Gly Lys He He His 930 935 940 Lys Asp Val Asn Leu Asp Leu Lys Tyr Val Glu Ser Phe Ala Ala Val 945 950 955 960 Met Leu Ala Ser Gly Val Arg Ser Arg Leu Ala Ser Glu Tyr Leu Ala 965 970 975 Lys Asn Leu Ser His Phe Ser Gly Asp Cys Ser Phe He Glu Wing Thr 980 985 990 Ser Phe Val Leu Arg Glu Lys He Arg Asn Met Thr Leu Asn Phe Asn 995 1000 1005 Glu Arg Leu Leu Gln Leu Val Lys Arg Val Ala Phe Wing Thr Leu Asp 1010 1015 1020 Val Ser Phe Leu Asp Leu Asp Ser Thr Leu Glu Ser He Thr Asp Phe 1025 1030 1035 1040 Wing Glu Cys Lys Val Wing He Glu Leu Asp Glu Leu Gly Cys Leu? Rg 1045 1050 1055 Wing Glu Wing Glu Asn Glu Lys He Arg Asn Leu Wing Gly Asp Ser He 1060 1065 1070 Wing Wing Lys Leu Wing Ser Glu He Val Val Asp He Asp Ser Lys Pro 1075 1080 1085 Ser Pro Lys Gln Val Gly Asn Ser Ser Glu Asn Wing Asp Lys Arg 1090 1095 1100 Glu Val Gln Arg Pro Gly Leu Arg Gly Gly Ser Arg Asn Gly Val Val 1105 1110 1115 1120 Gly Glu Phe Leu His Phe Val Val Asp Ser Ala Leu Arg Leu Phe Lys 1125 1130 1135 Tyr Wing Thr Asp Gln Gln Arg He Lys Ser Tyr Val Arg Phe Leu Asp 1140 1145 1150 Ser Wing Val Ser Phe Leu Asp Tyr Asn Tyr Asp Asn Leu Ser Phe He 1155 1160 1165 Leu Arg Val Leu Ser Glu Gly Tyr Ser Cys Met Phe Wing Phe Leu Wing 1170 1175 1180 Asn Arg Gly Asp Leu Ser Ser Arg Val Arg Ser Wing Val Cys Wing Val 1185 1190 1195 1200 Lys Glu Val Wing Thr Ser Cys Wing Asn Wing Ser Val Ser Lys Wing Lys 1205 1210 1215 Val Met He Thr Phe Wing Wing Wing Val Cys Wing Met Met Phe Asn Ser 1220 1225 1230 Cys Gly Phe Ser Gly Asp Gly Arg Glu Tyr Lys Ser Tyr He His Arg 1235 1240 1245 Tyr Thr Gln Val Leu Phe Asp Thr He Phe Phe Glu Asp Ser Ser Tyr 1250 1255 1260 Leu Pro He Glu Val Leu Ser Be Ala He Cys Gly Ala He Val Val 1255 1270 1275 1280 Leu Phe Ser Ser Gly Be Ser Be Leu Asn Ala Phe Leu Leu Gln 1285 1290 1295 He Thr Lys Gly Phe Ser Leu Glu Val Val Val Arg Asn Val Val Arg 1300 1305 1310 Val Thr His Gly Leu Ser Thr Thr Wing Thr Asp Gly Val He Arg Gly 1315 1320 1325 Val Phe Ser Gln He Val Ser His Leu Leu Val Gly Asn Thr Gly Asn 1330 1335 1340 Val Ala Tyr Gln Ser Ala Phe He Ala Ala Gly Val Val Pro Leu Leu Val 1345 1350 1355 1360 Lys Lys Cys Val Ser Leu He Phe He Leu Arg Glu Asp Thr Tyr Ser 1365 1370 1375 Gly Phe He Lys His ^ Gly He Ser Glu Phe Ser Phe Leu Ser Ser He 1380 1385 1390 Leu Lys Phe Leu Lys Gly Lys Leu Val Asp Glu Leu Lys Ser He He 1395 1400 1405 Gln Gly Val Phe Asp Ser Asn Lys His Val Phe Lys Glu Ala Thr Gln 1410 1415 1420 Glu Ala He Arg Thr Thr Val Val Gln Val Pro Val Ala Val Val Asp 1425 1430 1435 1440 Ala Leu Lys Ser Ala Ala Gly Lys He Tyr Asn Asn Phe Thr Ser Arg 1445 1450 1455 Arg Thr Phe Gly Lys Asp Glu Gly Be Ser Asp Gly Ala Cys Glu 1460 1465 1470 Glu Tyr Phe Ser Cys Asp Glu Gly Glu Gly Pro Gly Leu Lys Gly Gly 1475 1480 1485 Ser Ser Tyr Gly Phe Ser He Leu Wing Phe Phe Ser Arg He Met Trp 1490 1495 1500 Gly Wing Arg Arg Leu He Val Lys Val Lys His Glu Cys Phe Gly Lys 1505 1510 1515 1520 Leu Phe Glu Phe Leu Ser Leu Lys Leu His Glu Phe Arg Thr Arg Val 1525 1530 1535 Phe Gly Lys Asn Arg Thr Asp Val Gly Val Tyr Asp Phe Leu Pro Thr 1540 1545 1550 Gly lie Val Glu Tlir Leu Ser Ser lie Glu Glu Cys? Sp Gln lie Glu 1555 1560 1565 Glu Leu Leu Gly Asp? Sp Leu Lys Gly? sp Lys? sp? the Ser Leu Thr 1570 1575 1580? sp Het? sn Tyr Phe Glu Phe Ser Glu? sp Phe Leu? the Ser lie Glu 1585 1590 1595 1600 Glu Pro Pro Phe? Gly Leu? Rg Gly Gly Ser Lys Asn lie? La He 1605 1610 1615 Leu? La lie Leu Glu Tyr Ala His Asn Leu Phe Arg lie Val Ala Ser 1620 1625 1630 Lys Cys Ser Lys Arg Pro Leu Phe Leu? The Phe? The Glu Leu Ser Ser 1635 1640 1645 Wing Leu lie Glu Lys Phe Lys Glu Val Phe Pro Arg Lys Ser G n Leu 1650 1655 1660 Val Ala He Val? Rg Glu Tyr Thr Gln Arg Phe Leu Arg Ser Arg Met 1665 1670 1675 1680 Arg? The Leu Gly Leu Asn Asn Glu Phe Val Val Lys Ser Phe Ala? Sp 1685 1690 1695 Leu Leu Pro Ala Leu Met .Lys? Rg Lys Val Ser Gly Ser Phe Leu Ala 1700 1705 1710 Ser Val Tyr Arg Pro Leu Arg Gly Phe Ser Tyr Met Cys Val Ser? La 1715 1720 1725 Glu? Rg Arg Glu Lys Phe Phe Wing Leu Val Cys Leu lie Gly Leu Ser 1730 1735 1740 Leu Pro Phe Val Val Arg He Val Gly Ala Lys Ala Cys Glu Glu Leu 1745 1750 1755 1760 Val Ser Being Wing Arg Arg Phe Tyr Glu? Rg He Lys He Phe Leu? Rg 1765 1770 1775 Gln Lys Tyr Val Ser Leu Ser Asn Phe Phe Cys liis Leu Phe Ser Ser 1780 1785 1790 Asp Val Asp Asp Ser Be Wing Be Wing Gly Leu Lys Gly Gly Wing Ser 1795 1800 1805? Rg Met Thr Leu Phe His Leu Leu Val Arg Leu Wing Being Wing Leu Leu 1810 1815 1820 Ser Leu Gly Trp Glu Gly Leu Lys Leu Leu Leu Ser His His Asn Leu 1825 1830 1835 1840 Leu Phe Leu Cys Phe Ala Leu Val Asp? Sp Val Asn Val Leu He Lys 1845 1850 1855 Val Leu Gly Gly Leu Be Phe Phe Val Gln Pro He Phe Ser Leu Phe 1860 1865 1870 The Wing Met Leu Leu Gln Pro? sp Arg Phe Val Glu Tyr Ser Glu Lys 1875 1880 1885 Leu Val Thr? the Phe Glu Phe Phe Leu Lys Cys Ser Pro? rg Ala Pro 1B90 1895 1900 Wing Leu Leu Lys Gly Phe Phe Glu Cys Val Wing Asn Ser Thr Val Ser 1905 1910 1915 1920 Lys Thr Val Arg Arg Leu Leu? Rg Cys Phe Val Lys Met Leu Lys Leu 1925 1930 1935 Arg Lys Gly? Rg Gly Leu Arg Ala? Sp Gly? Rg Gly Leu His Arg Gln 1940 1945 1950 Lys Ala Val Pro Val He Pro Ser Asn Arg Val Val Thr Asp Gly Val 1955 1960 1965 Glu Arg Leu Ser Val Lys Met Gln Gly Val Glu Ala Leu? Rg Thr Glu 1970 1975 1980 Leu? Rg He Leu Glu? Sp Leu? Sp Ser Ala Val He Glu Lys Leu? Sn 1985 1990 1995 2000 Arg Arg? Rg Asn Arg Asp Thr Asn Asp Asp Glu Phe Thr Arg Pro? 2005 2010 2015 His Glu Gln Met Gln Glu Val Thr Thr Phe Cys Ser Lys? The? Sp Ser 2020 2025 2030 Wing Gly Leu Wing Leu Glu Arg? Val Leu Val Glu? Sp? He Lys 2035 2040 2045 Ser Glu Lys Leu Ser Lys Thr Val Asn Glu Met Val Arg Lys Gly Ser 2050 2055 2060 Thr Thr Ser Glu Val Val Wing Val Leu Ser Asp? Sp Glu Val Wing 2065 2070 2075 2080 Glu Glu He Ser Val Wing Asp Glu Arg Asp Asp Ser Pro Lys Thr Val 2085 2090 2095 Arg He Ser Glu Tyr Leu? Sn Arg Leu? Sn Ser Ser Phe Glu Phe Pro 2100 2105 2110 Lys Pro He Val Val Asp Asp Asn Lys Asp Thr Gly Gly Leu Thr Asn 2115 2120 2125? Val Arg Glu Phe Tyr Tyr Met Gln Glu Leu? Leu Phe Glu He 2130 2135 2140 His Ser Lys Leu Cys Thr Tyr Tyr Asp Gln Leu? Rg He Val Asn Phe 2145 2150 2155 2160 ? 3p Arg Ser Val Wing Pro Cys Ser Glu Asp Wing Gln Leu Tyr Val Arg 2165 2170 2175 Lys? Sn Gly Ser Thr He Val Gln Gly Lys- Glu Val Arg Leu His He 2180 2185 2190 Lys Asp Phe llis Asp His Asp Phe Leu Phe Asp Gly Lys He Be He 2195 2200 2205 Asn Lys Arg Arg? Rg Gly Gly Asn Val Leu Tyr llis Asp? Sn Leu Wing 2210 2215 2220 Phe Leu Ala Ser? Sn Leu P e Leu Wing Gly Tyr Pro Phe Ser Arg Ser 2225 2230 2235 2240 Phe Val Phe Thr Asn Ser Ser Val Asp Lie Leu Leu Tyr Glu Pro 2245 2250 2255 Pro Gly Gly Gly Lys Thr Thr Thr Leu He Asp Ser Phe Leu Lys Val 2260 2265 2270 Phe Lys Lys Gly ßlu Val Ser Thr Met He Leu Thr Wing Asn Lys Ser 2275 2280 2285 Ser Gln Val Glu He Leu Lys Lys Val Glu Lys Glu Val Ser? Sn He 2290 2295 2300 Glu Cys Gln Lys? Rg Lys? Sp Lys Arg Ser Pro Lys Lys Ser He Tyr 2305 2310 2315 2320 Thr He Asp? The Tyr Leu Met His His? Rg Gly Cys? Sp Wing Asp Val 2325 2330 2335 Leu Phe He Asp Glu Cys Phe Met Val His Wing Gly Ser Val Leu? La 2340 2345 2350 Cys He Glu Phe Thr Arg Cys Llis Lys Val Met He Phe Gly? Sp Ser 2355 2360 2365 Arg Gln He His Tyr He Glu Arg? Sn Glu Leu? Sp Lys Cys Leu Tyr 2370 2375 2380 Gly Asp Leu Asp Arg Phe Val Asp Leu Gln Cys Arg Val Tyr Gly? Sn 2385 2390 2395 2400 I have been Tyr? Rg Cys Pro Trp Asp Val Cys? The Trp Leu Ser Thr Val 2405 2410 2415 Tyr Gly Asn Leu He Wing Thr Val Lys Gly Glu Ser Glu Gly Lys Ser 2420 2425 2430 Ser Met Arg He Asn Glu He Asn Ser Val Asp Asp Leu Val Pro? Sp 2435 2440 2445 Val Gly Ser Thr Phe Leu Cys Met Leu Gln Ser Glu Lys Leu Glu He 2450 2455 2460 Ser Lys His Phe He Arg Lys Gly Leu Thr Lys Leu Asn Val Leu Thr 2465 2470 2475 2480 Val His Glu? The Gln Gly Glu Thr Tyr Ala Arg Val Asn Leu Val Arg 2485 2490 2495 Leu Lys Phe Gln Glu Asp Glu Pro Phe Lys Ser He Arg His He Thr 2500 2505 2510 Val Ala Leu Ser Arg His Thr Asp Ser Leu Thr Tyr? Sn Val Leu Wing 2515 2520 2525 Wing Arg Arg Gly Asp Wing Thr Cys Asp Wing He Gln Lys Ala Ala Glu 2530 2535 2540 Leu Val Asn Lys Phe Arg Val Phe Pro Thr Ser Phe Gly Gly Ser Val 2545 2550 2555 2560 He Asn Leu Asn Val Lys Lys Asp Val Glu Asp Asn Ser Arg Cys Lys 2565 2570 2575 Wing Being Wing Pro Leu Ser Val He Asn Asp Phe Leu Asn Glu Val 2580 2585 2590 Asn Pro Gly Thr Wing Val He Asp Phe Gly Asp Leu Ser Wing Asp Phe 2595 2600 2605 Ser Thr Gly Pro Phe Glu Cys Gly Wing Ser Gly He Val Val Arg Asp 2610 2615 2620 Asn He Ser Ser Ser As As He Thr Asp His Asp Lys Gln Arg Val 2625 2630 2635 and has a molecular weight of approximately 290 to 300 kDa, preferably 294 kDa. Another DNA molecule (GLRaV-2 ORFlb) includes nucleotides 7922-9301 of SEQ. ID. No.: 1, and codifies for a RNA-dependent RNA polyrase (RdRP) of the virus • curl vine leaf. This DNA molecule comprises the nucleotide sequence corresponding to SEQ. ID. No .: 4, as follows: AGCGTAGTTC GGTCGCAGGC GATTCCGCGT AGAAAACCTT CTCTACAAGA AAATTTGTAT 60 TCGTTTGAAG CGCGGAATTA TAACTTCTCG ACTTGCGACC GTAACACATC TGCTTCAATG 120 TTCGGAGAGG CTATGGCGAT GAACTGTCTT CGTCGTTGCT TCGACCTAGA TGCCTTTTCG 180 TCCCTGCGTG ATGATGTGAT TAGTATCACA CGTTCAGGCA TCGAACAATG GCTGGAGAAA 240 CGTACTCCTA GTCAGATTAA AGCATTAATG AAGGATGTTG AATCGCCTTT GGAAATTGAC 300 GATGAAATTT GTCGTTTTAA GTTGATGGTG AAGCGTGACG CTAAGGTGAA GTTAGACTCT 360 TCTTGTTTAA CTAAACACAG CGCCGCTCAA AATATCATGT TTCATCGCAA GAGCATTAAT 420CTCCTATCTT TAATGAGGTG AAAAACCGAA TAATGTGCTG TCTTAAGCCT 480 AACATAAAGT TTTTTACGGA GATGACTAAC AGGGATTTTG CTTCTGTTGT CAGCAACATG 540 CTTGGTGACG ACGATGTGTA CCATATAGGT GAAGTTGATT TCTCAAAGTA CGACAAGTCT 600 CAAGATGCTT TCGTGAAGGC TTTTGAAGAA GTAATGTATA AGGAACTCGG TGTTGATGAA 660 GAGTTGCTGG CTATCTGGAT GTGCGGCGAG CGGTTATCGA TAGCTAACAC TCTCGATGGT 720 CAGTTGTCCT TCACGATCGA GAATCAAAGG AAGTCGGGAG CTTCGAACAC TTGGATTGGT 780 AACTCTCTCG TCACTTTGGG TATTTTAAGT CTTTACTACG ACGTTAGAAA TTTCGAGGCG 840 TTGTACATCT CGGGCGATGA TTCTTTAATT TTTTCTCGCA GCGAGATTTC GAATT? TGCC 900 GACGACATAT GCACTGACAT GGGTTTTGAG ACAAAATTTA TGTCCCCAAG TGTCCCGTAC 960 TTTTGTTCTA AATTTGTTGT TATGTGTGGT CATAAGACGT TTTTTGTTCC CGACCCGTAC 1020 AAGCTTTTTG TCA? GTTGGG AGCAGTCAAA GAGGATGTTT CAATGGATTT CCTTTTCG? G 1080 ACTTTTACCT CCTTTAAAGA CTTAACCTCC GATTTTAACG ACG? GCGCTT AATTCAAAAG 1140 CTCGCTGAAC TTGTGGCTTT AAAATATGAG GTTCAA? CCG GCAACACCAC CTTGGCGTTA 1200 AGTGTGATAC ATTGTTTGCG TTCGAATTTC CTCTCGTTTA GCAAGTTATA TCCTCGCGTG 1260 AAGGGATGGC AGGTTTTTTA CACGTCGGTT AAGAAAGCGC TTCTCAAGAG TGGGTGTTCT 1320 CTCTTCGACA GTTTCATGAC CCCTTTTGGT CAGGCTGTCA TGGTTTGGGA TGATGAGTAG_1380_The RNA-dependent RNA polymerase has an amino acid sequence corresponding to SEQ. ID. No. 5, as follows: S1er Val Val Arg S5er Gln Ala He Pro A1r0g Arg Lys Pro Ser L1e5u Gln Glu Asn Leu Tyr Ser Phe Glu Wing Arg Asn Tyr Asn Phe Ser Thr Cys 20 25 30 Asp Arg Asn Thr Ser Wing Being Met Phe Gly Glu Wing Met Wing Met Asn 35 40 45 Cys Leu Arg Arg Cys Phe Asp Leu Asp Wing Phe Ser Ser Leu Arg Asp 50 55 60 Asp Val He Ser He Thr Arg Ser Gly He Glu Gln Trp Leu Glu Lys 65 70 75 80 Arg Thr Pro Ser Gln He Lys Ala Leu Met Lys Asp Val Glu Ser Pro 85 90 95 Leu Glu He Asp Asp Glu He Cys Arg Phe Lys Leu Met Val Lys Arg 100 105 110 Asp Wing Lys Val Lys Leu Asp Ser Ser Cys Leu Thr Lys His Ser Wing 115 120 125 Wing Gln Asn He Met Phe His Arg Lys Ser He Asn Wing He Phe Ser 130 135 140 Pro He Phe Asn Glu Val Lys Asn Arg He Met Cys Cys Leu Lys Pro 145 150 155 160 Asn He Lys Phe Phe Thr Glu Met Thr Asn Arg Asp Phe Ala Ser Val 165 170 175 Val Ser Asn Met Leu Gly Asp Asp Asp Val Tyr His He Gly Glu Val 180 185 190 Asp Phe Ser Lys Tyr Asp Lys Ser Gln Asp Wing Phe Val Lys Wing Phe 195 200 205 Glu Glu Val Met Tyr Lys Glu Leu Gly Val Asp Glu Glu Leu Leu Ala 210 215 220 He Trp Met Cys Gly Glu Arg Leu Ser He Wing Asn Thr Leu? Sp Gly 225 230 235 240 Gln Leu Ser Phe Thr He Glu Asn Gln Arg Lys Ser Gly Wing Ser Asn 245 250 255 Thr Trp He Gly Asn Ser Leu Val Thr Leu Gly He Leu Ser Leu Tyr 260 265 270 Tyr Asp Val Arg Asn Phe Glu Wing Leu Tyr He Ser Gly Asp Asp Ser 275 280 285 Leu He Phe Ser Arg Ser Glu He Ser Asn Tyr Wing Asp Asp He Cys 290 295 300 Thr Asp Met Gly Phe Glu Thr Lys Phe Met Pro Ser Ser Val Pro Tyr 305 310 315 320 Phe Cys Ser Lys Phe Val Val Met Cys Gly His Lys Thr Phe Phe Val 325 330 335 Pro Asp Pro Tyr Lys Leu Phe Val Lys Leu Gly Wing Val Lys Glu Asp 340 345 350 Val Ser Met Asp Phe Leu Phe Glu Thr Phe Thr Ser Phe Lys Asp Leu 355 360 365 Thr Ser Asp Phe Asn Asp Glu Arg Leu He Gln Lys Leu Ala Glu Leu 370 375 380 Val Ala Leu Lys Tyr Glu Val Gln Thr Gly Asn Thr Thr Leu Ala Leu 385 390 395 400 Ser Val He His Cys Leu Arg Ser Asn Phe Leu Ser Phe Ser Lys Leu 405 410 415 Tyr Pro Arg Val Lys Gly Trp Gln Val Phe Tyr Thr Ser Val Lys Lys 420 425 430 Wing Leu Leu Lys Ser Gly Cys Ser Leu Phe Asp Ser Phe Met Thr Pro 435 440 445 Phe Gly Gln Wing Val Met Val Trp Asp Asp Glu 450 455 and a molecular weight of approximately 50 to approximately 54 kDa, preferably approximately 52 kDa . Another DNA molecule (GLRaV-2 ORF2) includes nucleotides 9365-9535 of SEQ. ID. No.: 1, and encodes a small hydrophobic protein or polypeptide of vine leaf winding virus. This DNA molecule comprises the nucleotide sequence corresponding to SEQ. ID. No .: 6, as follows: ATGAATCAGG TTTTGCAGTT TGAATGTTTG TTTCTGCTGA ATCTCGCGGT TTTTGCTGTG 60 ACTTTCATTT TCATTCTTCT GGTCTTCCGC GTGATTAAGT CTTTTCGCCA GAAGGGTCAC 120 GAAGCACCTG TTCCCGTTGT TCGTGGCGGG GGTTTTTCAA CCGT? GTGTA G 171ydrophobic protein or polypeptide has an amino acid sequence corresponding to SEQ. ID. No .: 7, as follows: Met Asn Gln Val Leu Gln Phe Glu Cys Leu Phe Leu Leu Asn Leu Wing 1 5 10 15 Val Phe Wing Val Thr Phe He Phe He Leu Leu Val Phe Arg Val He 20 25 30 Lys Ser Phe Arg Gln Lys Gly His Glu Ala Pro Val Pro Val Val Arg 35 40 45 Gly Gly Gly Phe Ser Thr Val Val 50 55 and a molecular weight of about 5 to about 7 kDa, preferably about 6 kDa.

Another DNA molecule (GLRaV-2 ORF3) includes nucleotides 9551-11350 of SEQ. ID. No .: 1, and it codes for a heat-chogue protein 70 of the vine leaf winding virus. This DNA molecule comprises the nucleotide sequence corresponding to SEQ. ID. No .: 8, as follows: ATGGTAGTTT TCGGTTTGGA CTTTGGCACC ACATTCTCTA CGGTGTGTGT GTACAAGGAT 60 GGACGAGTTT TTTCATTCAA GCAGAATAAT TCGGCGTACA TCCCCACTTA CCTCTATCTC 120 TTCTCCGATT CTAACCACAT GACTTTTGGT TACGAGGCCG AATCACTGAT GAGTAATCTG 180 AAAGTTAAAG GTTCGTTTTA TAGAGATTTA AAACGTTGGG TGGGTTGCGA TTCGAGTAAC 240 CTCGACGCGT ACCTTGACCG TTTAAAACCT CATTACTCGG TCCGCTTGGT TAAGATCGGC 300 TCTGGCTTGA ACGAAACTGT TTCAATTGGA AACTTCGGGG GCACTGTTAA GTCTGAGGCT 360 CATCTGCCAG GGTTGATAGC TCTCTTTATT AAGGCTGTCA TTAGTTGCGC GGAGGGCGCG 420 TTTGCGTGCA CTTGCACCGG GGTTATTTGT TCAGTACCTG CCAATTATGA TAGCGTTCAA 480 AGGAATTTCA CTGATCAGTG TGTTTCACTC AGCGGTTATC AGTGCGTATA TATGATCAAT 540 GAACCTTCAG CGGCTGCGCT ATCTGCGTGT AATTCGATTG GAAAGAAGTC CGCAAATTTG 600 GCTGTTTACG ATTTCGGTGG TGGGACCTTC GACGTGTCTA TCATTTCATA CCGCAACAAT 660 ACTTTTGTTG TGCGAGCTTC TGGAGGCGAT CTAAATCTCG GTGGAAGGGA TGTTGATCGT 720 GCGTTTCTCA CGCACCTCTT CTCTTTAACA TCGCTGGAAC CTGACCTCAC TTTGGATATC 780 TCGAATCTGA AAGAATCTTT ATCAAAAACG GACGCAGAGA TAGTTTACAC TTTGAGAGGT 840 GTCGATGGAA GA? AAGAAGA CGTTAGAGTA AACAAAAACA TTCTTACGTC GGTGATGCTC 900 CCCTACGTGA ACAGAACGCT TAAGATATTA GAGTCAACCT TAAAATCGTA TGCTAAGAGT 960 ATGAATGAGA GTGCGCGAGT TAAGTGCGAT TTAGTGCTGA TAGGAGGATC TTCATATCTT 1020 CCTGGCCTGG CAGACGTACT AACGAAGCAT CAGAGCGTTG ATCGTATCTT AAGAGTTTCG 1080 GATCCTCGGG CTGCCGTGGC CGTCGGTTGC GCATTATATT CTTCATGCCT CTCAGGATCT 1140 GGGGGGGTTGC T? CTGATCGA CTGTGCAGCT CACACTGTCG CTATAGCGGA CAGAAGTTGT 1200 CATCAAATCA TTTGCGCTCC AGCGGGGGCA CCGATCCCCT TTTCAGGAAG CATGCCTTTG 1260 TACTTAGCCA GGGTCAACAA GAACTCGCAG CGTGAAGTCG CCGTGTTTGA AGGGGAGTAC 1320 GTTAAGTGCC CTAAGAACAG AAAGATCTGT GGAGCAAATA TAAGATTTTT TGATATAGGA 1380 GTGACGGGTG ATTCGTACGC ACCCGTTACC TTCTATATGG ATTTCTCCAT TTCAAGCGTA 1440 GGAGCCGTTT CATTCGTGGT GAGAGGTCCT GAGGGTATAGC AAGTGTCACT CACTGGAACT 1500 CCAGCGTATA ACTTTTCGTC TGTGGCTCTC GGATCACGCA GTGTCCGAGA ATTGCATATT 1560 AGTTTAAATA ATAAAGTTTT TCTCGGTTTG CTTCTACATA GAAAGGCGGA TCGACGAATA 1620 CTTTTCACTA AGGATGAAGC GATTCGATAC GCCGATTCAA TTGATATCGC GGATGTGCTA 1680 AAGGAATATA AAAGTTACGC GGCCAGTGCC TTACCACCAG ACGAGGATGT CGAATTACTC 1740 CTGGGAAAGT CTGTTCAAAA AGTTTTACGG GGAAGCAGAC TGGAAGAAAT ACCTCTCTAG_1800_The heat shock protein 70 is believed to function as a chaperone protein, and has an amino acid sequence corresponding to SEQ. ID. No .: 9, as follows: Met Val Val Phe Gly Leu Asp Phe Gly Thr Thr Phe Ser Thr Val Cys 1 5 10 15 Val Tyr Lys Asp Gly Arg Val Phe Ser Phe Lys Gln Asn Asn Ser Wing 20 25 30 Tyr He Pro Thr Tyr Leu Tyr Leu Phe Ser Asp Ser Asn His Met Thr 35 40 45 Phe Gly Tyr Glu Wing Glu Ser Leu Met Ser Asn Leu Lys Val Lys Gly 50 55 60 Ser Phe Tyr Arg Asp Leu Lys Arg Trp Val Gly Cys Asp Ser Asn 65 70 75 80 Leu Asp Wing Tyr Leu Asp Arg Leu Lys Pro His Tyr Ser Val Arg Leu 85 90 95 Val Lys He Gly Ser Gly Leu Asn Glu Thr Val Ser He Gly Asn Phe 100 105 110 Gly Gly Thr Val Lys Ser Glu Wing His Leu Pro Gly Leu He Wing Leu 115 120 125 Phe He Lys Wing Val He Ser Cys Wing Glu Gly Wing Phe Wing Cys Thr 130 135 140 Cys Thr Gly Val He Cys Ser Val Pro Wing Asn Tyr Asp Ser Val Gln 145 150 155 160 Arg Asn Phe Thr Asp Gln Cys Val Ser Leu Ser Gly Tyr Gln Cys Val 165 170 175 Tyr Met He Asn Glu Pro Be Wing Wing Wing Leu Being Wing Cys Asn Being 180 185 190 He Gly Lys Lys Being Wing Asn Leu Wing Val Tyr Asp Phe Gly Gly Gly 195 200 205 Thr Phe Asp Val Ser He He Ser Tyr Arg Asn Asn Thr Phe Val Val 210 215 220 Arg Wing Ser Gly Gly Asp Leu Asn Leu Gly Gly Arg Asp Val Asp Arg 225 230 235 240 Wing Phe Leu Thr His Leu Phe Ser Leu Thr Ser Leu Glu Pro Asp Leu 245 250 255 Thr Leu Asp He Ser Asn Leu Lys Glu Ser Leu Ser Lys Thr Asp Wing 260 265 270 Glu He Val Tyr Thr Leu Arg Gly Val Asp Gly Arg Lys Glu Asp Val 275 280 285 Arg Val Asn Lys Asn He Leu Thr Ser Val Met Leu Pro Tyr Val Asn 290 295 300 Arg Thr Leu Lys He Leu Glu Ser Thr Leu Lys Ser Tyr Ala Lys Ser 305 310 315 320 Met Asn Glu Be Wing Arg Val Lys Cys Asp Leu Val Leu He Gly Gly 325 330 335 Be Ser Tyr Leu Pro Gly Leu Wing Asp Val Leu Thr Lys His Gln Ser 340 345 350 Val Asp Arg He Leu Arg Val Ser Asp Pro Arg Wing Wing Val Wing Val 355 360 365 Gly Cys Wing Leu Tyr Ser Ser Cys Leu Ser Gly Ser Gly Gly Leu Leu 370 375 380 Leu He Asp Cys Wing Wing His Thr Val Wing He Wing Asp Arg Ser Cys 385 390 395 400 His Gln He He Cys Wing Pro Wing Gly Wing Pro He Pro Phe Ser Gly 405 410 415 Ser Met Pro Leu Tyr Leu Wing Arg Val Asn Lys Asn Ser Gln Arg Glu 420 425 430 Val Wing Val Phe Glu Gly Glu Tyr Val Lys Cys Pro Lys Asn Arg Lys 435 440 445 He Cys Gly Wing Asn He Arg Phe Phe Asp He Gly Val Thr Gly Asp 450 455 460 Ser Tyr Wing Pro Val Thr Phe Tyr Met Asp he Ser Ser Ser Ser Val 465 470 475 480 Gly Wing Val Ser Phe Val Val Arg Gly Pro Glu Gly Lys Gln Val Ser 485 490 495 Leu Thr Gly Thr Pro Ala Tyr Asn Phe Ser Ser Val Ala Leu Gly Ser 500 505 510 Arg Ser Val Arg Glu Leu liis He Ser Leu Asn Asn Lys Val Phe Leu 515 520 525 Gly Leu Leu Leu His Arg Lys Wing Asp Arg Arg He Leu Phe Thr Lys 530 535 540 Asp Glu Wing He Arg Tyr Wing Asp Ser He Asp He Wing Asp Val Leu 545 550 555 560 Lys Glu Tyr Lys Ser Tyr Ala Wing Wing Wing Leu Pro Pro Asp Glu Asp 565 570 575 Val Glu Leu Leu Leu Gly Lys Ser Val Gln Lys Val Leu Arg Gly Ser 580 585 590 Arg Leu Glu Glu He Pro Leu 595 and a molecular weight of from about 63 to about 67 kDa, preferably 65 kDa.

Another DNA molecule (GLRaV-2 ORF) includes nucleotides 11277-12932 of SEQ. ID. No .: 1, and encodes for a heat shock protein 90 of the grapevine leaf curl virus. This DNA molecule comprises a nucleotide sequence corresponding to SEQ. ID. No .: 10, as follows: ATGTCGAATT ACTCCTGGGA AAGTCTGTTC AAAAAGTTTT ACGGGGAAGC AGACTGGAAG 60 AAATACCTCT CTAGGAGCAT AGCAGCACAC TCAAGTGAAA TTAAAACTCT ACCAGACATT 120 CGATTGTACG GCGGTAGGGT TGTAAAGAAG TCCGAATTCG AATCAGCACT TCCTAATTCT 180 TTTGAACAGG AATTAGGACT GTTCATACTG AGCGAACGGG AAGTGGGATG GAGCAAATTA 240 TGCGGAATAA CGGTGGAAGA AGCAGCATAC GATCTTACGA ATCCCAAGGC TTATAAATTC 300 ACTGCCGAGA CATGTAGCCC GGATGTAAAA GGTGAAGGAC AAAAATACTC TATGGAAGAC 360 GTGATGAATT TCATGCGTTT ATCAAATCTG GATGTTAACG ACAAGATGCT GACGGAACAG 420 TGTTGGTCGC TGTCCAATTC ATGCGGTGAA TTGATCAACC CAGACGACAA AGGGCGATTC 480 GTGGCTCTCA CCTTTAAGGA CAGAGACACA GCTGATGACA CGGGTGCCGC CAACGTGGAA 540 TGTCGCGTGG GCGACTATCT AGTTTACGCT ATGTCCCTGT TTGAGCAGAG GACCC? AAAA 600 TCGCAGTCTG GCAACATCTC TCTGTACGAA AAGTACTGTG AATACATCAG GACCTACTTA 660 GGGAGTACAG ACCTGTTCTT CACAGCGCCG GACAGGATTC CGTTACTTAC GGGCATCCTA 720 TACGATTTTT GTAAGGAATA CAACGTTTTC TACTCGTCAT ATAAGAGAAA CGTCGATAAT 780 TTCAGATTCT TCTTGGCGAA TTATATGCCT TTGATATCTG ACGTCTTTGT CTTCCAGTGG 840 GTAAAACCCG CGCCGGATGT TCGGCTGCTT TTTGAGTTAA GTGCAGCGGA ACTAACGCTG 900 GAGGTTCCCA CACTGAGTTT GATAGATTCT CAAGTTGTGG TAGGTCATAT CTTA? GAT? C 960 GTAGAATCCT ACACATCAGA TCCAGCCATC G? CGCGTTAG AAGACAAACT GGAAGCGATA 1020 CTGAAAAGTA GCAATCCCCG TCTATCGACA GCGCA? CTAT GGGTTGGTTT CTTTTGTTAC 1080 TATGGTGAGT TTCGTACGGC TCAAAGTAGA GTAGTGCAAA GACCAGGCGT AT? CAAAACA 1140 CCTGACTCAG TGGGTGGATT TGAAATAAAC ATGAAAGATG TTGAGAAATT CTTCGATAAA 1200 CTTCAGAGAG AATTGCCTAA TGTATCTTTG CGGCGTCAGT TTAACGGAGC TAGAGCGCAT 1260 GAGGCTTTCA AAATATTTAA AAACGGAAAT ATAAGTTTCA GACCTATATC GCGTTTAAAC 1320 GTGCCTAGAG AGTTCTGGTA TCTGAACATA GACTACTTCA GGCACGCGAA TAGGTCCGGG 1380 TTAACCGAAG AAGAAATACT CATCCTAAAC AACATAAGCG TTGATGTTAG GAAGTTATGC 1440 GCTGAGAGAG CGTGCAATAC CCTACCTAGC GCGAAGCGCT TTAGTAAAAA TCATAAGAGT 1500 AATATACAAT CATCACGCCA AGAGCGGAGG ATTAAAGACC CATTGGTAGT CCTGAAAG? C 1560 ACTTTATATG AGTTCCAACA CAAGCGTGCC GGTTGGGGGT CTCGAAGCAC TCGAGACCTC 1620 GGGAGTCGTG CTGACCACGC GAAAGGAAGC GGTTGA 1656 The heat shock protein 90 has an acid sequence corresponding to SEQ. ID. No .: 11, as follows: Met Ser Asn Tyr Ser Trp Glu Ser Leu Phe Lys Lys Phe Tyr Gly Glu 1 5 10 15 Wing Asp Trp Lys Lys Tyr Leu Ser Arg Ser Wing Wing His Ser Ser 20 25 30 Glu He Lys Thr Leu Pro Asp He Arg Leu Tyr Gly Gly Arg Val Val 35 40 45 Lys Lys Ser Glu Phe Glu Be Ala Leu Pro Asn Ser Phe Glu Gln Glu 50 55 60 Leu Gly Leu Phe He Leu Ser Glu Arg Glu Val Gly Trp Ser Lys Leu 65 70 75 80 Cys Gly He Thr Val Glu Glu Ala Ala Tyr Asp Leu Thr Asn Pro Lys 85 90 95 Wing Tyr Lys Phe Thr Wing Glu Thr Cys Ser Pro Asp Val Lys Gly Glu 100 105 110 Gly Gln Lys Tyr Ser Met Glu Asp Val Met Asn Phe Met Arg Leu Ser 115 120 125 Asn Leu Asp Val Asn Asp Lys Met Leu Thr Glu Gln Cys Trp Ser Leu 130 135 140 Ser Asn Ser Cys Gly Glu Leu He Asn Pro Asp Asp Lys Gly Arg Phe 145 150 155 160 Val Ala Leu Thr Phe Lys Asp Arg Asp Thr Ala? Sp Asp Thr Gly Wing 165 170 175 Wing Asn Val Glu Cys Arg Val Gly Asp Tyr Leu Val Tyr Wing Met Ser 180 185 190 Leu Phe Glu Gln Arg Thr Gln Lys Ser Gln Ser Gly Asn He Ser Leu 195 200 205 Tyr G Lu Lys Tyr Cys Glu Tyr He Arg Thr Tyr Leu Gly Ser Thr Asp 210 215 220 Leu Phe Phe Thr Wing Pro Asp Arg He Pro Leu Leu Thr Gly He Leu 225 230 235 240 Tyr Asp Phe Cys Lys Glu Tyr Asn Val Phe Tyr Ser Ser Tyr Lys Arg 245 250 255 Asn Val Asp Asn Phe Arg Phe Phe Leu Wing Asn Tyr Met Pro Leu He 260 265 270 Ser Asp Val Phe Val Phe Gln Trp Val Lys Pro Pro Wing Asp Val Arg 275 280 285 Leu Leu Phe Glu Leu Be Wing Wing Glu Leu Thr Leu Glu Val Pro Thr 290 295 300 Leu Ser Leu He Asp Ser Gln Val Val Val Gly His He Leu Arg Tyr 305 310 315 320 Val Glu Ser Tyr Thr Ser Asp Pro Ala He Asp Ala Leu Glu Asp Lys 325 330 335 Leu Glu Wing He Leu Lys Ser Ser Asn Pro Arg Leu Ser Thr Wing Gln 340 345 350 Leu Trp Val Gly Phe Phe Cys Tyr Tyr Gly Glu Phe Arg Thr Wing Gln 355 360 365 Ser Arg Val Val Gln Arg Pro Gly Val Tyr Lys Thr Pro Asp Ser Val 370 375 380 Gly Gly Phe Glu He Asn Met Lys Asp Val Glu Lys Phe Phe Asp Lys 385 390 395 400 Leu Gln Arg Glu Leu Pro Asn Val Ser Leu Arg Arg Gln Phe Asn Gly 4 05 410 415 Arg Wing His Glu Wing Phe Lys He Phe Lys Asn Gly Asn He Ser 420 425 430 Phe Arg Pro He Ser Arg Leu Asn Val Pro? Rg Glu Phe Trp Tyr Leu 435 440 445 Asn He Asp Tyr Phe Arg His Wing Asn Arg Ser Gly Leu Thr Glu Glu 450 455 460 Glu He Leu He Leu Asn Asn He Ser Val Asp Val Arg Lys Leu Cys 465 470 475 480 Wing Glu Arg Wing Cys Asn Thr Leu Pro Being Wing Lys Arg Phe Ser Lys 485 490 495 Asn His Lys Ser Asn He Gln Be Ser Arg Gln Glu Arg Arg He Lys 500 505 510 Asp Pro Leu Val Val Leu Lys Asp Thr Leu Tyr Glu Phe Gln His Lys 515 520 525 Arg Wing Gly Trp Gly Ser Arg Ser Thr Arg Asp Leu Gly Ser Arg Ala 530 535 540 Asp His Ala Lys Gly Ser Gly 545 550 and a molecular weight of about 61 to about 65 kDa, preferably about 63 kDa.

Yet another DNA molecule of the present invention (GLRaV-2 0RF5) includes nucleotides 12844-13515 of SEQ. ID. No .: 1, and codes for a diverged coating protein. This DNA molecule comprises a nucleotide sequence corresponding to SEQ. ID. No .: 12, as follows: ATGAGTTCCA ACACAAGCGT GCCGGTTGGG GGTCTCGAAG CACTCGAGAC CTCGGGAGTC 60 GTGCTGACCA CGCGAAAGGA AGCGGTTGAT AAGTTTTTTA ATGAACTAAA AAACGAAAAT 120 TACTCATCAG TTGACAGCAG CCGATTAAGC GATTCGGAAG TAAAAGAAGT GTTAGAGAAA 180 AGTAAAGAAA GTTTCAAAAG CGAACTGGCC TCCACTGACG AGCACTTCGT CTACCACATT 240 ATATTTTTCT TAATCCGATG TGCTAAGATA TCGACAAGTG AAAAGGTGAA GTACGTTGGT 300 AGTCATACGT ACGTGGTCGA CGGAAAAACG TACACCGTTC TTGACGCTTG GGTATTCAAC 360 ATGATGAAAA GTCTCACGAA GAAGTACAAA CGAGTGAATG GTCTGCGTGC GTTCTGTTGC 420 GCGTGCGAAG ATCTATATCT AACCGTCGCA CCAATAATGT CAGAACGCTT TAAGACTAAA 480 GCCGTAGGGA TGAAAGGTTT GCCTGTTGGA AAGGAATACT TAGGCGCCGA CTTTCTTTCG 540 GGAACTAGCA AACTGATGAG CGATCACGAC AGGGCGGTCT CCATCGTTGC AGCGAAAAAC 600 GCTGTCGATC GTAGCGCTTT CACGGGTGGG GAGAGAAAGA TAGTTAGTTT GTATGATCTA 660 GGGAGGTACT AA 672 The diverged coat protein has an amino acid sequence corresponding to SEQ. ID. No .: 13, as follows: Met Ser Ser Asn Thr Ser Val Pro Val Gly Gly Leu Glu Ala Leu Glu 1 5 10 15 Thr Ser Gly Val Val Leu Thr Arg Lys Glu Val Val Asp Lys Phe 20 25 30 Phe Asn Glu Leu Lys Asn Glu Asn Tyr Ser Val Asp Ser Ser Arg 35 40 45 Leu Ser Asp Ser Glu Val Lys Glu Val Leu Glu Lys Ser Lys Glu Ser 50 55 60 Phe Lys Ser Glu Leu Wing Ser Thr Asp Glu His Phe Val Tyr llis He 65 70 75 80 He Phe Phe Leu He Arg Cys Wing Lys He Ser Thr Ser Glu Lys Val 85 90 95 Lys Tyr Val Gly Ser His Thr Tyr Val Val Asp Gly Lys Thr Tyr Thr 100 105 110 Val Leu Asp Wing Trp Val Phe As Met Met Met Lys Ser Leu Thr Lys Lys 115 120 125 Tyr Lys Arg Val Asn Gly Leu Arg Wing Phe Cys Cys Wing Cys Glu Asp 130 135 140 Leu Tyr Leu Thr Val? Pro He Met Ser Glu Arg Phe Lys Thr Lys 145 150 155 160 Wing Val Gly Met Lys Lys Gly Leu Pro Val Gly Lys Glu Tyr Leu Gly Wing 165 170 175 Asp Phe Leu Ser Gly Thr Ser Lys Leu Met Ser Asp His Asp Arg Wing 180 185 190 Val Ser He Val Wing Wing Lys Asn Wing Val Asp Arg Ser Wing Phe Thr 195 200 205 G and Gly Glu Arg Lys He Val Ser Leu Tyr Asp Leu Gly Arg Tyr 210 215 220 and a molecular weight of about 23 to about 27 kDa, preferably about 25 kDa. Another DNA molecule (GLRaV-2 0RF6) includes nucleotides 13584-14180 of SEQ. ID. No .: 1, and encodes for a vine leaf winding virus coating protein. This DNA molecule comprises a nucleotide sequence corresponding to SEQ. ID. No .: 14, as follows: ATGGAGTTGA TGTCCGACAG CAACCTTAGC AACCTGGTGA TAACCGACGC CTCTAGTCTA 60 AATGGTGTCG ACAAGAAGCT TTTATCTGCT GAAGTTGAAA A? ATGTTGGT GCAGAAAGGG 120 GCTCCTAACG AGGGTATAGA AGTGGTGTTC GGTCTACTCC TTTACGCACT CGCGGCAAGA 180 ACCACGTCTC CTAAGGTTCA GCGCGCAGAT TCAGACGTTA TATTTTCAAA TAGTTTCGGA 240 GAGAGGAATG TGGTAGTAAC AGAGGGTGAC CTTAAGAAGG TACTCGACGG GTGTGCGCCT 300 CTCACTAGGT TCACTAATAA AC TAGAACG TTCGGTCGTA CTTTCACTGA GGCTTACGTT 360 GACTTTTGTA TCGCGTATAA GCACAAATTA CCCCAACTCA ACGCCGCGGC GGAATTGGGG 420 ATTCCAGCTG AAGATTCGTA CTTAGCTGCA GATTTTCTGG GTACTTGCCC GAAGCTCTCT 480 GAATTACAGC AAAGTAGGAA GATGTTCGCG AGTATGTACG CTCTAAAAAC TGAAGGTGGA 540 GTGGTAAATA CACCAGTGAG CAATCTGCGT CAGCTAGGTA GAAGGGAAGT TATGTAA 597 The coating protein has an amino acid sequence corresponding to SEQ. ID. No .: 15, as follows: Met Glu Leu Met Being Asp Being Asn Leu Being Asn Leu Val He Thr Asp 1 5 10 15 Wing Being Ser Leu Asn Gly Val Asp Lys Lys Leu Leu Ser Wing Glu Val 20 25 30 Glu Lys Met Leu Val Gln Lys Gly Wing Pro Asn Glu Gly He Glu Val 35 40 45 Val Phe Gly Leu Leu Leu Tyr Ala Leu Ala Wing Arg Thr Thr Ser Pro 50 55 60 Lys Val Gln Arg Wing Asp Ser Asp Val He Phe Ser Asn Ser Phe Gly 65 70 75 80 Glu Arg Asn Val Val Val Thr Glu Gly Asp Leu Lys Lys Val Leu Asp 85 90 95 Gly Cys Ala Pro Leu Thr Arg Phe Thr Asn Lys Leu Arg Thr Phe Gly 100 105 110 Arg Thr Phe Thr Glu Wing Tyr Val Asp Phe Cys He Ala Tyr Lys His 115 120 125 Lys Leu Pro Gln Leu Asn Wing Wing Wing Glu Leu Gly He Pro Wing Glu 130 135 140 Asp Ser Tyr Leu Wing Wing Asp Phe Leu Gly Thr Cys Pro Lys Leu Ser 145 150 155 160 Glu Leu Gln Gln Ser Arg Lys Met Phe Ala Ser Met Tyr Ala Leu Lys 165 170 175 Thr Glu Gly Gly Val Val Asn Thr Pro Val Ser Asn Leu Arg Gln Leu 180 185 190 Gly Arg Arg Glu Val Met 195 and a molecular weight of about 20 to about 24 kDa, preferably about 22 kDa. -6Í- Another DNA molecule (GLRaV-2 0RF7) includes nucleotides 14180-14665 of SEQ. ID. No.: 1, and encodes a second undefined protein or polypeptide of the vine leaf winding virus. This DNA molecule comprises a nucleotide sequence corresponding to SEQ. ID. No .: 16, as follows: ATGGAAGATT ACGAAGAAAA ATCCGAATCG CTCATAGTGC TACGCACGAA TCTGAACACT 60 ATGCTTTTAG TGGTCAAGTC CGATGCTAGT GTAGAGCTGC CTAAACTACT AATTTGCGGT 120 TACTTACGAG TGTCAGGACG TGGGGAGGTG ACGTGTTGCA ACCGTGAGGA ATTAACAAGA 180 GATTTTGAGG GCAATCATCA TACGGTGATC CGTTCTAGAA TCATACAATA TGACAGCGAG 240 TCTGCTTTTG AGGAATTCAA CAACTCTGAT TGCGTAGTGA AGTTTTTCCT AGAGACTGGT 300 AGTGTCTTTT GGTTTTTCCT TCGAAGTGAA ACCAAAGGTA GAGCGGTGCG ACATTTGCGC 360 ACCTTCTTCG AAGCTAACAA TTTCTTCTTT GGATCGCATT GCGGTACCAT GGAGTATTGT 420 TTGAAGCAGG TACTAACTGA AACTGAATCT ATAATCGATT CTTTTTGGGA AGAAAGAAAT 480 CGTTAA 486The second undefined protein or polypeptide of the vine leaf winding virus has a deduced amino acid sequence corresponding to SEQ. ID. No .: 17, as follows: Met Glu Asp Tyr Glu Glu Lys Ser Glu Be Leu He Leu Leu Arg Thr 1 5 10 15 Asn Leu Asn Thr Met Leu Leu Val Val Lys Ser Asp Ala Ser Val Glu 20 25 30 Leu Pro Lys Leu Leu He Cys Gly Tyr Leu Arg Val Ser Gly Arg Gly 35 40 45 Glu Val Thr Cys Cys Asn Arg Glu Glu Leu Thr Arg Asp Phe Glu Gly 50 55 60 Asn His His Thr Val He Arg Ser Arg He He Gln Tyr Asp Ser Glu 65 70 75 80 Ser Ala Phe Glu Glu Phe Asn Asn As Asp Cys Val Val Lys Phe Phe 85 90 95 Leu Glu Thr Gly Ser Val Phe Trp Phe Phe Leu Arg Ser Glu Thr Lys 100 105 110 Gly Arg Ala Val Arg His Leu Arg Thr Phe Phe Glu Wing Asn Asn Phe 115 120 125 Phe Phe Gly Ser His Cys Gly Thr Met Glu Tyr Cys Leu Lys Gln Val 130 135 140 Leu Thr Glu Thr Glu Ser He He Asp Ser Phe Cys Glu Glu Arg Asn 145 150 155 160 Arg and a molecular weight of about 17 to about 21 kDA, preferably about 19 kDa. Yet another DNA molecule (GLRaV-2 ORF8) includes nucleotides 14667-15284 of SEQ. ID. No .: 1, and codes for a third undefined protein or polypeptide of the vine leaf winding virus. This DNA molecule comprises a nucleotide sequence corresponding to SEQ ID. No .: 18, as follows: ATGAGGGTTA TAGTGTCTCC TTATGAAGCT GAAGACATTC TGAAAAGATC GACTGACATG 60 TTACGAAACA TAGACAGTGG GGTCTTGAGC ACTAAAGAAT GTATCAAGGC ATTCTCGACG 120 ATAACGCGAG ACCTACATTG TGCGAAGGCT TCCTACCAGT GGGGTGTTGA CACTGGGTTA 180 TATCAGCGTA ATTGCGCTGA AA? ACGTTTA ATTGACACGG TGGAGTCAAA CATACGGTTG 240 GCTCAACCTC TCGTGCGTGA AAAAGTGGCG GTTCATTTTT GTAAGGATGA ACCAAAAGAG 300 CTAGTAGCAT TCATCACGCG AAAGTACGTG GAACTCACGG GCGTGGGAGT GAGAGAAGCG 360 GTGAAGAGGG AAATGCGCTC TCTTACCAAA ACAGTTTTAA ATAAAATGTC TTTGGAAATG 420 GCGTTTTACA TGTCACCACG AGCGTGGAAA AACGCTGAAT GGTTAGAACT A? AATTTTCA CCTGTGAAA 480? TCTTTAGAGA TCTGCTATTA GACGTGGAAA CGCTCAACGA ATTGTGCGCC 540 GAAGATGATG TTCACGTCGA CAAAGTAAAT GAGAATGGGG ACGAAAATCA CGACCTCGAA 600 CTCCAAGACG AATGTTAA 618 The third protein or undefined polypeptide has a deduced amino acid sequence corresponding to SEQ. ID. No .: 19, as follows: Met Arg Val He Val Ser Pro Tyr Glu Wing Glu Asp He Leu Lys Arg 1 5 10 15 Ser Thr Asp Met Leu Arg Asn He Asp Ser Gly Val Leu Ser Thr Lys 20 25 30 Glu Cys He Lys Wing Phe Ser Thr He Thr Arg Asp Leu His Cys Wing 35 40 45 Lys Wing Being Tyr Gln Trp Gly Val Asp Thr Gly Leu Tyr Gln Arg Asn 50 55 60 Cys Wing Glu Lys Arg Leu He Asp Thr Val Glu Ser? Sn He Arg Leu 65 70 75 80 Wing Gln Pro Leu Val Arg Glu Lys Val Wing Val His Phe Cys Lys Asp 85 90 95 Glu Pro Lys Glu Leu Val Wing Phe He Thr Arg Lys Tyr Val Glu Leu 100 105 110 Thr Gly Val Gly Val Arg Glu Wing Val Lys Arg Glu Met Arg Ser Leu 115 120 125 Thr Lys Thr Val Leu Asn Lys Met Ser Leu Glu Met Wing Phe Tyr Met 130 135 140 Ser Pro Arg Wing Trp Lys Asn Wing Glu Trp Leu Glu Leu Lys Phe Ser 145 150 155 160 Pro Val Lys He Phe Arg Asp Leu Leu Leu Asp Val Glu Thr Leu Asn 165 170 175 Glu Leu Cys Wing Glu Asp Asp Val His Val Asp Lys Val Asn Glu Asn 180 185 190 Gly Asp Glu Asn His Asp Leu Glu Leu Gln Asp Glu Cys 195 200 205 and a molecular weight of about 22 to about 26 kDa, preferably about 24 kDa.

Another DNA molecule of the present invention (GLRaV-2 3 'UTR) includes nucleotides 15285-15500 of SEQ. ID. No .: 1, and comprises a nucleotide sequence corresponding to SEQ. ID. No .: 23, as follows: ACATTGGTTA AGTTTAACGA AAATGATTAG TAAATAATAA ATCGAACGTG GGTGTATCTA 60 CCTGACGTAT CAACTTAAGC TGTTACTGAG TAATTAAACC AACAAGTGTT GGTGTAATGT 120 GTATGTTGAT GTAGAGAAAA ATCCGTTTGT AGAACGGTGT TTTTCTCTTC TTTATTTTTA 180 AAAAAAAAAT AAAAAAAAAA AAAAAAAAGC GGCCGC 216 The present invention also encompasses fragments of the DNA molecules of the present invention. Suitable fragments capable of imparting resistance to vine leaf winding to grape plants, are constructed by using appropriate restriction sites, revealed by inspecting the sequence of the DNA molecule, to: (i) insert an interposon (Felley et al., "Interposon Mutagenesis of Soil and Water Bacteria: A Family of DNA Fragments Designed for in vitro Insertion Mutagenesis of Gram-negative Bacteria ", Gene, 52: 147-15 (1987), which is incorporated herein by reference), in such a way that truncated forms of the polypeptide or vine leaf roll virus coating, lacking different amounts of the C term; or (ii) suppressing several internal portions of the protein. Alternatively, the sequence can be used to amplify any portion of the coding region, such that it can be cloned into a vector that delivers both transcription initiation and translation signals. Suitable DNA molecules are those that hybridize to a DNA molecule comprising a nucleotide sequence of at least 15 continuous bases of the SEQ. ID. No.:l under stringent conditions, characterized by a hybridization regulator comprising 0.9M sodium citrate regulator ("SSC"), at a temperature of 37 ° C, and which remain fixed when subjected to washing with SSC regulator at 37 ° C; and preferably in a hybridization regulator comprising 20% formamide in 0.9M serum / 0.9M SSC regulator, at a temperature of 42 ° C, and which remain fixed when subjected to a 42 ° C wash with SSC 0.2 regulator. xa 42 ° C. The variants also (or alternatively) can be modified by, for example, suppressing or adding nucleotides that have minimal influence on the properties, secondary structure, and hydropathic nature of the encoded protein or polypeptide. For example, nucleotides encoding a polypeptide can be conjugated to a signal sequence (or leader) at the N-terminus of the protein, which directs, in a co-translational or post-translational manner, the transfer of the protein. The nucleotide sequence can also be altered, such that the encoded polypeptide is conjugated with a linker or other sequence for ease of synthesis, purification or identification of the polypeptide. The protein or polypeptide of the present invention is preferably produced in a purified form (preferably, at least about 80 percent, more preferably 90 percent pure) by conventional techniques. Normally, the protein or polypeptide of the present invention is isolated by lysate and sonication. After washing, the lysate granule is resuspended in a regulator containing Tris-HCl. During dialysis, a precipitate is formed from this protein solution. The solution is centrifuged, and the granule is washed and resuspended in the regulator which contains Tris-HCl. The proteins are resolved by electrophoresis through an SDS / 12 percent polyacrylamide gel. The DNA molecule encoding the vine leaf winding virus (Type 2) protein or polypeptide of the present invention can be incorporated into cells using conventional recombinant DNA technology. In general, this involves inserting the DNA molecule into an expression system for which the DNA molecule is heterologous (ie, not normally present). The heterologous DNA molecule is inserted into the expression system or into the vector in orientation in the proper sense, and in the correct reading frame. The vector contains the necessary elements for the transcription and translation of the coding sequences of the inserted protein. U.S. Patent No. 4,237,224 to Cohen and Boyer, which is incorporated herein by reference, discloses the production of expression systems in the form of recombinant plasmids, using cleavage with restriction enzyme, and ligament with ligase from DNA These recombinant plasmids are then introduced by transformation, and replicated in unicellular cultures that include prokaryotic organisms and eukaryotic cells grown in culture. Recombinant genes can also be introduced into viruses, such as vaccinia virus. Recombinant viruses can be generated by transfection of plasmids in cells infected with the virus. Suitable vectors include, but are not limited to, the following viral vectors, such as the lambda gtll vector system, gt WES.tB, Charon 4, and the plasmid vectors, such as pBR322, pBR325, pACYC177, pACYC184, pUC8 , pUC9, pUCld, pUC19, pLG339, pR290, pKC37, pKClOl, SV 40, pBluescript II SK +/- or KS +/- (see "Stratagene Cloning Systems" Catalog (1993) by Stratagene, La Jolla, Calif., gue the pQE, pIH821, pGEX, pET series is incorporated herein by reference) (see Studier et al., "Use of T7 RNA Polymerase to Direct Expression of Cloned Genes," Gene Expression Technology, volume 185 (1990), which is incorporated herein by reference). incorporated herein by reference), and any derivatives thereof. Recombinant molecules can be introduced into the cells by transformation, transduction, conjugation, mobilization, or electroporation. The DNA sequences are cloned into the vector using standard cloning procedures in the art, as described by Maniatis et al., Molecular Cloninq: A Laboratorv Manual, Cold Springs Laboratory, Cold Springs Harbor, New York (1982), which is incorporated herein by reference. A variety of host-vector systems can be used to express the coding sequences of the protein. Primarily, the vector system must be compatible with the host cell used. Host-vector systems include, but are not limited to, the following: bacteria transformed with the bacteriophage DNA, the plasmid DNA, or the cosmid DNA; microorganisms, such as yeast containing yeast vectors; mammalian cell systems infected with virus (e.g., vaccinia virus, adenovirus, etc.); insect cell systems infected with virus (eg, baculovirus); and plant cells infected by bacteria or transformed by particle bombardment (ie, biolistics). The expression elements of these vectors vary in their strengths and specificities. Depending on the host-vector system used, any of a number of suitable transcription and translation elements can be used.

Different genetic signals and processing events control many levels of gene expression (eg, transcription of DNA, and translation of messenger RNA ("mRNA")). The transcription of the DNA depends on the presence of a promoter, which is a DNA sequence that directs the binding of the RNA polymerase, and thus promotes the synthesis of the mRNA. The DNA sequences of the eukaryotic promoters differ from those of the prokaryotic promoters. In addition, eukaryotic promoters and accompanying genetic signals may not be recognized in, or may not function in, a prokaryotic system, and in addition, prokaryotic promoters are not recognized, and do not work in eukaryotic cells. Similarly, the translation of mRNA into priocariotes depends on the presence of the appropriate priocariotic signals, which differ from those of eukaryotes. Efficient translation of mRNA in prokaryotes requires a ribosome binding site called the Shine-Dalgarno ("SD") sequence on the mRNA. This sequence is a short nucleotide sequence of mRNA that is located before the start codon, usually AUG, which encodes the amino-terminal methionine of the protein. The SD sequences are complementary to the 3 'end of the 16S rRNA (ribosomal RNA), and probably promote the binding of the mRNA to the ribosomes, doubling with the rRNA to allow proper ribosome placement. For a review on the maximization of gene expression, see Roberts and Lauer, Methods in Enzymolosy, 68: 473 (1979), which is incorporated herein by reference. The promoters vary in their "strength" (that is, their ability to promote transcription). For the purposes of expressing a cloned gene, it is desirable to use strong promoters, in order to obtain a high level of transcription and, consequently, expression of the gene. Depending on the amphiprione cell system used, any of a number of suitable promoters can be used. For example, when cloning into E. coli, its bacteriophages, or plasmids, promoters, such as the phage T7 promoter, the lac promoter, the trp promoter, the recA promoter, the ribosomal RNA promoter, the PR and PL promoters of lambda coliphage and others, including, but not limited to, _ZacUV5, gmpF, bla, Ipp, and the like, can be used to direct high levels of transcription of adjacent DNA segments. Additionally, a hybrid trp-lacOV5 (tac) promoter or other E. coli promoters produced by recombinant DNA or other synthetic DNA techniques can be used to provide transcription of the inserted gene. Strains of bacterial host cells and expression vectors that inhibit the action of the promoter can be selected, unless specifically induced. In certain operons, the addition of specific inductors is necessary for efficient transcription of the inserted DNA. For example, the lac operon is induced by the addition of lactose or IPTG (thioisopropyl-beta-D-galactoside). A variety of other operons, such as trp, pro, etc., are under different controls. Specific initiation signals are also required for efficient transcription and translation of the gene in prokaryotic cells. These transcription and translation initiation signals may vary in "strength", as measured by the amount of specific messenger RNA of the gene and protein synthesized, respectively. The DNA expression vector containing a promoter can also contain any combination of different "strong" transcription and / or translation initiation signals. For example, efficient translation in E. coli requires a Shine-Dalgarno ("SD") sequence of approximately 7 to 9 bases 5 'of the start codon ("ATG") to provide a ribosome binding site. Accordingly, any combination of SD-ATG that can be used by the ribosomes of the host cell can be employed. These combinations include, but are not limited to, the SD-ATG combination from the ero gene, or the N gene from the lambda coliphage, or from the E, D, C, B or A triftophane genes of E. coli. Additionally, can any combination of SD-ATG produced by AD be used? recombinant or other techniques that involve the incorporation of synthetic nucleotides. Once the molecules of AD? isolated that encode the different proteins or polypeptides of vine leaf winding virus (Type 2), as described above, have been cloned into an expression system, are ready to be incorporated into a host cell. This incorporation can be carried out by the different transformation forms mentioned above, depending on the vector / host cell system. Suitable host cells include, but are not limited to, bacteria, virus, yeast, mammalian cells, insect, plant and the like. The present invention also relates to RNA molecules that encode the different vine leaf winding virus (Type 2) proteins or polypeptides described above. The transcripts can be synthesized using the host cells of the present invention, by any of the conventional techniques. The mRNA can be translated, either in vi tro or in vivo. Cell-free systems typically include wheat germ or reticulosite extracts. The live translation can be effected, for example, by microinjection in frog oocytes. One aspect of the present invention involves the use of one or more of the above DNA molecules that encode the different proteins or polypeptides of a vine leaf winding virus (Type 2), to transform vine plants, in order to impart resistance to the winding of the vine leaf to the plants. The mechanism by which resistance is imparted is not known. In a hypothetical mechanism, the transformed plant can express a protein or polypeptide from the vine leaf roll (Type 2), and, when the transformed plant is inoculated with the leaf vine winding virus, such as GLRaV-1, GLRaV -2, GLRaV-3, GLRaV-4, GLRaV-5 or GLRaV-6, or combinations thereof, the expressed protein or polypeptide prevents translation of the viral DNA. In this aspect of the present invention, the target DNA molecule incorporated in the plant can be expressed in a constitutive manner. Alternatively, the expression can be regulated by a promoter that is activated by the presence of vine leaf winding virus. Suitable promoters for these purposes include those from genes expressed in the response to infiltration of vine leaf winding virus. The isolated DNA molecules of the present invention can be used to impart resistance to vine leaf winding virus for a wide variety of grapevine plants. DNA molecules are particularly suitable for imparting resistance to shoot cultures or Vitis root rhizome. The crops of shoots that can be protected include those commonly referred to as Table Grapes or Raisins, such as Almeria, Anab-E-Shahi, Autumn Black, Beauty Seedless, Black Corinth, Black Damascus, Black Malvoisie, Black Prince, Blackro-se , Bronx Seedless, Burgrave, Calmeria, Campbell Early, Canner, Cardinal, Catawba, Christmas, Concord, Dattier, Delight, Diamond, Dizmar, Duchess, Early Muscat, Emerald Seedless, Emperor, Exotic, Ferdinand de Lesseps, Feast, Flame seedless, Flame Tokay, Gasconade, Gold, Himrod, Hunisa, Hussiene, Isabella, Italy, July Muscat, Khandahar, Katta, Kourgane, Kishmishi, Loo Perlette, Malaga, Monukka, Muscat of Alexandria, Muscat Flame, Muscat Hamburg, New York Muscat, Niabell , Niagara, Olivette blanche, Ontario, Pierce, Queen, Red Malaga, Ribier, Rish Baba, Romulus, Ruby Seedless, Schuyler, Seneca, Suavis (IP 365), Thompson seedless, and Thomuscat. They also include those used in the production of wine, such as Aleatico, Alicante Bouschet, Aligote, Alvarelhao, Aramon, Baco blanc (22A), Burger, Cabernet franc, Cabernet, Sauvignon, Calzin, Carignane, Charbono, Chardonnay, Chasselas dore, Chenin blanc, Clairette blanche, Early Burgundy, Emerald Riesling, Feher Szagos, Fernao Pires, Flora, French Colombard, Freesia, Furmint, Gamay, Gewurztraminer, Grand noir, Gray Riesling, Green Hungarian, Green Veltliner, Grenache, Cricket, Helena, Inzolia, Lagrein, Lambrusco de Salamino, Malbec, Malvasia bianca, Mataro, Melon, Merlot, Meunier, Mission, Montua de Pilas, Muscadelle du Bordelais, Muscat blanc, Muscat Ottonel, Muscat Saint-Vallier, Nebbiolo, Nebbiolo fino, Nebbiolo Lampia, Orange Muscat, Palomino, Pedro Ximenes, Petit Bouschet, Petite Sirah, Peverella, Pinot noir, Pinot Saint-George, Primitivo di Gioa, Red Veltliner, Refosco, Rkatsiteli, Royalty, Rubired, Ruby Cabernet, Saint-Emilion, Saint Macaire, Salvador, Sangiovese, Sauvignon blanc, Sauvignon gris, 16 Sauvignon vert, Scarlet, Seibel 5279, Seibel 9110, Seibel 13053, Semillon, Servant, Shiraz, Souzao, Sultana Crimson, Sylvaner, Tannat, Teroldico, Ink Madeira, Red wine, Touriga, Traminer, Trebbiano Toscano, Trousseau, Valdepeñas, Viognier, Walschries-ling, White Riesling, and Zinfandel. Root rhizome crops that can be protected include Couderc 1202, Couderc 1613, Couderc 1616, Couderc 3309, Dog Ridge, Foex 33 EM, Freedom, Ganzin 1 (A x R # 1), Harmony, Kober 5BB, LN33, Millardet & from Grasset 41B, Millardet & from Grasset 420A, Millardet & from Grasset 101-14, Oppenheim 4 (S04), Paulsen 775, Paulsen 1045, Paulsen 1103, Richter 99, richter 110, Riparia Glorie, Ruggeri 225, Saint-George, Salt Creek, Teleki 5A, Vitis rupestris Constantia, Vitis california, and Vi tis girdiana. There is a wide similarity in the sequence regions related to hsp70 of GLRaV-2 and other closteroviruses, such as the Tristeza virus and the yellow beet virus. Accordingly, the gene related to hsp70 of GLRaV-2 can also be used to produce transgenic plants or crops other than grapes, such as citrus or sugar beet, which are resistant to closteroviruses other than vine leaf wrapping, such as Sadness virus and yellow beet virus. Suitable citrus crops include lemon, lime, orange, grapefruit, pineapple, tangerine, and the like, such as Joppa, Mal taise Ovale, Parson (Parson Brown), Pear, Pineapple, Queen, Shamouti, Valencia, Tenerife, Imperial Dobl Fine, Washington Sanguine, Moro, Sanguinello Mosca to, Spanish Sanguine-lli, Tarocco, Atwood, Australian, Bahia, Baiana, Cram, Dalmau, Eddy, Fisher, Frost Washington, Gillete, LengNavelina, Washington, Satsuma Mandarin, Dancy, Robinson, Ponkan, Duncan, Marsh, Pink Marsh, Ruby Red, Red Seedless, Smooth Seville, Orlando Tangelo, Eureka, Lisbon, Meyer Lemon, Rough Lemon, Sour Orange, Persxan Lime, West Indian Lime, Bearss, Sweet Lime, Trox Cxtrange, and Citrus Trifolxata. Each of these citrus crops is suitable for producing transgenic citrus plants resistant to the Tristeza virus. The economically important species of sugar beet is Beta vulgaris L. , which has four important types of crops: sugar beet, table beet, fodder beet, and Swiss chard. Each of these beet crops is suitable for producing transgenic beet plants resistant to yellow beetle virus, as described above. Because it has been known that GLRaV-2 infects tobacco plants (e.g., Nxcotiana benthamiana), it is also desirable to produce transgenic tobacco plants that are resistant to vine leaf winding viruses, such as GLRaV-2. . The plant tissue suitable for transformation includes leaf tissue, root tissue, meristems, zygotic and somatic embryos, and anthers. It is particularly preferred to use embryos obtained from anther cultures. The expression system of the present invention can be used to transform virtually any plant tissue under suitable conditions. Transformed tissue cells according to the present invention can be cultured in vitro in a suitable medium, to impart resistance to the vine leaf winding virus. The transformed cells can be regenerated in whole plants, such that the protein or polypeptide imparts resistance to the vine leaf winding virus in the intact transgenic plants. In any case, the plant cells transformed with the recombinant DNA expression system of the present invention are cultured and made to express the DNA molecule to produce one of the vine leaf winding virus proteins or polypeptides. described above and, therefore, to impart resistance to vine leaf winding virus. In the production of transgenic plants, the construction of DNA in a vector described above, can be directly injected into the plant cells by the use of micropipettes, to mechanically transfer the recombinant DNA. Crossway, Mol. Gen. Genetics, 202: 179-85 (1985), which is incorporated herein by reference. The genetic material can also be transferred to the plant cell using polyethylene glycol. Krens, et al., Nature, 296: 72-74 (1982), which is incorporated herein by reference. Another technique for transforming plants with DNA molecules according to the present invention, it is by contacting the tissue of these plants with an inoculum of a bacterium transformed with a vector comprising a gene according to the present invention, imparting vine leaf winding resistance. In general, this procedure involves inoculating the plant tissue with a suspension of bacteria, and incubating the tissue for 48 to 72 hours on a regeneration medium without antibiotics at 25-28 ° C. Bacteria of the genus Agrobacterium can be used to transform plant cells. Suitable species of this bacterium include Agrobacterium tumefaciens and Agrobacterium rhizogenes. Agrobacterium tumefaciens (for example, strains C58, LBA4404, or EHA105) is particularly useful, due to its well-known ability to transform plants. The heterologous genetic sequences can be introduced into appropriate plant cells, by means of the Ti plasmid of A. tumefaciens or of the Ri plasmid of A. rhizogenes. The Ti or Ri plasmid is transmitted to plant cells after infection by Agrobacterium, and is stably integrated into the genome of the plant. J. Schell, Science, 237: 1176-83 (1987), which is incorporated herein by reference. After transformation, the transformed plant cells must be regenerated. The regeneration of plants from cultured protoplasts is described by Evans et al., Handbook of Plant Cell Cultures, Volume 1: (MacMillan Publishing Co., New York, 1983); and Vasil I.R. (ed.), Cell Culture and Somatic Cell Genetics of Plants, Acad. Press, Orlando, Volume I, 1984, and Volume III (1986), which are incorporated herein by reference. It is known that practically all plants can be regenerated from cultured cells or tissues, including, but not limited to, all major species of sugarcane, sugar beet, cotton, fruit trees and legumes. The means for regeneration vary from species to species of plants, but in general, a suspension of transformed protoplasts, or a Petri dish containing explants, is first provided. Callus tissue is formed, and buds can be induced from callus, and subsequently rooted. Alternatively, the formation of the embryo in the callus tissue can be induced. These embryos germinate as natural embryos to form plants. The culture medium will generally contain different amino acids and hormones, such as auxin and cytokinins. It is also convenient to add glutamic acid and proline to the medium. An efficient regeneration will depend on the medium, the genotype, and the history of the crop. If these three variables are controlled, then regeneration is usually reproducible and repeatable. After the expression cassette is stably incorporated into the transgenic plants, it can be transferred to other plants by sexual cross. Any one of a number of conventional breeding techniques can be used, depending on the species to be crossed. Once such transgenic plants are produced, the plants themselves can be cultured according to the conventional procedure, such that the DNA construct is present in the resulting plants. In an alternative way, the transgenic seeds are recovered from the transgenic plants. Then these seeds can be planted in the soil, and can be grown using conventional procedures to produce transgenic plants. Another approach to transforming plant cells with a gene that imparts resistance to pathogens is particle bombardment (also known as biolistic transformation) of the host cell. This can be done in one of several ways. The first involves propelling inert or biologically active particles to the cells. This technique is disclosed in U.S. Patent Nos. 4,945,050; 5,036,006 and 5,100,792, all to Sanford et al., And to Emerschad et al., "Somatic Embryogenesis and Plant Development from Immature Zygotic Embryos of Seedless Grapes (Vitis vini f era)", Plant Cell Reports, 14: 6-12 (1995) ( "Emerschad (1995)"), which are incorporated herein by reference. In general, this method involves propelling inert or biologically active particles to the cells, under effective conditions to penetrate the external surface of the cell, and to be incorporated into the interior thereof. When inert particles are used, the vector can be introduced into the cell by coating the particles with the vector containing the heterologous DNA. In an alternative way, the target cell can be surrounded with the vector, such that the vector is brought into the cell upon the awakening of the particle. Biologically active particles (eg, dried bacterial cells containing the vector and heterologous DNA) can also be propelled into the plant cells. Once a grape plant tissue, a citrus plant tissue, a beet plant tissue, or a tobacco plant tissue plant is transformed, in accordance with the present invention, the transformed tissue is regenerated to form a transgenic plant. In general, regeneration is carried out by culturing the transformed tissue on a medium containing the appropriate growth regulators and nutrients to allow initiation of the shoot meristems. Appropriate antibiotics are added to the regeneration medium to inhibit the growth of Agrobacterium, and to select the development of the transformed cells. Following the initiation of the outbreak, the shoots are allowed to develop tissue culture, and are selected to determine the activity of the marker gene. The DNA molecules of the present invention can be made capable of being transcribed to a messenger RNA, which, although coding for a vine leaf winding protein or polypeptide (Type 2), does not move to the protein. This is known as RNA-mediated resistance. When a culture of shoots or rhizomes of Vitis, or a citrus, beet or tobacco crop, is transformed with this DNA molecule, the DNA molecule can be transcribed under effective conditions to keep the messenger RNA in the plant cell in readings of low level density. Density readings of between 15 and 50 are preferred, using a Hewlett ScanJet and an Image Analysis Program. A portion of one or more DNA molecules of the present invention, as well as other DNA molecules, may be used in a transgenic grape plant, citrus plant, beet plant or tobacco plant, in accordance with the patent application of the United States Serial No. 09 / 025,635, which is incorporated herein by reference. The vine leaf winding virus (type 2) protein or polypeptide of the present invention can also be used to reproduce antibodies or fixative portions thereof or probes. The antibodies can be monoclonal or fixative portions thereof or probes. The antibodies can be monoclonal or polyclonal. The production of monoclonal antibodies can be effected by techniques that are well known in the art. Basically, the process involves first obtaining immune cells (lymphocytes) from the spleen of a mammal (e.g., mouse) that has been previously immunized with the antigen of interest, either in vivo or in vitro. Then the lymphocytes that secrete antibodies are fused with myeloma (mouse) cells or transformed cells, which are capable of replicating indefinitely in the cell culture, thus producing an immortal immunoglobulin-secreting cell line. The resulting fused cells, or hybridomas are cultured, and the resulting colonies are screened for the production of the desired monoclonal antibodies. The colonies that produce these antibodies are cloned, and cultured, either in vivo or in vitro, to produce large amounts of antibody. A description of the theoretical basis and practical methodology of fusing these cells is stipulated in Kohler and Milstein, Nature, 256: 495 (1975), which is incorporated herein by reference. Mammalian lymphocytes are immunized by in vivo immunization of the animal (e.g., a mouse) with the protein or polypeptide of the present invention. These immunizations are repeated as necessary at intervals of up to several weeks, to obtain a sufficient titration of antibodies. After the last antigen reinforcement, the animals are sacrificed, and the spleen cells are removed. Fusion with cells with mammalian myeloma or other fusion partners capable of replicating indefinitely in cell culture, is effected by conventional and well-known techniques, for example, by the use of polyethylene glycol ("PEG") or other fusion agents. (See Milstein and Kohler, Eur. J. Immunol., 6: 511 (1976), which is incorporated herein by reference.) This immortal cell line, which is preferably murine, but which can also be derived from other mammalian species, including, but not limited to, rats and humans, are selected to be deficient in the enzymes necessary for the utilization of certain nutrients, to be able to have rapid growth, and to have a good melting capacity Many of these cell lines are known to those skilled in the art., and others are described regularly. Methods for reproducing polyclonal antibodies are also well known. Typically, these antibodies can be reproduced by administering the protein or polypeptide of the present invention subcutaneously to New Zealand white rabbits, which have been first bled to obtain a pre-immune serum. The antigens can be injected in a total volume of 100 microliters per site in six different sites. Each injected material will contain synthetic pluronic acid polyols of synthetic surfactant, or powdered acrylamide gel containing the protein or polypeptide after electrophoresis in SDS-polyacrylamide gel. The rabbits are then bled two weeks after the first injection, and are periodically boosted with the same antigen three times every six weeks. A serum sample is then collected 10 days after each boost. The polyclonal antibodies are then recovered from the serum by affinity chromatography, using the corresponding antigen to capture the antibody. Finally, the rabbits are euthanized with pentobarbital, 150 milligrams / kilogram, intravenously. This and other methods for reproducing polyclonal antibodies are disclosed in Harlow et al., Editors, Antibodies: A Laboratory Manual (1998), which is incorporated herein by reference. In addition to using whole antibodies, binding portions of these antibodies can be used. These fixative portions include Fab (Fab ') 2 fragments, and Fv fragments. These antibody fragments can be made by conventional methods, such as proteolytic fragmentation procedures, as described in Goding, Monoclonal antibodies: Principles and Practice, New York: Academic Press, pages 98-118 (1983), which is incorporated into the - $ 1 present as reference). The present invention also relates to probes that are found in nature, or synthetically prepared by recombinant DNA methods. Suitable probes are molecules that bind to the vine leaf winding viral antigens (Type 2) identified by the polyclonal antibodies of the present invention. These probes can be, for example, probes of proteins, peptides, lectins or nucleic acid. The antibodies or fixative portions thereof or the probes can be administered to suckers cultures or rhizome cultures infected with vine leaf winding virus. Alternatively, at least the binding portions of these antibodies can be sequenced, and the coding DNA can be synthesized. The encoding DNA molecule can be used to transform plants together with a promoter that causes the expression of the encoded antibody when the plant is infected by vine leaf winding virus. In either case, the antibody or fixative portion thereof or the probe will bind to the virus, and will help prevent the usual leaf roll response. The antibodies reproduced against the GLRaV-2 proteins or polypeptides of the present invention, or the binding portions of these antibodies, can be used in a method for the detection of vine leaf winding viruses in a -g8-tissue sample, such as tissue (for example, of a shoot or rhizome) from a grape plant or a tobacco plant. Antibodies or fixative portions thereof, suitable for use in the detection method, include those reproduced against a helicase, a methyltransferase, a protease of the papain type, an RNA-dependent RNA polymerase, a heat shock protein 70 , a heat shock protein 90, a coat protein, a diverged coat protein, or other proteins or polypeptides according to the present invention. Any reaction of the sample with the antibody is detected using a test system that indicates the presence of vine leaf winding virus in the sample. A variety of test systems can be used, such as enzyme-linked immunosorbent assays, radioimmunoassays, gel diffusion precipitin reaction assays, immunodiffusion assays, agglutination assays, fluorescent immunoassays, protein A immunoassays, or immunoelectrophoresis assays. Alternatively, the vine leaf roll virus can be detected in this sample using a nucleotide sequence of the RNA molecule, or a fragment thereof, that codes for a protein or polypeptide of the present invention. The nucleotide sequence is provided as a probe in a nucleic acid hybridization assay, or in an amplification detection method of the gene (for example, using a polymerase chain reaction method). The nucleic acid probes of the present invention can be used in any nucleic acid hybridization assay system known in the art, including, but not limited to, Southern blots (Southern, EM, "Detection of Specific Sequences Among DNA Fragments Separated by Gel Electrophoresis ", J. Mol. Biol., 98: 503-17 (1975), which is incorporated herein by reference), Northern blots (Thomas, PS; "Hybridization of Denatured RNA and Small DNA Fragments Transferred to Nitrocellulose", Proc. Nat'l Acad. Sci. USA, 77: 5201-05 (1980), which is incorporated herein by reference), and Colony blots (Grunstein, M. et al., "Colony Hybridization: A Method for the Isolation of Cloned cDNAs that Contain a Specific Gene ", Proc. Nat'l Acad. Sci. USA, 72: 3961-65 (1975), which is incorporated herein by reference). Alternatively, the probes can be used in a method of detecting amplification of the gene (eg, a reaction in the polymerase chain). Erlich, H.A. and collaborators, "Recent Advances in the Polymerase Chain Reaction," Science 252: 1643-51 (1991), which is incorporated herein by reference. Any reaction with the probe is detected, so that the presence of the virus is indicated by a vine leaf roll in the sample. This detection is facilitated by providing a probe with the probe of the present invention. Suitable labels include a radioactive compound, a fluorescent compound, a chemiluminescent compound, an enzyme compound or other equivalent nucleic acid tags. Depending on the desired detection range, it is possible to use probes that have nucleotide sequences that correspond to the conserved or variable regions of the ORF or UTR. For example, to distinguish a vine leaf roll virus from other related viruses (eg, other closteroviruses), it is desirable to use probes containing nucleotide sequences corresponding to the most highly conserved sequences among all leaf roll viruses. of vine. Also, to distinguish between different vine leaf winding viruses (ie, GLRaV-2 from GLRaV-1, GLRaV-3, GLRaV-4, GLRaV-5 and GLRaV-6, it is desirable to use probes containing sequences of nucleotide corresponding to the less highly conserved sequences between the different vine leaf winding viruses The nucleic acid probes (DNA or RNA) of the present invention will hybridize to complementary GLRaV-2 nucleic acid under stringent conditions. In general, the stringent conditions are selected from about 50 ° C lower than the thermal melting point (Tm) for the specific sequences at a defined ionic strength and pH.Tm is the temperature (under defined ionic strength and pH) in which hybridizes 50 percent of the target sequence in a perfectly coupled probe.Tm depends on the conditions of the solution and the base composition of the probe, and can be calculated using the following equation: Tm = 79.8 ° C + (18.5 x Log [Na +]) + (58.4 ° C x% [G + C]) (820 / #bp in duplex) (0.5 x% formamide) You can also control a non-specific binding using any of a number of known techniques, such as, for example, blocking the membrane with solutions containing protein, adding RNA, DNA and heterologous SDS to the hybridization buffer, and RNAse treatment. The washing conditions are usually carried out at or below the astringency. In general, stringent conditions suitable for nucleic acid hybridization assays or genetic amplification detection methods are as stipulated above. You can also select more or less stringent conditions. Examples The following examples are provided to illustrate the embodiments of the present invention, but by no means are intended to limit its scope. Example 1 - Northern Hybridization The specificity of the selected clones was confirmed by Northern hybridization. Northern hybridization was performed after electrophoresis of GLRaV-2 dsRNA in a 1 percent non-denaturing agarose conditioning gel. The agarose gel was denatured by soaking in 50 mM NaOH containing 0.4 M NaCl for 30 minutes, and then neutralized with 0.1 M Tris HCl (pH 7.5) containing 0.5 M NaCl for another 30 minutes. RNA was stained in sandwich overnight on a Genescreen ™ Plus membrane (DuPont NEN Research Product) in 10 X SSC regulator, and hybridized as described in the manufacturer's instructions (DuPont, NEN). Example 2 - Sequencing and Sequence Analysis of Nucleotides and Amino Acids Assisted by Computer. The DNA inserts were sequenced in pBluescript SK + by using T3 and T7 primers for the terminal region sequence, and additional oligonucleotide primers designed according to the sequence known for the internal region sequence. Purification of the plasmid DNA was performed by a mini alkaline-lysis / PEG precipitation procedure described by the manufacturer (Applied Biosystems, Inc.). Nucleotide sequencing was performed on both strands of the cDNA using the Abl TaqDyeDeoxy Terminator Cycle Sequencing Kit (Applied Biosystems, Inc.). Automatic sequencing was performed on an ABI373 Automated Sequencer (Applied Biosystems, Inc.) at Cornell University, Geneva, NY.

The nucleotide sequences of GLRaV-2 were assembled and analyzed with the EditSeq and SeqMan program, respectively, of the DNASTAR package (Madison, Wl). The amino acid sequences deduced from the nucleotide sequences and their open coding reading frames were conducted using the MapDraw program. Multiple alignments of amino acid sequences, identification of amino acid sequences in consensus, and generation of phylogenetic trees were performed, using the Clustal method in the MegAlign program. The nucleotide and amino acid sequences of other closteroviruses were obtained with the Entrez Program; and sequence comparisons with non-redundant databases were searched with the Blast Program of the National Center for Biotechnology Information. Example 3 - Isolation of the dsRNA Several vines of Vitis vinifera, Pinot Noir variety infected with GLRaV-2 originating from a central New York vineyard, served as the source for the isolation of the dsRNA and the cloning of the cDNA. The dsRNA was extracted from the phloem tissue of infected vines according to the method described by Hu et al., "Characterization of Closterovirus-Like Particles Associated with Grapevine Leafroll Disease", J. Phytopatholoqy 128: 1-14 (1990), which incorporates this as a reference. The purification of the high molecular weight dsRNA (approximately 15 kb) was performed by electrophoretic separation of the total dsRNA on a 0.7 percent low melting point agarose gel, and phenol / chloroform extraction, following the method described. by Sambrook et al., Molecular Cloninq: A Laboratory Manual, 2nd edition, Cold Spring Harbor Laboratory Press, New York (1989), which is incorporated herein by reference. The concentration of dsRNA was estimated with ultraviolet fluorescent density of a dsRNA band stained with ethidium bromide, compared to a known concentration of DNA marker. Example 4 - Synthesis and Cloning of DNAs The synthesis of the cDNA was carried out following the method initially described by Jelkmann et al., "Cloning of Four Plant Viruses From Small Quantities of Double-Stranded RNA", Phytopatholoqy 79: 1250-53 (1989), and modified by Ling et al., "The Coat Protein Gene of Grapevine Leafroll Associated Closterovirus-3: Cloning, Nucleotide Sequencing and Expression in Transgenic Plants", Arch. Viroloqy 142: 1101-16 (1997), both of which are incorporated in the present as a reference. Approximately 100 nanograms of the high molecular weight dsRNA purified from the low melting point agarose gel were denatured in 20 mM methylmercuric hydroxide and incubated at room temperature for 10 minutes with 350 nanograms of random primers. The cDNA of the first strand was synthesized using bird myeloblastosis virus (AMV) reverse transcriptase. The cDNA of the second strand was obtained using RNAse H, and DNA polymerase I from E. coli. The double-stranded cDNA was made blunt-ended with T4 DNA polymerase, and ligated with EcoR I adapters. The cDNA, which had EcoR I adapters at the ends, was activated by kinase reaction, and ligated into arms prepared from Lambda ZAP II / EcoR I, following the manufacturer's instructions (Stratagene). The recombinant DNA was then packed in vitro in Gigapack® II packaging extract (Stratagene). The packed phage particles were amplified and titrated according to the manufacturer's instructions. Two kinds of probes were used to identify the specific clones of GLRaV-2 from the library. One type was prepared from the synthesized cDNA, which was amplified by reaction in the polymerase chain after ligation with the specific Uni-Amp ™ adapters of EcoR I (Clontech); and the other type was of DNA inserts or products of the reaction in the polymerase chain from already sequenced clones. Clones from the cDNA library were selected by colony-collation hybridization on the colonies / plates mesh membrane (NEN Research Product) with the probe described above. The probe was prepared by labeling with 32P [a-dATP] using the Klenow fragment of DNA polymerase I from E. coli. The steps of prehybridization, hybridization, and washing, were performed at 65 ° C according to the manufacturer's instructions (DuPont Research Product, NEN). The selected plates were converted to recombinant pBluescript by the live separation method according to the manufacturer's instructions (Stratagene). To obtain clones that will represent the 3 'terminus of GLRaV-2, the dsRNA was polyadenylated with yeast poly (A) polymerase. Using the dsRNA with poly (A) tail as template, the cDNA was amplified by reverse transcription polymerase chain reaction, with oligo (dT) 18 and a specific primer, CP-1 / T7R, which was derived from of clone CP-1, and having a nucleotide sequence according to SEQ. ID. No .: 20, as follows: TGCTGGAGCT TGAGGTTCTG C 21 The product resulting from the reaction in the polymerase chain (3 '-PCR) was cloned into a TA vector (Invitrogen), and sequenced. As shown in Figure IA, a high molecular weight dsRNA of approximately 15 kb was consistently identified from vines infected with GLRaV-2, but not from healthy vines. In addition, several low molecular weight dsRNAs were also detected from the infected tissue. The yield of GLRaV-2 dsRNA was estimated to be between 5 and 10 nanograms / 15 grams of phloem tissue, which was much lower than that of GLRaV-3 (Hu et al., "Characterization of Closterovirus-Like Particles Associated with Grapevine Leafroll Disease ", J. Phvtopatholoqy 128: 1-14 (1990), which is incorporated herein by reference). Only the high molecular weight dsRNA was used, which was purified from the low melting point agarose gel for cDNA synthesis, cloning, and the establishment of the Lambda / ZAP II cDNA library. Two kinds of probes were used for the selection of the cDNA library. The initial clones were identified by hybridization with amplified cDNA with reaction in the Uni-AmpMR polymerase chain as probes. The specificity of these clones (e.g. TC-1), which are from a size of 200 to 1,800 base pairs, was confirmed by Northern hybridization for GLADV-2 dsRNA, as shown in Figure IB. Additionally, more than 40 different clones of a size from 800 to 7,500 base pairs were identified following hybridization with the probes generated from the GLRaV-2 specific cDNA clones, or from the reaction products in the polymerase chain. Then, more than 40 clones were sequenced on both chains (Figure 2). Example 5 - Expression of Coating Protein in E. coli, and Immunoblot. To determine that the ORF6 was the GLRaV-2 coat protein gene, the ORF6 DNA molecule was subcloned from a reaction product into the polymerase chain, and inserted into the protein expression vector. of fusion pMAL-C2 (New England Biolabs, Inc.). The specific primers used for the reaction in the polymerase chain were CP-96F and CP-96R, where an EcoR I or BamH I site was included to facilitate cloning. CP-96F was designed to include the start codon of the coat protein, and comprises a nucleotide sequence according to SEQ. ID. No .: 21, as follows: CGGAATTCAC CATGGAGTTG ATGTCCGACA G 31 The CP-96R was 66 nucleotides downstream of the stop codon of the coat protein, and comprises the nucleotide sequence corresponding to SEQ. ID. No .: 22, as follows: AGCGGATCCA TGGCAGATTC GTGCGTAGCA GTA 33 The coating protein was expressed as a fusion protein with maltose binding protein (MBP) from E. coli, under the control of a "tac" promoter, and was suppressed by the "lac" repressor. The MBP-CP fusion protein was induced by the addition of 0.3 mM isopropyl-β-D-thio-galactopyranoside (IPTG), and purified by a one-step affinity column according to the manufacturer's instructions (New England , Biolabs, Inc.). The MBP-CP fusion protein or the coat protein dissociated from the fusion protein was tested for reacting with a specific antiserum of GLRaV-2 (kindly provided by Dr. Charles Greif of INRA, Colmar, France) in Western blot. , according to the method described by Hu et al., "Characterization of Closterovirus-Like Particles Associated with Grapevine Leafroll Disease", J. Phytopatholoqy 128: 1-14 (1990), which is incorporated herein by reference. In contrast, non-recombinant plasmids, or non-induced cells, did not react with the GLRaV-2 antiserum. Example 6 - Sequence Analysis and Genome Organization of GLRaV-2. A total of 15,500 base pairs of the RNA genome of the GLRaV-2 genome was sequenced and deposited in GenBank (accession number AF039204). About 85 percent of the total RNA genome was revealed from at least two different clones. The sequence in the region of the coat protein gene was determined and confirmed from several different overlapping clones. The genome organization of GLRaV-2, shown in Figure 2, includes nine open reading frames (eg, ORFla, lb-8). ORFla and ORFlb: Analysis of the amino acid sequence of the N-terminal portion of the product encoded by the GLRaV-2 gel ORF1 revealed two putative papain-like protease domains, which showed significant similarity to the leader protease. type of papain from BYV (Agranovsky et al., "Beet Yellows Closterovirus: Complete Genome Structure and Identification of a Papain-like Thiol Portease", Viroloqy 198: 311-24 (1994), which is incorporated herein by reference). Accordingly, it allowed the prediction of the catalytic residues of cysteine and histidine for the putative GLRaV-2 protease. After alignment of the papain-like protease sequence of BYV with a GLRaV-2 helix, the dissociation site at the Gly-Gly residues (amino acids 588-589) of BYV was aligned with the corresponding alanine dipeptide. glycine (Ala-Gly) and Gly-Gly of GLRaV-2 (Figure 3A). Dissociation at this site would result in a leader protein and a 234 kDa C-terminal fragment (2090 amino acids) consisting of the MT and HEL domains. However, the region upstream of the papain-like protease domain in GLRaV-2 showed no similarity to the corresponding region of BYV. In addition, variability was present in the residues located in the separable bond (Gly in BYV, and Ala in GLRaV-2). A similar variability of the dissociation site residue in the P-PRO domain has been described in LChV (Jelkmann et al., "Complete Genome Structure and Phylogenetic Analysis of Little Cherry Virus, to Mealybug-Transmissible Closterovirus." J. General Viroloqy 78: 2067 -71 (1997), which is incorporated herein by reference.) The search in the database with the deduced amino acid sequence of the protein encoded by the ORFla / lb, revealed a significant similarity with the MT, HEL and RdRP of other closteroviruses The downstream region of the P-PRO dissociation site showed significant similarity (identity of 57.4 percent in an alignment of 266 residues) with the putative BYV methyltransferase domain, and it contained all the conserved motifs typical of the viral type I MTs of the positive chain RNA (Figure 3B). The C-terminal portion of the ORFla was identified as a helicase domain, whose sequence showed high similarity (identity of 57.1 percent in an alignment of 315 residues) with the helicase domain of BYV, and contained the seven conserved motifs characteristic of the helicase from the Superfamily I of the positive strand RNA viruses (Figure 3C) (Hodgman, "A New Superfamily of Replicative Proteins", Nature 333: 22-23 (1988); Koonin and Dolja, "Evolution and Taxonomy of Positive-Strand RNA Viruses: Implications of Comparative Analysis of Amino Acid Sequences", Crit. Rev. in Biochem. and Mol. Biol. 28: 375-430 (1993), both of which are incorporated herein by reference). The ORFlb encoded a polypeptide of 460 amino acids with a molecular mass of 52,486 Da, counting from the site of frame change. The search in the database with RdRP showed a significant similarity with the RdRP domains of the positive chain RNA viruses. The comparison of the RdRP domains of GLRaV-2 and BYV showed the presence of eight conserved motifs of RdRP (Figure 3D). As shown in Figure 8, a tentative phylogenetic tree of the RdRP of GLRaV-2 with respect to other closteroviruses shows that it is closely related to the oncopatite closteroviruses BYV, BYSV and CTV. In closteroviruses, it has been suggested that a mechanism of ribosomal frame change to +1 in the expression of ORFlb is involved, as a large fusion protein with ORFla (Agranovsky et al., "Beet Yellows Closterovirus: Complete Genome Structure and Identification of a Papain-like Thiol Protease ", Viroloqy 198: 311-24 (1994), Karasev et al.," Complete Sequence of the Citrus Sadness Virus RNA Genome ", Viroloqy 208: 511-20 (1995), Klaassen et al. , "Genome Structure and Phylogenetic Analysis of Lettuce Infectious Yellows Virus, to Whitefly-Transmitted, Bipartite Closterovirus", Viroloqy 208: 99 (1995), Karasev et al, "Organization of the 3 '-Terminal Half of Beet Yellow Stunt Virus Genome and Implications for the Evolution of Closteroviruses ", Viroloqy 221: 199-207 (1996), Jelkmann and collaborators," Complete Genome Structure and Phylogenetic Analysis of Little Cherry Virus, a Mealybug-Transmissible Closterovirus ", J. General Viroloqy 78: 206 -71 (1997), all of which are incorporated herein by reference). In the ORFla / lb overlap region of BYV, it is believed that the GGGUUUA gliding sequence and two hair pin structures (stem cycle and pseudonym) result in a +1 frame change (Agranovsky et al., "Beet Yellows Closterovirus"). : Complete Genome Structure and Identification of a Papain-like Thiol Portease ", Viroloqy 198: 311-24 (1994), which is incorporated herein by reference). None of these characteristics are preserved in CTV and BYSV (Karasev et al., "Complete Sequence of the Citrus Sadness Virus Genome Virus", Viroloqy 208: 511-20 (1995); Karasev et al., "Organization of the 3 '-Terminal Half of Beet Yellow Stunt Virus Genome and Implications for the Evolution of Closteroviruses ", Viroloqy 221: 199-207 (1996), both of which are incorporated herein by reference), where it was suggested that a ribosomal pause in a terminator or in a rare codon it performs the same function. Comparisons of the nucleotide sequence of the C-terminal region of the helicase, and the N-terminal region of RdRP of GLRaV-2 with the same region of other closteroviruses, revealed a significant similarity with BYV, BYSV and CTV. As shown in Figure 4, the UAG terminator at the end of the C-terminal helicase of GLRaV-2 was aligned with the UAG terminator of BYV and BYSV, and the CGG arginine codon of CTV. . ORF2 encodes a peptide protein consisting of 171 base pairs (57 amino acids) with a molecular mass of 6.297 Da. As predicted, the deduced-amino acid sequence includes a stretch of non-polar amino acids, which is presumed to form a transmembrane helix. A small hydrophobic analog protein is also present in BYV, BYSV, CTV, LIYV and LChV (Agranovsky et al., "Nucleotide Sequence of the 3'-Terminal Half of Beet Yellows" Closterovirus RNA Genome Unique Arrangement of Eight Virus Genes ", J. General Viroloqy 72: 15-24 (1991); Karasev et al., "Organization of the 3 '-Terminal Half of Beet Yellow Stunt Virus Genome and Implications for the Evolution of Closteroviruses", Viroloqy 221: 199-207 (1996); Pappu et al., "Nucleotide Sequence and Organization of Eight 3 'Open Reading Frames of the Citrus Tristeza Closterovirus Genome", Viroloqy 199: 35-46 (1994); Klaassen et al., "Partial Characterization of the Lettuce Infectious Yellows Virus Genomic RNAs, Identification of the Coat Protein Gene and Comparison of its Amino Acid Sequence With Those of Other Filamentous RNA Plant Viruses", J. General Viroloqy 75: 1525-33 (1994); Jelkmann et al, "Complete Genome Structure and Phylogenetic Analysis of Little Cherry Virus, to Mealybug-Transmissible Closterovirus", J. General Viroloqy 78: 2067-71 (1997), all of which are incorporated herein by reference). ORF3 encodes a polypeptide of 600 amino acids with a molecular mass of 65,111 Da, which is homologous to the HSP70 cellular heat shock protein. HSP70 is highly conserved among closteroviruses, and is probably involved in the activity of ATPase, and in the integration of protein with protein for chaperone activity (Agranovsky et al., "The Beet Yellows Closterovirus p65 Homologue of HSP70 Chaperones has ATPase Activity Associated with its Conserved N-terminal Domain but Interact with Unfolded Protein Chains ", J. General Viroloqy 78: 535-42 (1997); Agranovsky et al.," Bacterial Expression and Some Properties of the p65, to Homologue of Cell Heat Shock Protein HSP70 Encoded in RNA Genome of Beet Yellows Closterovirus ", Doklady Akademii Nauk, 340: 416-18 (1995); Karasev et al.," HSP70-Related 65-kDa Protein of Beet Yellows Closterovirus is a Microtubule-Binding Protein " , FEBS Letters 304: 12-14 (1992), all of which are incorporated herein by reference). As shown in Figure 5, alignment of the entire ORF3 of GLRaV-2 with the HSV70 homolog of BYV revealed the presence of the eight conserved motifs. The similarity percentage of HSP70 between GLRaV-2 and that of BYV, BYSV, CTV, LIYV and LChV is 47.8 percent, 47.2 percent, 38.6 percent, 20.9 percent and 17.7 percent, respectively. . The ORF4 encodes a protein of 551 amino acids, with a molecular mass of 63,349 Da. The search in the database with the ORF4 protein product did not identify similar proteins, except those of their counterparts in the closteroviruses, BYV (P64), BYSV (P61), CTV (P61), LIYV (P59), and LChV (P61). It is believed that this protein is a putative heat shock protein. As shown in Figure 9, two conserved motifs that were present in BYV were also identified (Agranovsky et al., "Nucleotide Sequence of the 3'-Terminal Half of Beet Yellows Closterovirus RNA Genome Unique Arrangement of Eight Virus Genes", J. General Viroloqy 72: 15-24 (1991), which is incorporated herein by reference), and CTV (Pappu et al., "Nucleotide Seguence and Organization of Eight 3 'Open Reading Frames of the Citrus Tristeza Closterovirus Genome", Viroloqy 199 : 35-46 (1994), which is incorporated herein by reference) into the ORF4 of GLRaV-2. ORF5 and ORF6 encode polypeptides with a molecular mass of 24.803 Da and 21.661 Da, respectively. The start codon of both open reading frames is in a favorable context for translation. ORF6 was identified as the GLRaV-2 coat protein gene, based on sequence comparison with other closteroviruses. The calculated molecular mass of the protein product of ORF6 (21.662 Da) is in good agreement with the approximately 22 to 26 kDa previously estimated, based on SDS-PAGE (Zimmermann et al., "Characterization and Serological Detection of Four Closterovirus-like Particles Associated with Leafroll Disease on Grapevine ", J. Phvtopatholoqy 130: 205-18 (1990), Boscia et al," Nomenclature of Grapevine Leafroll-Associated Putative Closteroviruses ", Vitis 34: 171-75 (1995), both of which are incorporated to the present as reference). The search in the database with the deduced amino acid sequence of the ORF6 of GLRaV-2 showed a similarity with the coat proteins of the closteroviruses, BYV, BYSV, CTV, LIYV, LChV and GLRaV-3. At the nucleotide level, the highest percentage of similarities was found with the BYSV coat protein (34.8 percent); At the amino acid level, the highest percentage of similarity was with the coat proteins of BYV (32.7 percent) and BYSV (32.7 percent).

As shown in Figure 6A, the alignment of the amino acid sequence of the coat protein and the duplicate coat protein of GLRaV-2 with respect to other closteroviruses revealed that there were invariant amino acid residues (NRGD) present in both ORF5 and ORF6 of GLRaV-2. It is believed that two of these amino acid residues (R and D) are involved in the stabilization of molecules by salt bridge formation and proper folding in the most conserved core region of the coating proteins of all filamentous plant viruses (Dolja et al., "Phylogeny of Capsid Proteins of Rod-Shaped and Filamentous RNA Plant Viruses Two Families With Distinct Patterns of Sequence and Probably Structure Conservation", Viroloav 184: 79-86 (1991), which is incorporated herein by reference ). The identification of the ORF6 as the gene of the coating protein, was further confirmed by Western blot, followed by the expression of a fusion protein, consisting of 22 kDa of the ORF6 coat protein, and 42 kDa of the binding protein. of maltose, produced by E. col i transformed, as described in Example 5 above. As shown in Figure 6B, the assumed phylogenetic tree of the coating protein and the coating protein duplicate of GLRaV-2, with those of other closteroviruses, showed that GLRaV-2 is more closely related to the transmissible closteroviruses by aphids (BYV, BYSV and CTV) (Candresse, "Closteroviruses and Clostero-like Elongated Plant Viruses", in Encyclopedia of Viroloqy, pages 242-48, Webster and Granoff, eds., Academic Press, New York (1994), which is incorporated herein by reference) that with the closterovirus transmissible by whitefly (LIYV) or by coconuts (LChV and GLRaV-3) (Raine et al., "Transmission of the Agent Causin Little Cherry Disease by the Apple Mealybug Phenacoccus aceris and the Dodder Cuscuta Lupuliformis ", Canadian J. Plant Patholoqy 8: 6-11 (1986), Jelkmann et al.," Complete Genome Structure and Phylogenetic Analysis of Little Cherry Virus, to Mealybug-Transmissible Closterovirus ", J. General Viroloqy 78: 2067-71 (1997), Rosciglione and Gugelli, "Transmission of Grapevine Leafroll Disease and an Associated Closterovirus to Healthy Grapevine by the Mealybug Planococcus ficus", Phytopara-sitica 17:63 (1989), Engelbrecht and Kasdorf, " Transmission of Grapevine Leafroll Disease and Associated Closteroviruses by the Vine Mealybug planococcus-ficus ", Phytophlactica, 22: 341-46 (1990); Cabaleiro and Segura, 1997: Petersen and Charles, "Transmission of Grapevine Leafroll-Associated Closteroviruses by Pseudococcus longispinus and P. calceolariae, Plant Patholoqy 46: 509-15 (1997), all of which are incorporated herein by reference. and ORF8 encode 162 amino acid polypeptides with a molecular mass of 18,800 Da and 206 amino acids with a molecular mass of 23,659 Da, respectively.

The search in the database with the ORF7 and the ORF8 did not show a significant similarity with any other proteins. However, these genes were of a size and location similar to those observed in the sequence of other closteroviruses, BYV (P20, P21), BYSV (P18, P22) and LChV (P21, P27) (Figure 7). However, no conserved regions were observed between the ORF7 or ORF8 and their counterparts in BYV, BYSV and LChV. The 3'-terminal non-translated region (3 '-UTR) consists of 216 nucleotides. The analysis of the nucleotide sequence revealed a long stretch of oligo (A) near the end of the GLRaV-2 genome, which is similar to that observed in the genome of BYV and BYSV (Agranovsky et al., "Nucleotide Sequence of the 3'-Terminal Half of Beet Yellows Closterovirus RNA Genome Unique Arrangement of Eight Virus Genes", J. General Viroloqy 72: 15-24 (1991); Karasev et al., "Organization of the 3 '-Terminal Half of Beet Yellow Stunt Virus Genome and Implications for the Evolution of Closteroviruses", Viroloqy 221: 199-207 (1996), both of which are incorporated herein by reference) . The genome of BYV ends in CCC; BYSV and CTV end in CC with additional G or A in the replicative double-stranded form of BYSV (Karasev et al., "Organization of the 3 '-Terminal Half of Beet Yellow Stunt Virus Genome and Implications for the Evolution of Closteroviruses", Viroloqy 221: 199-207 (1996), which is incorporated herein by reference), and CTV Karasev et al., "Complete Sequence of the Citrus Tristeza Virus Genome Virus", Viroloqy 208: 511-20 (1995), which is incorporated herein by reference), respectively. GLRaV-2 had CGC in the 3 'terminus of the genome. Recently, a cis-element of 60 nucleotides conserved in the 3'-UTR of three monopartite closteroviruses was identified, which included a prominent stem structure and cycle conserved (Karasev et al., 1996). As shown in Figure 10, alignment of the 3'-UTR sequence of GLRaV-2 with the same regions of BYV, BYSV and CTV showed the presence of the same conserved 60 nucleotide stretch. In addition to this cis element, no conserved sequences were found in the 3 '-UTRs of GLRaV-2, BYV, BYSV and CTV. The closteroviruses studied up to now (for example, BYV, BYSV, CTV, LIYV, LChV and GLRaV-3) have apparent similarities in the organization of the genome, including genes associated with replication consisting of the conserved MT, HEL and RdRP domains, and an array of five unique genes for closteroviruses (Dolja et al., "Molecular Biology and Evolution of Closter Viruses: Sophisticated Build-up of Large RNA Genomes," Annual Rev. Photopatholoqy 32: 261-85 (1994); Agranovsky, "Principies of Molecular Organization, Expression, and Evolution of Closter Viruses: Over the Barriers, "Adv. in Virus Res. 47: 119-218 (1996), Jelkmann et al," Complete Genome Structure and Phylogenetic Analysis of Little Cherry Virus, to Mealybug- Transmissible Closterovirus ", J. General Viroloqy 78: 2067-71 (1997), Ling et al.," Nucleotide Seguence of the 3 'Terminal Two-Thirds of the Grapevine Leafroll Associated Virus-3 Genome Reveal Typical Monopartite Closterovirus ", J. General Viroloqy 79 (5): 1289-1301 (1998), all of which are incorporated herein by reference). The above data clearly show that GLRaV-2 is a closterovirus. In the genome of GLRaV-2, two putative type proteinases of papain were identified, and an autoproteolytic dissociation process was predicted. Proteins associated with replication consisting of conserved motifs MT, HEL, and RdRP were also identified, which were closely related phylogenetically to proteins associated with replication of other closteroviruses. A unique genetic arrangement that included a small hydrophobic transmembrane protein, homologous to HSP70, homologous to HSP90, diverged CP, and CP, in GLRaV-2 was also preserved. In addition, the calculated molecular mass (21,661 Da) of the coating protein (ORF6) of GLRaV-2 is in good agreement with agüella of the other closterovirus (22 to 28 Kda) (Martelli and Bar-Joseph, "Closteroviruses"). : Classification and Nomenclature of Viruses ", Fifth Report of the International Committee on Taxonomy of Viruses, Francki et al., Eds., Springer-Verlag Wein, New York, pages 345-47 (1991); Candresse and Martelli," Genus Closterovirus " , in Virus Taxonomy, Report of the International Committee on Taxonomy of Viruses, Murphy et al., eds., Springer-Verlag, NY, pages 461-63 (1995), both of which are incorporated herein by reference). Two open reading frames downstream of the coating protein are of a similar size and location, to those observed in the BYV genome. In addition, the lack of a poly (A) tail at the 3 'end of GLRaV-2 is also in good agreement with other closteroviruses. Like all other closteroviruses, it is suspected that expression of ORFlb occurs through a ribosomal frame change 1, and 3'-proximal open reading frames are likely expressed by the formation of a nested set of subgenomic RNAs. . Due to the sliding sequence, the structure of stem cycle and pseudonym in the frame change of BYV was absent in GLRaV-2, and the change of maco * 1 of GLRaV-2 could be equal to that proposed for CTV (Karasev et al., "Complete Seguence of the Citrus Tristeza Virus RNA Genome ", Viroloqy 208: 511-20 (1995), which is incorporated herein by reference), and BYSV (Karasev et al.," Organization of the 3 '-Terminal Half of Beet Yellow Stunt Virus Genome and Implications for the Evolution of Closteroviruses ", Viroloqy 221: 199-207 (1996), which is incorporated herein by reference). Above all, GLRaV-2 is more closely related to the monopartite BYV, BYSV and CTV closteroviruses than to GLRaV-3 (Figure 7) (Ling et al., "Nucleotide Sequence of the 3 'Terminal Two-Thirds of the Grapevine Leafroll Associated Virus -3 Genome Reveáis Typical Monopartite Closterovirus "," d.

General Viroloqy 79 (5): 189-1301 (1998), which is incorporated herein by reference), even though the latter occasions symptoms of leaf rolling similar on the vine (Rosciglione and Gugerli, "Maladies de 1 'Enroulement et du Bois Strie de la Vigne: Analyze Microscopigue et Serologique (Leaf Curl and Vine Stem Sting: Microscopic and Serological Analysis), "Rev Suisse Viticult Arboricult Horticultur 18: 207-11 (1986); Hu et al. Zation of Closterovirus-Like Particles Associated with Grapevine Leafroll Disease ", J. Phytopatholoqy 128: 1-14 (1990), both of which are incorporated herein by reference). Closteroviruses are a diverse group with complex and heterogeneous genome organizations. So far, GLRaV-2 is the only closterovirus that matches the genome organization of BYV, the type member of the Closterovirus genus. In addition, the genomic RNA of GLRaV-2 is approximately the same size as that of BYV; however, the transmission vector of GLRaV-2 is unknown. The genome organization of GLRaV-2 is more closely related to aphid-transmissible closteroviruses (BYV and CTV) than to whitefly-transmissible closterovirus (LIYV) or cocci (LChV and GLRaV-3). Therefore, it is possible that GLRaV-2 is transmitted by aphids. The aphid transmission experiments with GLRaV-2 should provide information that can help develop methods to further control GLRaV-2.

A total of 15,500 nucleotides or more than 95 percent of the estimated GLRaV-2 genome have been cloned and sequenced. GLRaV-2 and GLRaV-3 (Ling et al., "Nucleotide Sequence of the 3 'Terminal Two Thirds of the Grapevine Leafroll Associated Virus-3 Genome Reveal Typical Monopartite Closterovirus", J. General Viroloqy 79 (5): 1289-1301 (1998), which is incorporated herein by reference) are the first closteroviruses associated with vine leaf curl that have been almost completely sequenced. The above data clearly justify the inclusion of GLRaV-2 in the Closterovirus genus. In addition, information regarding the GLRaV-2 genome would provide a better understanding of these and related GLRaVs, and would add fundamental knowledge to the closterovirus group. Example 7 - Construction of the GLRaV-2 Coating Proxy Gene in an Expression Vector in Plants. Vitis vxnifra vines, Pinot Noir variety infected with GLRaV-2 originating from the central New York vineyard, were used as the virus isolate, from which the cp gene of GLRaV-2 was identified. Based on the sequence information, two oligonucleotide primers have been designed. The primer in sense CP-96F (SEQ ID No.:21) starts from the start codon ATG of the coat protein gene, and the complementary primer CP-96R (SEQ ID No.:22) starts from 56 nucleotides downstream of the stop codon of the coat protein gene. A Neo I restriction site (11 base pairs in SEQ ID No .: 21, and 13 base pairs in SEQ ID No.:22) is introduced at the beginning of both primers, to facilitate cloning . The GLRaV-2 coat protein gene was amplified from dsRNA extracted from GLRaV-2 infected vine, using reverse transcriptase polymerase chain reaction (RT-PCR). The coating protein product amplified with reaction in the polymerase chain, was purified from low melting temperature agarose gel, digested with Neo I, and cloned into the same plant expression vector pEPT8 digested with enzyme (shown in Figure 11). After screening, the orientation of the recombinant construct was verified by using the internal restriction site of the coat protein gene, and direct sequencing of the coat protein gene. The recombinant construction with the translatable full-length coat protein gene (in sense), pEPT8CP-GLRaV-2, was going through for additional cloning. The expression cassette in plants, which consisted of a 35S enhancer of double cauliflower mosaic virus (CaMV), a 35S promoter of CaMV, a 5 'leader sequence of RNA from alfalfa mosaic virus (ALMV), a GLRaV-2 coating protein (CP-GLRaV-2), and a 3 'untranslated region of 35S of CaMV as a terminator, was cut using the restriction enzyme EcoR I, isolated from low temperature agarose gel of fusion point, and was cloned in the same binary vector pGA482GG or pGA482G treated with restriction enzyme (a derivative of pGA482) (An et al., "Binary Vectors", in Plant Molecular Bioloqy Manual, pages A3: 1-19, Gelvin and Schilperoot, eds., Kinwer Academic Publishers, Dordrecht, The Netherlands (1988), which is incorporated herein by reference). The resulting recombinant constructs are pGA482GG / EPT8CP-GLRaV2 (shown in Figure HA), which contains both neomycin and phosphotransferase (np II) and β-glucuronidase (GUS) in the internal region of the T-DNA, and pGA482G / EPT8CP-GLRaV2 (shown in Figure 11B) without GUS. These recombinant constructs were introduced separately by electroporation into the unarmored avirulent strain of Agrobacterium tumefaciens C58Z707. Agrobacterium tumefaciens, which contained the vector, was used to infect wounded leaf discs with Nicotiana benthamiana according to the procedure essentially described by Horsch et al., "A Simple and General Method for Transferring Genes into Plants", Science 277: 1229-1231 81985), which is incorporated herein by reference. Example 8 - Analysis of Nicotiana Plants. Transgenic benthamiana with the GLRaV-2 Coating Protein Gene. NPT II-ELISA: Immunosorbent assay bound with double antibody sandwich enzyme (DAS-ELISA) was used to detect the np II enzyme with a NPT II-ELISA kit (5 'prime to 3' prime, Inc., Boulder, Co .).

Indirect ELISA: Polyclonal antibodies were used for GLRaV-2, which were prepared from the coating protein expressed in E. coli. Plates were coated with homogenized samples in extraction buffer (1:10 weight / volume) (phosphate-regulated serum containing 0.05 percent Tween 20, and 2 percent polyvinylpyrrolidone), and incubated overnight at 4 ° C . After washing with phosphate regulated serum containing 0.05 percent Tween 20 (PBST), plates were blocked with blog buffer (serum regulated with phosphate containing 2 percent bovine serum albumin), and incubated at room temperature for 1 hour. Anti-GLRaV-2 IgG was added in 2 micrograms / milliliter after washing with PBST. After incubation at 30 ° C for 4 hours, the plates were washed with PBST, and goat anti-rabbit alkaline phosphatase conjugate was added (Sigma) in a dilution of 1: 10,000. The absorbance was measured at 405 nanometers with a MicroELISA AutoReader. In addition, Western blot was also performed according to the method described by Hu et al., "Characterization of Closterovirus-like Particle Associated Grapevine Leafroll Disease", J. Phytophatho-loqy 128: 1-14 (1990), which is incorporated in the present as a reference. Polymerase Chain Reaction Analysis: Genomic DNA was extracted from leaves of transgenic and non-transgenic plants assumed in accordance with the method described by Cheung et al., "A Simple and Rapid DNA Microextraction Method for Plants, Animal, and Insect Suitable for RAPD and other PCR analysis ", PCR Methods and Applications 3:69 (1996), which is incorporated herein by reference. The total extracted DNA served as template for the reaction in the polymerase chain. The primers CP-96F and CP-96R (SEQ ID Nos. 21 and 22, respectively) were used for the GLRaV-2 coating protein gene, as well as the npt II 5 'and 3' primers for the reaction analysis in the polymerase chain. The reaction in the polymerase chain was performed at 94 ° C for 3 minutes for one cycle, followed by 30 cycles of 94 ° C for 1 minute, 50 ° C for 1 minute, and 72 ° C for 2:30 minutes, with an additional extension at 72 ° C for 1-0 minutes. The product of the reaction in the polymerase chain was analyzed on agarose gel. After the transformation, a total of 42 Nicotiana benthamiana lines resistant to kanamycin (R0) were obtained, from which the leaf samples were tested by NPT II enzyme activity. Among them, 37 lines were positive for NPT II by ELISA, which took approximately 88.0 percent of the total transformants. However, some of the NPT II negative plants were obtained among these selected kanamycin-resistant plants. All the transgenic plants were self-pollinated in a greenhouse, and the seeds of these transgenic lines were germinated for further analysis.

The production of GLRaV-2 coating protein in transgenic plants was detected by indirect ELISA before inoculation, and the results showed that the expression of the GLRaV-2 coat protein gene was not detectable in all the transgenic plants tested. . This result was further confirmed with Western blot. Using the antibody for GLRaV-2, the production of the coating protein in the transgenic and non-transgenic control plants was not detected. However, a protein of the expected size (approximately 22 kDa) was detected in the positive control plants infected with GLRaV-2. This result was consistent with the result of ELISA. The presence of the GLRaV-2 coat protein gene in transgenic plants was detected from the total genomic DNA extracted from the plant tissue by reaction analysis in the polymerase chain (Figure 12). The DNA product of the expected size (653) base pairs was amplified from 20 transgenic lines tested, but not in non-transgenic plants. The result indicated that the GLRaV-2 coat protein gene was present in these transgenic lines, which was also confirmed by Northern blot analysis. Example 9 - Plants of Nicotiana benthamiana Transgenic R? And R2 are Resistant to GLRaV-2. Inoculation of transgenic plants: The isolate 94/970 of GLRaV-2, which was originally identified and transmitted from grapevine to Nicotiana benthamiana in South Africa (Goszcynski et al., "Detection of Two Strains of Grapevine Leafroll-Associated Virus 2", Vitis 35: 133-35 (1996), which is incorporated herein by reference), was used as inoculum. The coat protein gene of isolate 94/970 was sequenced; and is identical to the coat protein gene used in the construction. Nicotiana benthamiana is an experimental host of GLRaV-2. Its infection produces occasional chlorotic and necrotic lesions followed by release of the systemic vein. The release of the vein results in necrosis of the vein. Eventually, the infected plants died, starting from top to bottom. In the five to seven leaf stage, two younger apical leaves were stimulated with the isolated 94/970 of GLRaV-2. The inoculum was prepared by grinding 1.0 gram of Nicotiana benthamiana leaf tissue infected with GLRaV-2 in 5 milliliters of phosphate buffer (K2HP04 0.01M, pH 7.0). The test plants were sprinkled with carborundum, and rubbed with the prepared inoculum. The non-transformed plants were inoculated simultaneously as above. The plants were observed to determine the development of symptoms every third day for 60 days after inoculation. The Rl resistant transgenic plants were taken to R2 generation for further evaluation. Initially, the transgenic progenies were screened from the 20 R0 lines to determine the resistance to GLRaV-2, followed by inoculation with the 94/970 isolate of GLRaV-2. The seedlings of the transgenic plants (positive for NPT II), and the non-transformed control plants, were inoculated with GLRaV-2. After inoculation, the reaction of the test plants was divided into three types: highly susceptible (ie, typical symptoms were observed two to four weeks after inoculation); tolerant (ie, no symptoms developed early, and typical symptoms were shown four to eight weeks after inoculation); and resistant (ie, the plants remained asymptomatic eight weeks after inoculation). Based on the reaction of the plants, the resistant plants were obtained from fourteen different lines (mentioned in the following Table 1). In each of these fourteen lines, no viruses were detected within these plants by ELISA at six weeks after inoculation. In contrast, GLRaV-2 was detected in symptomatic plants by indirect ELISA. In the other six lines, although there were a few plants with some kind of delay in the development of symptoms, all the inoculated transgenic plants died three to eight weeks after inoculation. Based on the initial screening results, five representative lines were selected consisting of three resistant lines (1, 4 and 19), and two susceptible lines (12 and 13) for further analysis.

Table 1 The following Table 2 shows the development of symptoms in transgenic plants in relation to non-transgenic control plants, in the five selected lines in separate experiments. The non-transgenic control plants were all infected two to four weeks after inoculation, which showed the typical symptoms of GLRaV-2 in Nicotiana benthamiana, including chlorotic and local lesions, followed by systemic vein release and necrosis of the vein in the leaves. Three of the tested lines (1, 4 and 19) showed some resistance that was manifested by an absence, or by a delay, in the development of symptoms. Two other lines, 12 and 13, developed symptoms almost at the same time as the non-transformed control plants. From top to bottom, the leaves of the infected plants gradually became yellowed, withered and dried, and eventually the whole plants died. No matter when the infection occurred, the eventual result was the same. Six weeks after the inoculation, all the non-transgenic plants and the susceptible plants were dead. Some tolerant plants began to die. In contrast, asymptomatic plants were normally blooming and pollinating like non-inoculated healthy control plants (Figure 13).

Table 2 The ELISA was performed at 6 weeks after the inoculation, to test the replication of GLRaV-2 in the plants. Presumably, the highest level of coating protein reflected the replication of the virus. The result showed that the absorbance value in the symptomatic plants reached (OD) from 0.7 to 3.2, compared with (OD) from 0.10 to 0.13 before the inoculation. In contrast, no GLRaV-2 was detected in the asymptomatic plants, of which the absorbance value was the same or almost the same as that of the non-transformed healthy control plants. The data confirm that the virus was replicated in symptomatic plants, but not in asymptomatic plants. The replication of GLRaV-2 was suppressed in the asymptomatic plants. This result implied that another mechanism different from the resistance mediated by the coating protein was probably involved. Three R2 progenies derived from resistant transgenic plants of lines 1, 4 and 19 were generated, and were used to examine the stable transmission, and if the resistance was maintained in the generation R2. These results are shown in Table 3 below. The NPT II analysis revealed that R2 progeny were still segregating. The expression of coat protein in progeny R2 was not yet detectable. After inoculation, all non-transgenic plants were infected, and showed symptoms of GLRaV-2 in the leaves after 24 days after inoculation. In contrast, the transgenic R2 inoculated progeny showed different levels of resistance from those highly susceptible to highly resistant. The tolerant and resistant plants were manifested by a delay in the development of symptoms and by absence of symptoms, respectively. At 6 weeks after inoculation, GLRaV-2 was detected in tolerant symptomatic infected plants by indirect ELISA; but not in asymptomatic plants. This result indicated that replication of the virus in these resistant plants was suppressed, which was confirmed by Western blot. These resistant plants remained asymptomatic eight weeks after inoculation, and were blooming normally and pollinating. Table 3 Example 10 - Evidence of RNA Mediated Protection in Transgenic Plants. Northern blot analysis: Total RNA was extracted from the leaves before inoculation following the method described by Napoli et al., Plant Cell 2: 279-89 (1990), which is incorporated herein by reference. The concentration of the extracted RNA was measured by the spectrophotometer at OD 260. Approximately 10 grams of total RNA was used for each sample. The probe used was a third part 3 'of the GLRaV-2 coating protein gene, which was randomly labeled with 32P (a-dATP), using the Klenow fragment of polymerase I of the DNA. Using DNA corresponding to a third part 3 'of the sequence of the coat protein gene as a probe, a single band was detected in the RNA extracted from susceptible plants from progeny Rl of lines 5, 12 and 13, by means of Northern hybridization. There was little or no signal detected in the transgenic plants of the Rl progeny of lines 1, 4 and 19. This RNA is not present in the non-transformed control plants. The size of the hybridization signal was estimated at a nucleic acid of approximately 0.9 kb, which was approximately equal to that estimated (Figure 14). In lines 1, 4 and 19, the level of continuous state of RNA expression was also low in progeny R2. These data showed that the susceptible plants of lines 12 and 13 had a high level of mRNA, and all the transgenic plants of lines 1, 4 and 19 had a low level of mRNA. Example 11 - Transformation and Analysis of Transgenic Vines with the GLRaV Coating Protein Gene - Plant Materials: The cultures of rhizome Couderc 3309 (3309C) (V. riparia x V. rupestris), Vi ris riparia 'Gloire de Montpellier '(Gloire), Teleki 5C (5C) (V. berlandieri x V. riparia), Millardet et De Grasset 101-14 (101-14 MGT) (V. riparia x V. rupestris), and Richter 110 (110R) (V. rupestris x V. berlandieri) The initial embryogenic calli of Gloire were provided by Mozsar and Süle (Institute for Plant Protection, Hungarian Academy of Sciences, Budapest) All the other plants came from a vineyard in the Station of New York State Agricultural Experiments, Geneva, NY Sprouts were removed from the clusters, and surface sterilized in 70 percent ethanol for 1 or 2 minutes.Spouts (from the greenhouse and field) were transferred to hypochlorite from sodium at 1 percent for 15 m inutes, then rinsed three times in sterile double-distilled water. The anthers were aseptically separated from the flower buds with the help of a stereomicroscope. The pollen was crushed on a microscope slide under a coverslip with a drop of acetocarmine to observe the cytological stage. This was done to determine which stage was the most favorable for callus induction. Somatic embryogenesis and regeneration: The anthers were coated under aseptic conditions at a density of 40 to 50 per Petri dish with a diameter of 9 cm containing MSE. The dishes were grown at 28 ° C in the dark. The callus was started, and, after 60 days, the embryos were induced, and transferred to a HMG medium free of hormones for differentiation. The embryos in the torpedo stage of the HMG medium were then transferred to MGC to promote germination of the embryo. The cultures were kept in the dark at 26-28 ° C, and transferred to a fresh medium at intervals of 3 to 4 weeks. The elongated embryos were transferred to a rooting medium in baby food containers (5 to 8 embryos per container). The embryos were cultured in a tissue culture room at 25 ° C, with a daily photoperiod of 16 hours (76 micromoles per second) to induce shoot and root formation. After the plants developed roots, they were transplanted to the earth in the greenhouse. Transformation: The protocols used for the transformation were modified from those described by Scorza et al., "Transformation of Grape (Vi tis vinifera L.) Sygotic-Derived Somatic Embryos and Regeneration of Transgenic Plants", Plant Cell Rpt. 14: 589-92 (1995), which is incorporated herein by reference). Night cultures of Agrobacterium strain C58Z707 or LBA4404 were grown in an LB medium at 28 ° C in a shaking incubator. The bacteria were centrifuged for 5 minutes at 3000-5000 rpm, and resuspended in a liquid medium MS (OD 1.0 to A600 nanometers). The embryo calluses were immersed in the bacterial suspension for 15 to 30 minutes, dried, and transferred to an HMG medium with or without acetosyringone (100 μM). The embryogenic calli were co-cultivated with the bacteria for 48 hours in the dark at 28 ° C. Then, the plant material was washed in MS liquid plus cefotaxime (300 milligrams / milliliter) and carbenicillin (200 milligrams / milliliter) 2 to 3 times. To select the transgenic embryos, the material was transferred to an HMG medium containing 20 or 40 milligrams / liter of kanamycin, 300 milligrams / liter of cefotaxime, and 200 milligrams / liter of carbenicillin. Alternatively, after co-culture, the embryogenic calli were transferred to an initiation MSE medium containing 25 milligrams / liter of kanamycin plus the same antibiotics mentioned above. All plant materials were incubated in continuous darkness at 28 ° C. After growth on the selection medium for 3 months, the embryos were transferred to HMG or MGC without kanamycin to promote the lengthening of the embryos. Then they were transferred to a rooting medium without antibiotics. The untransformed calli were cultured on the same medium with and without kanamycin to verify the efficiency of the kanamycin selection process. Although the invention has been described in detail for purposes of illustration, it is understood that this detail is exclusively for that purpose, and those skilled in the art can make variations therein without departing from the spirit and scope of the invention, which defined by the following claims.

LIST OF SEQUENCES (1) GENERAL INFORMATION: (i) TITLE OF THE INVENTION: PROTEINS, AND THEIR USES, OF THE VIRUSES (TYPE 2) OF THE VINEYARD OF THE ROLL OF LEAVES OF THE VINE (ii) NUMBER OF SEQUENCES: 23 (2) INFORMATION FOR SEQ ID NO: 1: (i) CHARACTERISTICS OF THE SEQUENCE: (A) Length: 15500 base pairs (B) type: nucleic acid (C) Chain type: simple (D) Topology: linear (ii) TYPE MOLECULE: cDNA (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 1: TAAACATTGC GAGAGAACCC CATTAGCGTC TCCGGGGTGA ACTTGGGAAG GTCTGCCGCC 60 GCTCAGGTTA TTTATTTCGG CAGTTTCACG CAGCCCTTCG CGTTGTATCC GCGCCAAGAG 120 AGCGCGATCG TAAAAACGCA ACTTCCACCG GTCAGTGTAG TGAAGGTGGA GTGCGTAGCT 180 GCGGAGGTAG CTCCCGACAG GGGCGTGGTC GACAAGAAAC CTACGTCTGT TGGCGTTCCC 240 CCGCAGCGCG GTGTGCTTTC TTTTCCGACG GTGGTTCGGA ACCGCGGCGA CGTGATAATC 300 ACAGGGGTGG TGCATGAAGC CCTGAAGAAA ATTAAAGACG GGCTCTTACG CTTCCGCGTA 360 GGCGGTGACA TGCGTTTTTC GAGATTTTTC TCATCGAACT ACGGCTGCAG ATTCGTCGCG 420 AGCGTGCGTA CGAACACTAC AGTTTGGCTA AA TTGCACGA AAGCGAGTGG TGAGAAATTC 480 TCACTCGCCG CCGCGTGCAC GGCGGATTAC GTGGCGATGC TGCGTTATGT GTGTGGCGGG 540 AAATTTCCAC TCGTCCTCAT GAGTAGAGTT ATTTACCCGG ATGGGCGCTG TTACTTGGCC 600 CATATGAGGT ATTTGTGCGC CTTTTACTGT CGCCCGTTTA GAGAGTCGGA TTATGCCCTC 660 GGAATGTGGC CTACGGTGGC GCGTCTCAGG GCATGCGTTG AGAAGAACTT CGGTGTCGAA 720 GCTTGTGGCA TAGCTCTTCG TGGCTATTAC ACCTCTCGCA ATGTTTATCA CTGTGATTAT 780 GACTCTGCTT ATGTAAAATA TTTTAGAAAC CTTTCCGGCC GCATTGGCGG TGGTTCGTTC 840 GATCCGACAT CTTTAACCTC CGTAATAACG GTGAAGATTA GCGGTCTTCC AGGTGGTCTT 900 CCTAAAAATA TAGCGTTTGG TGCCTTCCTG TGCGATATAC GTTACGTCGA ACCGGTAGAC 960 TCGGGCGGCA TTCAATCGAG CGTTAAGACG AAACGTGAAG ATGCGCACCG AACCGTAGAG 1020 GAACGGGCGG CCGGCGGATC CGTCGAGCAA CCGCGACAAA AGAGGATAGA TGAGAAAGGT 1080 TGCGGCAGAG TTCCTAGTGG AGGTTTTTCG CATCTCCTGG TCGGCAACCT TAACGAAGTT 1140 AGGAGGAAGG TAGCTGCCGG ACTTCTACGC TTTCGCGTTG GCGGTGATAT GGATTTTCAT 1200 CGCTCGTTCT CCACCCAAGC GGGCCACCGC TTGCTGGTGT GGCGCCGCTC GAGCCGGAGC 1260 GTGTGCCTTG AACTTTACTC ACCATCTAAA AAC TTTTTGC GTTACGATGT CTTGCCCTGT 1320 TCTGGAGACT ATGCAGCGAT GTTTTCTTTC GCGGCGGGCG GCCGTTTCCC TTTAGTTTTG 1380 ATGACTAGAA TTAGATACCC GAACGGGTTT TGTTACTTGG CTCACTGCCG GTACGCGTGC 1440 GCGTTTCTCT TAAGGGGTTT TGATCCGAAG CGTTTCGACA TCGGTGCTTT CCCCACCGCG 1500 GCCAAGCTCA GAAACCGTAT GGTTTCGGAG CTTGGTGAAA GAAGTTTAGG TTTGAACTTG 1560 TACGGCGCAT ATACGTCACG CGGCGTCTTT CACTGCGATT ATGACGCTAA GTTTATAAAG 1620 GATTTGCGTC TTATGTCAGC AGTTATAGCT GGAAAGGACG GGGTGGAAGA GGTGGTACCT 1680 TCTGACATAA CTCCTGCCAT GAAGCAGAAA ACGATCGAAG CCGTGTATGA TAGATTATAT 1740 GGCGGCACTG ACTCGTTGCT GAAACTGAGC ATCGAGAAAG ACTTAATCGA TTTCAAAAAT 1800 GACGTGCAGA GTTTGAAGAA AGATCGGCCG ATTGTCAAAG TGCCCTTTTA CATGTCGGAA 1860 GCAACACAGA ATTCGCTGAC GCGTTTCTAC CCTCAGTTCG AACTTAAGTT TTCGCACTCC 1920 TCGCATTCAG ATCATCCCGC CGCCGCCGCT TCTAGACTGC TGGAAAATGA AACGTTAGTG 1980 CGCTTATGTG GTAATAGCGT TTCAGATATT GGAGGTTGTC CTCTTTTCCA TTTGCATTCC 2040 AAGACGCAAA GACGGGTTCA CGTATGTAGG CCTGTGTTGG ATGGCAAGGA TGCGCAGCGT 2100 CGCGTGGTGC GTGATTTGCA GTATTC CAAC GTGCGTTTGG GAGACGATGA TAAAATTTTG 2160 GAAGGGCCAC GCAATATCGA CATTTGCCAC TATCCTCTGG GCGCGTGTGA CCACGAAAGT 2220 AGTGCTATGA TGATGGTGCA GGTGTATGAC GCGTCCCTTT ATGAGATATG TGGCGCCATG 2280 ATCAAGAAGA AAAGCCGCAT AACGTACTTA ACCATGGTCA CGCCCGGCGA GTTTCTTGAC 2340 GGACGCGAAT GCGTCTACAT GGAGTCGTTA GACTGTGAGA TTGAAGTTGA TGTGCACGCG 2400 GACGTCGTAA TGTACAAATT CGGTAGTTCT TGCTATTCGC ACAAGCTTTC AATCATCAAG 2460 GACATCATGA CCACTCCGTA CTTGACACTA GGTGGTTTTC TATTCAGCGT GGAGATGTAT 2520 GAGGTGCGTA TGGGCGTGAA TTACTTCAAG ATTACGAAGT CCGAAGTATC GCCTAGCATT 2580 AGCTGCACCA AGCTCCTGAG ATACCGAAGA GCTAATAGTG ACGTGGTTAA AGTTAAACTT 2640 CCACGTTTCG ATAAGAAACG TCGCATGTGT CTGCCTGGGT ATGACACCAT ATACCTAGAT 2700 TCGAAGTTTG TGAGTCGCGT TTTCGATTAT GTCGTGTGTA ATTGCTCTGC CGTGAACTCA 2760 AAAACTTTCG AGTGGGTGTG GAGTTTCATT AAGTCTAGTA AGTCGAGGGT GATTATTAGC 2820 GGTAAAATAA TTCACAAGGA TGTGAATTTG GACCTCAAGT ACGTCGAGAG TTTCGCCGCG 2880 GTTATGTTGG CCTCTGGCGT GCGCAGTAGA CTAGCGTCCG AGTACCTTGC TAAGAACCTT 2940 AGTCATTTTT CGGGAGATT G CTCCTTTATT GAAGCCACGT CTTTCGTGTT GCGTGAGÁAA 3000 ATCAGAAACA TGACTCTGAA TTTTAACGAA AGACTTTTAC AGTTAGTGAA GCGCGTTGCC 3060 TTTGCGACCT TGGACGTGAG TTTTCTAGAT TTAGATTCAA CTCTTGAATC AATAACTGAT 3120 TTTGCCGAGT GTAAGGTAGC GATTGAACTC GACGAGTTGG GTTGCTTGAG AGCGGAGGCC 3180 GAGAATGAAA AAATCAGGAA TCTGGCGGGA GATTCGATTG CGGCTAAACT CGCGAGCGAG 3240 ATAGTGGTCG ATATTGACTC TAAGCCTTCA CCGAAGCAGG TGGGTAATTC GTCATCCGAA 3300 AACGCCGATA AGCGGGAAGT TCAGAGGCCC GGTTTGCGTG GTGGTTCTAG AAACGGGGTT 3360 GTTGGGGAGT TCCTTCACTT CGTCGTGGAT TCTGCCTTGC GTCTTTTCAA ATACGCGACG 3420 GATCAACAAC GGATCAAGTC TTACGTGCGT TTCTTGGACT CGGCGGTCTC ATTCTTGGAT 3480 TACAACTACG ATAATCTATC GTTTATACTG CGAGTGCTTT CGGAAGGTTA TTCGTGTATG 3540 TTCGCGTTTT TGGCGAATCG CGGCGACTTA TCTAGTCGTG TCCGTAGCGC GGTGTGTGCT 3600 GTGAAAGAAG TTGCTACCTC ATGCGCGAAC GCGAGCGTTT CTAAAGCCAA GGTTATGATT 3660 ACCTTCGCAG CGGCCGTGTG TGCTATGATG TTTAATAGCT GCGGTTTTTC AGGCGACGGT 3720 CGGGAGTATA AATCGTATAT ACATCGTTAC ACGCAAGTAT TGTTTGACAC TATCTTTTTT 3780 GAGGACAGCA GTTACCTACC CA TAGAAGTT CTGAGTTCGG CGATATGCGG TGCTATCGTC 3840 ACACTTTTCT CCTCGGGCTC GTCCATAAGT TTAAACGCCT TCTTACTTCA AATTACCAAA 3900 GGATTCTCCC TAGAGGTTGT CGTCCGGAAT GTTGTGCGAG TCACGCATGG TTTGAGCACC 3960 ACAGCGACCG ACGGCGTCAT ACGTGGGGTT TTCTCCCAAA TTGTGTCTCA CTTACTTGTT 4020 GGAAATACGG GTAATGTGGC TTACCAGTCA GCTTTCATTG CCGGGGTGGT GCCTCTTTTA 4080 GTTAAAAAGT GTGTGAGCTT AATCTTCATC TTGCGTGAAG ATACTTATTC CGGTTTTATT 4140 AAGCACGGAA TCAGTGAATT CTCTTTCCTT AGTAGTATTC TGAAGTTCTT GAAGGGTAAG 4200 CTTGTGGACG AGTTGAAATC GATTATTCAA GGGGTTTTTG ATTCCAACAA GCACGTGTTT 4260 AAAGAAGCTA CTCAGGAAGC GATTCGTACG ACGGTCATGC AAGTGCCTGT CGCTGTAGTG 4320 GATGCCCTTA AGAGCGCCGC GGGAAAAATT TATAACAATT TTACTAGTCG ACGTACCTTT 4380 GGTAAGGATG AAGGCTCCTC TAGCGACGGC GCATGTGAAG AGTATTTCTC ATGCGACGAA 4440 GGTGAAGGTC CGGGTCTGAA AGGGGGTTCC AGCTATGGCT TCTCAATTTT AGCGTTCTTT 4500 TCACGCATTA TGTGGGGAGC TCGTCGGCTT ATTGTTAAGG TGAAGCATGA GTGTTTTGGG 4560 AAACTTTTTG AATTTCTATC GCTCAAGCTT CACGAATTCA GGACTCGCGT TTTTGGGAAG 4620 AATAGAACGG ACGTG GGAGT TTACGATTTT TTGCCCACGG GCATCGTGGA AACGCTCTCA 4680 TCGATAGAAG AGTGCGACCA AATTGAAGAA CTTCTCGGCG ACGACCTGAA AGGTGACAAG 4740 GATGCTTCGT TGACCGATAT GAATTACTTT GAGTTCTCAG AAGACTTCTT AGCCTCTATC 4800 GAGGAGCCGC CTTTCGCTGG ATTGCGAGGA GGTAGCAAGA ACATCGCGAT TTTGGCGATT 4860 TTGGAATACG CGCATAATTT GTTTCGCATT GTCGCAAGCA AGTGTTCGAA ACGACCTTTA 4920 TTTCTTGCTT TCGCCGAACT CTCAAGCGCC CTTATCGAGA AATTTAAGGA GGTTTTCCCT 4980 CGTAAGAGCC AGCTCGTCGC TATCGTGCGC GAGTATACTC AGAGATTCCT CCGAAGTCGC 5040 ATGCGTGCGT TGGGTTTGAA TAACGAGTTC GTGGTAAAAT CTTTCGCCGA TTTGCTACCC 5100 GCATTAATGA AGCGGAAGGT TTCAGGTTCG TTCTTAGCTA GTGTTTATCG CCCACTTAGA 5160 GGTTTCTCAT ATATGTGTGT TTCAGCGGAG CGACGTGAAA AGTTTTTTGC TCTCGTGTGT 5220 TTAATCGGGT TAAGTCTCCC TTTCTTCGTG CGCATCGTAG GAGCGAAAGC GTGCGAAGAA 5280 CTCGTGTCCT CAGCGCGTCG CTTTTATGAG CGTATTAAAA TTTTTCTAAG GCAGAAGTAT 5340 GTCTCTCTTT CTAATTTCTT TTGTCACTTG TTTAGCTCTG ACGTTGATGA CAGTTCCGCA 5400 TCTGCAGGGT TGAAAGGTGG TGCGTCGCGA ATGACGCTCT TCCACCTTCT GGTTCGCCTT 5460 GCTAGTGC CC TCCTATCGTT AGGGTGGGAA GGGTTAAAGC TACTCTTATC GCACCACAAC 5520 TTGTTATTTT TGTGTTTTGC ATTGGTTGAC GATGTGAACG TCCTTATCAA AGTTCTTGGG 5580 GGTCTTTCTT TCTTTGTGCA ACCAATCTTT TCCTTGTTTG CGGCGATGCT TCTACAACCG 5640 GACAGGTTTG TGGAGTATTC CGAGAAACTT GTTACAGCGT TTGAATTTTT CTTAAAATGT 5700 TCGCCTCGCG CGCCTGCACT ACTCAAAGGG TTTTTTGAGT GCGTGGCGAA CAGCACTGTG 5760 TCAAAAACCG TTCGAAGACT TCTTCGCTGT TTCGTGAAGA TGCTCAAACT TCGAAAAGGG 5820 CGAGGGTTGC GTGCGGATGG TAGGGGTCTC CATCGGCAGA AAGCCGTACC CGTCATACCT 5880 TCTAATCGGG TCGTGACCGA CGGGGTTGAA AGACTTTCGG TAAAGATGCA AGGAGTTGAA 5940 GCGTTGCGTA CCGAATTGAG AATCTTAGAA GATTTAGATT CTGCCGTGAT CGAAAAACTC 6000 AATAGACGCA GAAATCGTGA CACTAATGAC GACGAATTTA CGCGCCCTGC TCATGAGCAG 6060 ATGCAAGAAG TCACCACTTT CTGTTCGAAA GCCAACTCTG CTGGTTTGGC CCTGGAAAGG 6120 GCAGTGCTTG TGGAAGACGC TATAAAGTCG GAGAAACTTT CTAAGACGGT TAATGAGATG 6180 GTGAGGAAAG GGAGTACCAC CAGCGAAGAA GTGGCCGTCG CTTTGTCGGA CGATGAAGCC 6240 GTGGAAGAAA TCTCTGTTGC TGACGAGCGA GACGATTCGC CTAAGACAGT CAGGATAAGC 6300 GAATACCTAA ATAGGTTAAA CTCAAGCTTC GAATTCCCGA AGCCTATTGT TGTGGACGAC 6360 AACAAGGATA CCGGGGGTCT AACGAACGCC GTGAGGGAGT TTTATTATAT GCAAGAACTT 6420 GCTCTTTTCG AAATCCACAG CAAACTGTGC ACCTACTACG ATCAACTGCG CATAGTCAAC 6480 TTCGATCGTT CCGTAGCACC ATGCAGCGAA GATGCTCAGC TGTACGTACG GAAGAACGGC 6540 TCAACGATAG TGCAGGGTAA AGAGGTACGT TTGCACATTA AGGATTTCCA CGATCACGAT 6600 TTCCTGTTTG ACGGAAAAAT TTCTATTAAC AAGCGGCGGC GAGGCGGAAA TGTTTTATAT 6660 CACGACAACC TCGCGTTCTT GGCGAGTAAT TTGTTCTTAG CCGGCTACCC CTTTTCAAGG 6720 AGCTTCGTCT TCACGAATTC GTCGGTCGAT ATTCTCCTCT ACGAAGCTCC ACCCGGAGGT 6780 GGTAAGACGA CGACGCTGAT TGACTCGTTC TTGAAGGTCT TCAAGAAAGG TGAGGTTTCC 6840 ACCATGATCT TAACCGCCAA CAAAAGTTCG CAGGTTGAGA TCCTAAAGAA AGTGGAGAAG 6900 GAAGTGTCTA ACATTGAATG CCAGAAACGT AAAGACAAAA GATCTCCGAA AAAGAGCATT 6960 TACACCATCG ACGCTTATTT AATGCATCAC CGTGGTTGTG ATGCAGACGT TCTTTTCATC 7020 GATGAGTGTT TCATGGTTCA TGCGGGTAGC GTACTAGCTT GCATTGAGTT CACGAGGTGT 7080 CATAAAGTAA TGATCTTCGG GGATAGCCGG CAGATTCACT ACATTGAAAG GAACGAATTG 7140 GAC AAGTGTT TGTATGGGGA TCTCGACAGG TTCGTGGACC TGCAGTGTCG GGTTTATGGT 7200 AATATTTCGT ACCGTTGTCC ATGGGATGTG TGCGCTTGGT TAAGCACAGT GTATGGCAAC 7260 CTAATCGCCA CCGTGAAGGG TGAAAGCGAA GGTAAGAGCA GCATGCGCAT TAACGAAATT 7320 AATTCAGTCG ACGATTTAGT CCCCGACGTG GGTTCCACGT TTCTGTGTAT GCTTCAGTCG 7380 GAGAAGTTGG AAATCAGCAA GCACTTTATT CGCAAGGGTT TGACTAAACT TAACGTTCTA 7440 ACGGTGCATG AGGCGCAAGG TGAGACGTAT GCGCGTGTGA ACCTTGTGCG ACTTAAGTTT 7500 CAGGAGGATG AACCCTTTAA ATCTATCAGG CACATAACCG TCGCTCTTTC TCGTCACACC 7560 GACAGCTTAA CTTATAACGT CTTAGCTGCT CGTCGAGGTG ACGCCACTTG CGATGCCATC 7620 CAGAAGGCTG CGGAATTGGT GAACAAGTTT CGCGTTTTTC CTACATCTTT TGGTGGTAGT 7680 GTTATCAATC TCAACGTGAA GAAGGACGTG GAAGATAACA GTAGGTGCAA GGCTTCGTCG 7740 GCACCATTGA GCGTAATCAA CGACTTTTTG AACGAAGTTA ATCCCGGTAC TGCGGTGATT 7800 GATTTTGGTG ATTTGTCCGC GGACTTCAGT ACTGGGCCTT TTGAGTGCGG TGCCAGCGGT 7860 ATTGTGGTGC GGGACAACAT CTCCTCCAGC AACATCACTG ATCACGATAA GCAGCGTGTT 7920 TAGCGTAGTT CGGTCGCAGG CGATTCCGCG TAGAAAACCT TCTCTACAAG AAAATTTGTA 7 980 TTCGTTTGAA GCGCGGAATT ATAACTTCTC GACTTGCGAC CGTAACACAT CTGCTTCAAT 8040 GTTCGGAGAG GCTATGGCGA TGAACTGTCT TCGTCGTTGC TTCGACCTAG ATGCCTTTTC 8100 GTCCCTGCGT GATGATGTGA TTAGTATCAC ACGTTCAGGC ATCGAACAAT GGCTGGAGAA 8160 ACGTACTCCT AGTCAGATTA AAGCATTAAT GAAGGATGTT GAATCGCCTT TGGAAATTGA 8220 CGATGAAATT TGTCGTTTTA AGTTGATGGT GAAGCGTGAC GCTAAGGTGA AGTTAGACTC 8280 TTCTTGTTTA ACTAAACACA GCGCCGCTCA AAATATCATG TTTCATCGCA AGAGCATTAA 8340 TGCTATCTTC TCTCCTATCT TTAATGAGGT GAAAAACCGA ATAATGTGCT GTCTTAAGCC 8400 TAACATAAAG TTTTTTACGG AGATGACTAA CAGGGATTTT GCTTCTGTTG TCAGCAACAT 8460 GCTTGGTGAC GACGATGTGT ACCATATAGG TGAAGTTGAT TTCTCAAAGT ACGACAAGTC 8520 TCAAGATGCT TTCGTGAAGG CTTTTGAAGA AGTAATGTAT AAGGAACTCG GTGTTGATGA 8580 AGAGTTGCTG GCTATCTGGA TGTGCGGCGA GCGGTTATCG ATAGCTAACA CTCTCGATGG 8640 TCAGTTGTCC TTCACGATCG AGAATCAAAG GAAGTCGGGA GCTTCGAACA CTTGGATTGG 8700 TAACTCTCTC GTCACTTTGG GTATTTTAAG TCTTTACTAC GACGTTAGAA ATTTCGAGGC 8760 GTTGTACATC TCGGGCGATG ATTCTTTAAT TTTTTCTCGC AGCGAGATTT CGAA TTATGC 8820 CGACGACATA TGCACTGACA TGGGTTTTGA GACAAAATTT ATGTCCCCAA GTGTCCCGTA 8880 CTTTTGTTCT AAATTTGTTG TTATGTGTGG TCATAAGACG TTTTTTGTTC CCGACCCGTA 8940 CAAGCTTTTT GTCAAGTTGG GAGCAGTCAA AGAGGATGTT TCAATGGATT TCCTTTTCGA 9000 GACTTTTACC TCCTTTAAAG ACTTAACCTC CGATTTTAAC GACGAGCGCT TAATTCAAAA 9060 GCTCGCTGAA CTTGTGGCTT TAAAATATGA GGTTCAAACC GGCAACACCA CCTTGGCGTT 9120 AAGTGTGATA CATTGTTTGC GTTCGAATTT CCTCTCGTTT AGCAAGTTAT ATCCTCGCGT 9180 GAAGGGATGG CAGGTTTTTT ACACGTCGGT TAAGAAAGCG CTTCTCAAGA GTGGGTGTTC 9240 TCTCTTCGAC AGTTTCATGA CCCCTTTTGG TCAGGCTGTC ATGGTTTGGG ATGATGAGTA 9300 GCGCTAACTT GTGCGCAGTT TCTTTGTTCG TGACATACAC CTTGTGTGTC ACCGTGCGTT 9360 TATAATGAAT CAGGTTTTGC AGTTTGAATG TTTGTTTCTG CTGAATCTCG CGGTTTTTGC 9420 TGTGACTTTC ATTTTCATTC TTCTGGTCTT CCGCGTGATT AAGTCTTTTC GCCAGAAGGG 9480 TCACGAAGCA CCTGTTCCCG TTGTTCGTGG CGGGGGTTTT TCAACCGTAG TGTAGTCAAA 9540 AGACGCGCAT ATGGTAGTTT TCGGTTTGGA CTTTGGCACC ACATTCTCTA CGGTGTGTGT 9600 GTACAAGGAT GGACGAGTTT TTTCATTCAA GCAGAATAAT TCGGCGT HERE9660 CCTCTATCTC TTCTCCGATT CTAACCACAT GACTTTTGGT TACGAGGCCG AATCACTGAT 9720 GAGTAATCTG AAAGTTAAAG GTTCGTTTTA TAGAGATTTA AAACGTTGGG TGGGTTGCGA 9780 TTCGAGTAAC CTCGACGCGT ACCTTGACCG TTTAAAACCT CATTACTCGG TCCGCTTGGT 9840 TAAGATCGGC TCTGGCTTGA ACGAAACTGT TTCAATTGGA AACTTCGGGG GCACTGTTAA 9900 GTCTGAGGCT CATCTGCCAG GGTTGATAGC TCTCTTTATT AAGGCTGTCA TTAGTTGCGC 9960 GGAGGGCGCG TTTGCGTGCA CTTGCACCGG GGTTATTTGT TCAGTACCTG CCAATTATGA 10020 TAGCGTTCAA AGGAATTTCA CTGATCAGTG TGTTTCACTC AGCGGTTATC AGTGCGTATA 10080 TATGATCAAT GAACCTTCAG CGGCTGCGCT ATCTGCGTGT AATTCGATTG GAAAGAAGTC 10140 CGCAAATTTG GCTGTTTACG ATTTCGGTGG TGGGACCTTC GACGTGTCTA TCATTTCATA 10200 CCGCAACAAT ACTTTTGTTG TGCGAGCTTC TGGAGGCGAT CTAAATCTCG GTGGAAGGGA 10260 TGTTGATCGT GCGTTTCTCA CGCACCTCTT CTCTTTAACA TCGCTGGAAC CTGACCTCAC 10320 TTTGGATATC TCGAATCTGA AAGAATCTTT ATCAAAAACG GACGCAGAGA TAGTTTACAC 10380 TTTGAGAGGT GTCGATGGAA GAAAAGAAGA CGTTAGAGTA AACAAAAACA TTCTTACGTC 10440 GGTGATGCTC CCCTACGTGA ACAGAACGCT TAAGAT ATTA GAGTCAACCT TAAAATCGTA 10500 TGCTAAGAGT ATGAATGAGA GTGCGCGAGT TAAGTGCGAT TTAGTGCTGA TAGGAGGATC 10560 TTCATATCTT CCTGGCCTGG CAGACGTACT AACGAAGCAT CAGAGCGTTG ATCGTATCTT 10620 AAGAGTTTCG GATCCTCGGG CTGCCGTGGC CGTCGGTTGC GCATTATATT CTTCATGCCT 10680 CTCAGGATCT GGGGGGTTGC TACTGATCGA CTGTGCAGCT CACACTGTCG CTATAGCGGA 10740 CAGAAGTTGT CATCAAATCA TTTGCGCTCC AGCGGGGGCA CCGATCCCCT TTTCAGGAAG 10800 CATGCCTTTG TACTTAGCCA GGGTCAACAA GAACTCGCAG CGTGAAGTCG CCGTGTTTGA 10860 AGGGGAGTAC GTTAAGTGCC CTAAGAACAG AAAGATCTGT GGAGCAAATA TAAGATTTTT 10920 TGATATAGGA GTGACGGGTG ATTCGTACGC ACCCGTTACC TTCTATATGG ATTTCTCCAT 10980 TTCAAGCGTA GGAGCCGTTT CATTCGTGGT GAGAGGTCCT GAGGGTAAGC AAGTGTCACT 11040 CACTGGAACT CCAGCGTATA ACTTTTCGTC TGTGGCTCTC GGATCACGCA GTGTCCGAGA 11100 ATTGCATATT AGTTTAAATA ATAAAGTTTT TCTCGGTTTG CTTCTACATA GAAAGGCGGA 11160 TCGACGAATA CTTTTCACTA AGGATGAAGC GATTCGATAC GCCGATTCAA TTGATATCGC 11220 GGATGTGCTA AAGGAATATA AAAGTTACGC GGCCAGTGCC TTACCACCAG ACGAGGATGT 11280 CGAATTACTC CTGGGA AAGT CTGTTCAAAA AGTTTTACGG GGAAGCAGAC TGGAAGAAAT 11340 ACCTCTCTAG GAGCATAGCA GCACACTCAA GTGAAATTAA AACTCTACCA GACATTCGAT 11400 TGTACGGCGG TAGGGTTGTA AAGAAGTCCG AATTCGAATC AGCACTTCCT AATTCTTTTG 11460 AACAGGAATT AGGACTGTTC ATACTGAGCG AACGGGAAGT GGGATGGAGC AAATTATGCG 11520 GAATAACGGT GGAAGAAGCA GCATACGATC TTACGAATCC CAAGGCTTAT AAATTCACTG 11580 CCGAGACATG TAGCCCGGAT GTAAAAGGTG AAGGACAAAA ATACTCTATG GAAGACGTGA 11640 TGAATTTCAT GCGTTTATCA AATCTGGATG TTAACGACAA GATGCTGACG GAACAGTGTT 11700 GGTCGCTGTC CAATTCATGC GGTGAATTGA TCAACCCAGA CGACAAAGGG CGATTCGTGG 11760 CTCTCACCTT TAAGGACAGA GACACAGCTG ATGACACGGG TGCCGCCAAC GTGGAATGTC January 1820 CTATCTAGTT GCGTGGGCGA TACGCTATGT CCCTGTTTGA GCAGAGGACC CAAAAATCGC 11880 AGTCTGGCAA CATCTCTCTG TACGAAAAGT ACTGTGAATA CATCAGGACC TACTTAGGGA January 1940 GTACAGACCT GTTCTTCACA GCGCCGGACA GGATTCCGTT ACTTACGGGC ATCCTATACG 12000 ATTTTTGTAA GGAATACAAC GTTTTCTACT CGTCATATAA GAGAAACGTC GATAATTTCA 12060 GATTCTTCTT GGCGAATTAT ATGCCTTTGA TATCTGACGT CTTTGTCTTC CAGTGGGTAA 12120 AACCCGCGCC GGATGTTCGG CTGCTTTTTG AGTTAAGTGC AGCGGAACTA ACGCTGGAGG 12180 TTCCCACACT GAGTTTGATA GATTCTCAAG TTGTGGTAGG TCATATCTTA AGATACGTAG_12240_AATCCTACAC ATCAGATCCA GCCATCGACG CGTTAGAAGA CAAACTGGAA GCGATACTGA 12300 AAAGTAGCAA TCCCCGTCTA TCGACAGCGC AACTATGGGT TGGTTTCTTT TGTTACTATG 12360 GTGAGTTTCG TACGGCTCAA AGTAGAGTAG TGCAAAGACC AGGCGTATAC AAAACACCTG 12420 ACTCAGTGGG TGGATTTGAA ATAAACATGA AAGATGTTGA GAAATTCTTC GATAAACTTC 12480 AGAGAGAATT GCCTAATGTA TCTTTGCGGC GTCAGTTTAA CGGAGCTAGA GCGCATGAGG 12540 CTTTCAAAAT ATTTAAAAAC GGAAATATAA GTTTCAGACC TATATCGCGT TTAAACGTGC 12600 CTAGAGAGTT CTGGTATCTG AACATAGACT ACTTCAGGCA CGCGAATAGG TCCGGGTTAA 12660 CCGAAGAAGA AATACTCATC CTAAACAACA TAAGCGTTGA TGTTAGGAAG TTATGCGCTG 12720 AGAGAGCGTG CAATACCCTA CCTAGCGCGA AGCGCTTTAG TAAAAATCAT AAGAGTAATA 12780 TACAATCATC ACGCCAAGAG CGGAGGATTA AAGACCCATT GGTAGTCCTG AAAGACACTT 12840 TATATGAGTT CCAACACAAG CGTGCCGGTT GGGGGTCTCG AAGCACTCGA GACCTCGGGA 12900 GTCGTGCTGA CCACGCGAAA GGAAGCGGTT GATAAGTTTT TTAATGAACT12960 AATTACTCAT CAGTTGACAG CAGCCGATTA AGCGATTCGG AAGTAAAAGA AGTGTTAGAG 13020 AAAAGTAAAG AAAGTTTCAA AAGCGAACTG GCCTCCACTG ACGAGCACTT CGTCTACCAC 13080 ATTATATTTT TCTTAATCCG ATGTGCTAAG ATATCGACAA GTGAAAAGGT GAAGTACGTT 13140 GGTAGTCATA CGTACGTGGT CGACGGAAAA ACGTACACCG TTCTTGACGC TTGGGTATTC 13200 AACATGATGA AAAGTCTCAC GAAGAAGTAC AAACGAGTGA ATGGTCTGCG TGCGTTCTGT 13260 TGCGCGTGCG AAGATCTATA TCTAACCGTC GCACCAATAA TGTCAGAACG CTTTAAGACT 13320 AAAGCCGTAG GGATGAAAGG TTTGCCTGTT GGAAAGGAAT ACTTAGGCGC CGACTTTCTT 13380 TCGGGAACTA GCAAACTGAT GAGCGATCAC GACAGGGCGG TCTCCATCGT TGCAGCGAAA 13440 AACGCTGTCG ATCGTAGCGC TTTCACGGGT GGGGAGAGAA AGATAGTTAG TTTGTATGAT 13500 CTAGGGAGGT ACTAAGCACG GTGTGCTATA GTGCGTGCTA TAATAATAAA CACTAGTGCT 13560 TAAGTCGCGC AGAAGAAAAC GCTATGGAGT TGATGTCCGA CAGCAACCTT AGCAACCTGG 13620 TGATAACCGA CGCCTCTAGT CTAAATGGTG TCGACAAGAA GCTTTTATCT GCTGAAGTTG 13680 AAAAAATGTT GGTGCAGAAA GGGGCTCCTA ACGAGGGTAT AGAAGTGGTG TTCGGTCTAC 13740 TCCTTTACGC ACTCGCGGCA AGAACCACGT CTCCTAAGGT TCAGCGCGCA GATTCAGACG 13800 TTATATTTTC AAATAGTTTC GGAGAGAGGA ATGTGGTAGT AACAGAGGGT GACCTTAAGA 13860 AGGTACTCGA CGGGTGTGCG CCTCTCACTA GGTTCACTAA TAAACTTAGA ACGTTCGGTC 13920 GTACTTTCAC TGAGGCTTAC GTTGACTTTT GTATCGCGTA TAAGCACAAA TTACCCCAAC 13980 TCAACGCCGC GGCGGAATTG GGGATTCCAG CTGAAGATTC GTACTTAGCT GCAGATTTTC 14040 TGGGTACTTG CCCGAAGCTC TCTGAATTAC AGCAAAGTAG GAAGATGTTC GCGAGTATGT 14100 ACGCTCTAAA AACTGAAGGT GGAGTGGTAA ATACACCAGT GAGCAATCTG CGTCAGCTAG_14160_GTAGAAGGGA AGTTATGTAA TGGAAGATTA CGAAGAAAAA TCCGAATCGC TCATACTGCT 14220 ACGCACGAAT CTGAACACTA TGCTTTTAGT GGTCAAGTCC GATGCTAGTG TAGAGCTGCC 14280 TAAACTACTA ATTTGCGGTT ACTTACGAGT GTCAGGACGT GGGGAGGTGA CGTGTTGCAA 14340 CCGTGAGGAA TTAACAAGAG ATTTTGAGGG CAATCATCAT ACGGTGATCC GTTCTAGAAT 14400 CATACAATAT GACAGCGAGT CTGCTTTTGA GGAATTCAAC AACTCTGATT GCGTAGTGAA 14460 GTTTTTCCTA GAGACTGGTA GTGTCTTTTG GTTTTTCCTT CGAAGTGAAA CCAAAGGTAG_14520_AGCGGTGCGA CATTTGCGCA CCTTCTTCGA AGCTAACAAT TTCTTCTTTG GATCGCATTG 14580 CGGTACCATG GAGTATTGTT TGAAGCAGGT ACTAACTGAA ACTGAATCTA TAATCGATTC 14640 TTTTTGCGAA GAAAGAAATC GTTAAGATGA GGGTTATAGT GTCTCCTTAT GAAGCTGAAG 14700 ACATTCTGAA AAGATCGACT GACATGTTAC GAAACATAGA CAGTGGGGTC TTGAGCACTA 14760 AAGAATGTAT CAAGGCATTC TCGACGATAA CGCGAGACCT ACATTGTGCG AAGGCTTCCT 14820 ACCAGTGGGG TGTTGACACT GGGTTATATC AGCGTAATTG CGCTGAAAAA CGTTTAATTG 14880 ACACGGTGGA GTCAAACATA CGGTTGGCTC AACCTCTCGT GCGTGAAAAA GTGGCGGTTC 14940 ATTTTTGTAA GGATGAACCA AAAGAGCTAG TAGCATTCAT CACGCGAAAG TACGTGGAAC 15000 TCACGGGCGT GGGAGTGAGA GAAGCGGTGA AGAGGGAAAT GCGCTCTCTT ACCAAAACAG 15060 TTTTAAATAA AATGTCTTTG GAAATGGCGT TTTACATGTC ACCACGAGCG TGGAAAAACG 15120 CTGAATGGTT AGAACTAAAA TTTTCACCTG TGAAAATCTT TAGAGATCTG CTATTAGACG 15180 TGGAAACGCT CAACGAATTG TGCGCCGAAG ATGATGTTCA CGTCGACAAA GTAAATGAGA 15240 ATGGGGACGA AAATCACGAC CTCGAACTCC AAGACGAATG TTAAACATTG GTTAAGTTTA 15300 ACGAAAATGA TTAGTAAATA ATAAATCGAA CGTGGGTGTA TCTACCTGAC GTATCAACTT 15360 AAGCTGTTAC TGAGTAATTA AACCAACAAG TGTTGGTGTA ATGTGTATGT TGATGTA GAG 15420 AAAAATCCGT TTGTAGAACG GTGTTTTTCT CTTCTTTATT TTTAAAAAAA AAATAAAAAA 15480 AAAAAAAAAA AAGCGGCCCCC 15500 (2) INFORMATION FOR SEQ ID NO: 2: (i) CHARACTERISTICS OF THE SEQUENCE: (A) Length: 7920 base pairs (B) Type: nucleic acid (C) ) Chain type: simple (D) Topology: linear (ii) TYPE OF MOLECULE: cDNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 2: ACATTGCGAG AGAACCCCAT TAGCGTCTCC GGGGTGAACT TGGGAAGGTC TGCCGCCGCT 60 CAGGTTATTT ATTTCGGCAG TTTCACGCAG CCCTTCGCGT TGTATCCGCG CCAAGAGAGC 120 GCGATCGTAA AAACGCAACT TCCACCGGTC AGTGTAGTGA AGGTGGAGTG CGTAGCTGCG 180 GAGGTAGCTC CCGACAGGGG CGTGGTCGAC AAGAAACCTA CGTCTGTTGG CGTTCCCCCG 240 CAGCGCGGTG TGCTTTCTTT TCCGACGGTG GTTCGGAACC GCGGCGACGT GATAATCACA 300 GGGGTGGTGC ATGAAGCCCT GAAGAAAATT AAAGACGGGC TCTTACGCTT CCGCGTAGGC 360 GGTGACATGC GTTTTTCGAG ATTTTTCTCA TCGAACTACG GCTGCAGATT CGTCGCGAGC 420 GTGCGTACGA ACACTACAGT TTGGCTAAAT TGCACGAAAG CGAGTGGTGA GAAATTCTCA 480 CTCGCCGCCG CGTGCACGGC GGATTACGTG GCGATGCTGC GTTATGTGTG TGGCGGGAAA 540 TTTCCACTCG TCCTCATGAG TAGAGTTATT TACCCGGATG GGCGCTGTTA CTTGGCCCAT 600 ATGAGGTATT TGTGCGCCTT TTACTGTCGC CCGTTTAGAG AGTCGGATTA TGCCCTCGGA 660 ATGTGGCCTA CGGTGGCGCG TCTCAGGGCA TGCGTTGAGA AGAACTTCGG TGTCGAAGCT 720 TGTGGCATAG CTCTTCGTGG CTATTACACC TCTCGCAATG TTTATCACTG TGATTATGAC 780 TCTGCTTATG TAAAATATTT TAGAAACCTT TCCGGCCGCA TTGGCGGTGG TTCGTTCGAT 840 CCGACATCTT TAACCTCCGT AATAACGGTG AAGATTAGCG GTCTTCCAGG TGGTCTTCCT 900 AAAAATATAG CGTTTGGTGC CTTCCTGTGC GATATACGTT ACGTCGAACC GGTAGACTCG 960.

GGCGGCATTC AATCGAGCGT TAAGACGAAA CGTGAAGATG CGCACCGAAC CGTAGAGGAA 1020 CGGGCGGCCG GCGGATCCGT CGAGCAACCG CGACAAAAGA GGATAGATGA GAAAGGTTGC 1080 GGCAGAGTTC CTAGTGGAGG TTTTTCGCAT CTCCTGGTCG GCAACCTTAA CGAAGTTAGG 1140 AGGAAGGTAG CTGCCGGACT TCTACGCTTT CGCGTTGGCG GTGATATGGA TTTTCATCGC 1200 TCGTTCTCCA CCCAAGCGGG CCACCGCTTG CTGGTGTGGC GCCGCTCGAG CCGGAGCGTG 1260 TGCCTTGAAC TTTACTCACC ATCTAAAAAC TTTTTGCGTT ACGATGTCTT GCCCTGTTCT 1320 GGAGACTATG CAGCGATGTT TTCTTTCGCG GCGGGCGGCC GTTTCCCTTT AGTTTTGATG 1380 ACTAGAATTA GATACCCGAA CGGGTTTTGT TACTTGGCTC ACTGCCGGTA CGCGTGCGCG 1440 TTTCTCTTAA GGGGTTTTGA TCCGAAGCGT TTCGACATCG GTGCTTTCCC CACCGCGGCC 1500 AAGCTCAGAA ACCGTATGGT TTCGGAGCTT GGTGAAAGAA GTTTAGGTTT GAACTTGTAC 1560 GGCGCATATA CGTCACGCGG CGTCTTTCAC TGCGATTATG ACGCTAAGTT TATAAAGGAT 1620 TTGCGTCTTA TGTCAGCAGT TATAGCTGGA AAGGACGGGG TGGAAGAGGT GGTACCTTCT 1680 GACATAACTC CTGCCATGAA GCAGAAAACG ATCGAAGCCG TGTATGATAG ATTATATGGC 1740 GGCACTGACT CGTTGCTGAA ACTGAGCATC GAGAAAGACT TAATCGATTT CAAAAATGA C 1800 GTGCAGAGTT TGAAGAAAGA TCGGCCGATT GTCAAAGTGC CCTTTTACAT GTCGGAAGCA 1860 ACACAGAATT CGCTGACGCG TTTCTACCCT CAGTTCGAAC TTAAGTTTTC GCACTCCTCG 1920 CATTCAGATC ATCCCGCCGC CGCCGCTTCT AGACTGCTGG AAAATGAAAC GTTAGTGCGC 1980 TTATGTGGTA ATAGCGTTTC AGATATTGGA GGTTGTCCTC TTTTCCATTT GCATTCCAAG 2040 ACGCAAAGAC GGGTTCACGT ATGTAGGCCT GTGTTGGATG GCAAGGATGC GCAGCGTCGC 2100 GTGGTGCGTG ATTTGCAGTA TTCCAACGTG CGTTTGGGAG ACGATGATAA AATTTTGGAA 2160 GGGCCACGCA ATATCGACAT TTGCCACTAT CCTCTGGGCG CGTGTGACCA CGAAAGTAGT 2220 GCTATGATGA TGGTGCAGGT GTATGACGCG TCCCTTTATG AGATATGTGG CGCCATGATC 2280 AAGAAGAAAA GCCGCATAAC GTACTTAACC ATGGTCACGC CCGGCGAGTT TCTTGACGGA 2340 CGCGAATGCG TCTACATGGA GTCGTTAGAC TGTGAGATTG AAGTTGATGT GCACGCGGAC 2400 GTCGTAATGT ACAAATTCGG TAGTTCTTGC TATTCGCACA AGCTTTCAAT CATCAAGGAC 2460 ATCATGACCA CTCCGTACTT GACACTAGGT GGTTTTCTAT TCAGCGTGGA GATGTATGAG 2520 CTTCAAGATT GTGCGTATGG GCGTGAATTA ACGAAGTCCG AAGTATCGCC TAGCATTAGC 2580 TGCACCAAGC TCCTGAGATA CCGAAGAGCT AATAGTGACG TGGTTAAAGT T AAACTTCCA 2640 CGTTTCGATA AGAAACGTCG CATGTGTCTG CCTGGGTATG ACACCATATA CCTAGATTCG 2700 AAGTTTGTGA GTCGCGTTTT CGATTATGTC GTGTGTAATT GCTCTGCCGT GAACTCAAAA 2760 ACTTTCGAGT GGGTGTGGAG TTTCATTAAG TCTAGTAAGT CGAGGGTGAT TATTAGCGGT 2820 AAAATAATTC ACAAGGATGT GAATTTGGAC CTCAAGTACG TCGAGAGTTT CGCCGCGGTT 2880 ATGTTGGCCT CTGGCGTGCG CAGTAGACTA GCGTCCGAGT ACCTTGCTAA GAACCTTAGT 2940 CATTTTTCGG GAGATTGCTC CTTTATTGAA GCCACGTCTT TCGTGTTGCG TGAGAAAATC 3000 AGAAACATGA CTCTGAATTT TAACGAAAGA CTTTTACAGT TAGTGAAGCG CGTTGCCTTT 3060 GCGACCTTGG ACGTGAGTTT TCTAGATTTA GATTCAACTC TTGAATCAAT AACTGATTTT 3120 GCCGAGTGTA AGGTAGCGAT TGAACTCGAC GAGTTGGGTT GCTTGAGAGC GGAGGCCGAG 3180 AATGAAAAAA TCAGGAATCT GGCGGGAGAT TCGATTGCGG CTAAACTCGC GAGCGAGATA 3240 GTGGTCGATA TTGACTCTAA GCCTTCACCG AAGCAGGTGG GTAATTCGTC ATCCGAAAAC 3300 GCCGATAAGC GGGAAGTTCA GAGGCCCGGT TTGCGTGGTG GTTCTAGAAA CGGGGTTGTT 3360 GGGGAGTTCC TTCACTTCGT CGTGGATTCT GCCTTGCGTC TTTTCAAATA CGCGACGGAT 3420 CAACAACGGA TCAAGTCTTA CGTGCGTTTC TTGGACTCGG CGGTCTCATT CTTGGATTAC 3480 AACTACGATA ATCTATCGTT TATACTGCGA GTGCTTTCGG AAGGTTATTC GTGTATGTTC 3540 GCGTTTTTG CGAATCGCGG CGACTTATCT AGTCGTGTCC GTAGCGCGGT GTGTGCTGTG 3600 AAAGAAGTTG CTACCTCATG CGCGAACGCG AGCGTTTCTA AAGCCAAGGT TATGATTACC 3660 TTCGCAGCGG CCGTGTGTGC TATGATGTTT AATAGCTGCG GTTTTTCAGG CGACGGTCGG 3720 GAGTATAAAT CGTATATACA TCGTTACACG CAAGTATTGT TTGACACTAT CTTTTTTGAG 3780 GACAGCAGTT ACCTACCCAT AGAAGTTCTG AGTTCGGCGA TATGCGGTGC TATCGTCACA 3840 CTTTTCTCCT CGGGCTCGTC CATAAGTTTA AACGCCTTCT TACTTCAAAT TACCAAAGGA 3900 TTCTCCCTAG AGGTTGTCGT CCGGAATGTT GTGCGAGTCA CGCATGGTTT GAGCACCACA 3960 GCGACCGACG GCGTCATACG TGGGGTTTTC TCCCAAATTG TGTCTCACTT ACTTGTTGGA 4020 AATACGGGTA ATGTGGCTTA CCAGTCAGCT TTCATTGCCG GGGTGGTGCC TCTTTTAGTT 4080 AAAAAGTGTG TGAGCTTAAT CTTCATCTTG CGTGAAGATA CTTATTCCGG TTTTATTAAG 4140 CACGGAATCA GTGAATTCTC TTTCCTTAGT AGTATTCTGA AGTTCTTGAA GGGTAAGCTT 4200 GTGG ACGAGT TGAAATCGAT TATTCAAGGG GTTTTTGATT CCAACAAGCA CGTGTTTAAA 4260 GAAGCTACTC AGGAAGCGAT TCGTACGACG GTCATGCAAG TGCCTGTCGC TGTAGTGGAT 4320 GCCCTTAAGA GCGCCGCGGG AAAAATTTAT AACAATTTTA CTAGTCGACG TACCTTTGGT 4380 AAGGATGAAG GCTCCTCTAG CGACGGCGCA TGTGAAGAGT ATTTCTCATG CGACGAAGGT 4440 GAAGGTCCGG GTCTGAAAGG GGGTTCCAGC TATGGCTTCT CAATTTTAGC GTTCTTTTCA 4500 CGCATTATGT GGGGAGCTCG TCGGCTTATT GTTAAGGTGA AGCATGAGTG TTTTGGGAAA 4560 CTTTTTGAAT TTCTATCGCT CAAGCTTCAC GAATTCAGGA CTCGCGTTTT TGGGAAGAAT 4620 AGAACGGACG TGGGAGTTTA CGATTTTTTG CCCACGGGCA TCGTGGAAAC GCTCTCATCG 4680 ATAGAAGAGT GCGACCAAAT TGAAGAACTT CTCGGCGACG ACCTGAAAGG TGACAAGGAT 4740 GCTTCGTTGA CCGATATGAA TTACTTTGAG TTCTCAGAAG ACTTCTTAGC CTCTATCGAG 4800 GAGCCGCCTT TCGCTGGATT GCGAGGAGGT AGCAAGAACA TCGCGATTTT GGCGATTTTG 4860 GAATACGCGC ATAATTTGTT TCGCATTGTC GCAAGCAAGT GTTCGAAACG ACCTTTATTT 4920 CTTGCTTTCG CCGAACTCTC AAGCGCCCTT ATCGAGAAAT TTAAGGAGGT TTTCCCTCGT 4980 AAGAGCCAGC TCGTCGCTAT CGTGCGCGAG TATACTCAGA GATTCCTCCG AAGTCGCATG 50 40 CGTGCGTTGG GTTTGAATAA CGAGTTCGTG GTAAAATCTT TCGCCGATTT5100 TTAATGAAGC GGAAGGTTTC AGGTTCGTTC TTAGCTAGTG TTTATCGCCC ACTTAGAGGT 5160 TTCTCATATA TGTGTGTTTC AGCGGAGCGA CGTGAAAAGT TTTTTGCTCT CGTGTGTTTA 5220 ATCGGGTTAA GTCTCCCTTT CTTCGTGCGC ATCGTAGGAG CGAAAGCGTG CGAAGAACTC 5280 GTGTCCTCAG CGCGTCGCTT TTATGAGCGT ATTAAAATTT TTCTAAGGCA GAAGTATGTC 5340 TCTCTTTCTA ATTTCTTTTG TCACTTGTTT AGCTCTGACG TTGATGACAG TTCCGCATCT 5400 GCAGGGTTGA AAGGTGGTGC GTCGCGAATG ACGCTCTTCC ACCTTCTGGT TCGCCTTGCT 5460 AGTGCCCTCC TATCGTTAGG GTGGGAAGGG TTAAAGCTAC TCTTATCGCA CCACAACTTG 5520 TTATTTTTGT GTTTTGCATT GGTTGACGAT GTGAACGTCC TTATCAAAGT TCTTGGGGGT 5580 CTTTCTTTCT TTGTGC AACC AATCTTTTCC TTGTTTGCGG CGATGCTTCT ACAACC-GGAC 5640 AGGTTTGTGG AGTATTCCGA GAAACTTGTT ACAGCGTTTG AATTTTTCTT AAAATGTTCG 5700 CCTCGCGCGC CTGCACTACT CAAAGGGTTT TTTGAGTGCG TGGCGAACAG CACTGTGTCA 5760 AAAACCGTTC GAAGACTTCT TCGCTGTTTC GTGAAGATGC TCAAACTTCG AAAAGGGCGA 5820 GGGTTGCGTG CGGATGGTAG GGGTCTCCAT CGGCAGAAAG CCGTACCCGT CATACCTTCT 5880 AATCGGGTCG TGACCGACGG GGTTGAAAGA CTTTCGGTAA AGATGCAAGG AGTTGAAGCG 5940 TTGCGTACCG AATTGAGAAT CTTAGAAGAT TTAGATTCTG CCGTGATCGA AAAACTCAAT 6000 AGACGCAGAA ATCGTGACAC TAATGACGAC GAATTTACGC GCCCTGCTCA TGAGCAGATG 6060 CAAGAAGTCA CCACTTTCTG TTCGAAAGCC AACTCTGCTG GTTTGGCCCT GGAAAGGGCA 6120 GTGCTTGTGG AAGACGCTAT AAAGTCGGAG AAACTTTCTA AGACGGTTAA TGAGATGGTG 6180 AGGAAAGGGA GTACCACCAG CGAAGAAGTG GCCGTCGCTT TGTCGGACGA TGAAGCCGTG 6240 GAAGAAATCT CTGTTGCTGA CGAGCGAGAC GATTCGCCTA AGACAGTCAG GATAAGCGAA 6300 TACCTAAATA GGTTAAACTC AAGCTTCGAA TTCCCGAAGC CTATTGTTGT GGACGACAAC 6360 AAGGATACCG GGGGTCTAAC GAACGCCGTG AGGGAGTTTT ATTATATGCA AGAACTTGCT 6420 CTTTTCGAAA TCCACAGCAA ACTGTGCACC TACTACGATC AACTGCGCAT AGTCAACTTC 6480 GATCGTTCCG TAGCACCATG CAGCGAAGAT GCTCAGCTGT ACGTACGGAA GAACGGCTCA 6540 ACGATAGTGC AGGGTAAAGA GGTACGTTTG CACATTAAGG ATTTCCACGA TCACGATTTC 6600 CTGTTTGACG GAAAAATTTC TATTAACAAG CGGCGGCGAG GCGGAAATGT TTTATATCAC 6660 GACAACCTCG CGTTCTTGGC GAGTAATTTG TTCTTAGCCG GCTACCCCTT TTCAAGGAGC 6720 TTCGTCTTCA CGAATTCGTC GGTCGATATT CTCCTCTACG AAGCTCCACC CGGAGGTGGT 6780 AAGACGACGA CGCTGATTGA CTCGTTCTTG AAGGTCTTCA AGA AAGGTGA GGTTTCCACC 6840 ATGATCTTAA CCGCCAACAA AAGTTCGCAG GTTGAGATCC TAAAGAAAGT GGAGAAGGAA 6900 GTGTCTAACA TTGAATGCCA GAAACGTAAA GACAAAAGAT CTCCGAAAAA GAGCATTTAC 6960 ACCATCGACG CTTATTTAAT GCATCACCGT GGTTGTGATG CAGACGTTCT TTTCATCGAT 7020 GAGTGTTTCA TGGTTCATGC GGGTAGCGTA CTAGCTTGCA TTGAGTTCAC GAGGTGTCAT 7080 AAAGTAATGA TCTTCGGGGA TAGCCGGCAG ATTCACTACA TTGAAAGGAA CGAATTGGAC 7140 AAGTGTTTGT ATGGGGATCT CGACAGGTTC GTGGACCTGC AGTGTCGGGT TTATGGTAAT 7200 ATTTCGTACC GTTGTCCATG GGATGTGTGC GCTTGGTTAA GCACAGTGTA TGGCAACCTA 7260 ATCGCCACCG TGAAGGGTGA AAGCGAAGGT AAGAGCAGCA TGCGCATTAA CGAAATTAAT 7320 TCAGTCGACG ATTTAGTCCC CGACGTGGGT TCCACGTTTC TGTGTATGCT TCAGTCGGAG 7380 AAGTTGGAAA TCAGCAAGCA CTTTATTCGC AAGGGTTTGA CTAAACTTAA CGTTCTAACG 7440 GTGCATGAGG CGCAAGGTGA GACGTATGCG CGTGTGAACC TTGTGCGACT TAAGTTTCAG 7500 GAGGATGAAC CCTTTAAATC TATCAGGCAC ATAACCGTCG CTCTTTCTCG TCACACCGAC 7560 AGCTTAACTT ATAACGTCTT AGCTGCTCGT CGAGGTGACG CCACTTGCGA TGCCATCCAG 7620 AAGGCTGCGG AATTGGTGAA CAAGTTTCGC GTTTTT CCTA CATCTTTTGG TGGTAGTGTT 7680 ATCAATCTCA ACGTGAAGAA GGACGTGGAA GATAACAGTA GGTGCAAGGC TTCGTCGGCA 7740 CCATTGAGCG TAATCAACGA CTTTTTGAAC GAAGTTAATC CCGGTACTGC GGTGATTGAT 7800 TTTGGTGATT TGTCCGCGGA CTTCAGTACT GGGCCTTTTG AGTGCGGTGC CAGCGGTATT 7860 GTGGTGCGGG ACAACATCTC CTCCAGCAAC ATCACTGATC ACGATAAGCA GCGTGTTTAG_7920_(2) INFORMATION FOR SEQ ID NO: 3: (i) CHARACTERISTICS OF THE SEQUENCE: (A) Length: 2639 amino acids (B) Type: amino acids (C) Chain type: (D) Topology: linear (ii) TYPE OF MOLECULE: protein (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 3: Thr Leu Arg Glu Asn Pro lie Ser Val Ser Gly Val Asn Leu Gly Arg 1 5 10 15 Be Wing Wing Wing Gln Val He Tyr Phe Gly Ser Phe Thr Gln Pro Phe 20 25 30 Wing Leu Tyr Pro Arg Gln Glu Wing Wing Val Lys Thr Gln Leu Pro 35 40 45 Pro Val Ser Val Val Lys Val Glu Cys Val Ala Wing Glu Val Wing Pro 50 55 60 Asp Arg Gly Val Val Asp Lys Lys Pro Thr Ser Val Gly Val Pro Pro 65 70 75 80 Gln Arg Gly Val Leu Ser Phe Pro Thr Val Val Arg Asn Arg Gly Asp 85 90 95 Val He He Thr Gly Val Val His Glu Ala Leu Lys Lys He Lys Asp 100 105 110 Gly Leu Leu Arg Phe Arg Val Gly Gly Asp Met Arg Phe Ser Arg Phe 115 120 125 Phe Ser Ser Asn Tyr Gly Cys Arg Phe Val Wing Ser Val Arg Tbr Asn 130 135 140 Thr Thr Val Trp Leu Asn Cys Thr Lys Wing Ser Gly Glu Lys Phe Ser 145 150 155 160 Leu Ala Ala Ala Cys Thr Ala Asp Tyr Val Ala Met Leu Arg Tyr Val 165 170 175 Cys Gly Gly Lys Phe Pro Leu Val Leu Met Ser Arg Val He Tyr Pro 180 185 190 Asp Gly Arg Cys Tyr Leu Wing His Met Arg Tyr Leu Cys Wing Phe Tyr 195 200 205 Cys Arg Pro Phe Arg Glu Ser Asp Tyr Ala Leu Gly Met Trp Pro Thr 210 215 220 Val Wing Arg Leu Arg Wing Cys Val Glu Lys Asn Phe Gly Val Glu Ala 225 230 235 240 Cys Gly He Ala Leu Arg Gly Tyr Tyr Thr Ser Arg Asn Val Tyr His 245 250 255 Cys Asp Tyr Asp Ser Wing Tyr Val Lys Tyr Phe Arg Asn Leu Ser Gly 260 265 270 Arg He Gly Gly Gly Se r Phe Asp Pro Thr Ser Leu Thr Ser Val He 275 280 285 Thr Val Lys He Ser Gly Leu Pro Gly Gly Leu Pro Lys Asn He Wing 290 295 300 Phe Gly Wing Phe Leu Cys Asp He Arg Tyr Val Glu Pro Val Asp Ser 305 310 315 320 Gly Gly He Gln Ser Ser Val Lys Thr Lys Arg Glu Asp Wing His Arg 325 330 335 Thr Val Glu Glu Arg Wing Wing Gly Gly Ser Val Glu Gln Pro Arg Gln 340 345 350 Lys Arg He Asp Glu Lys Gly Cys Gly Arg Val Pro Ser Gly Gly Phe 355 360 365 Ser His Leu Leu Val Gly Asn Leu Asn Glu Val Arg Arg Lys Val Wing 370 375 380 Wing Gly Leu Leu Arg Phe Arg Val Gly Gly Asp Met Asp Phe His Arg 385 390 395 400 Ser Phe Ser Thr Gln Wing Gly His Arg Leu Leu Val Trp Arg Arg Ser 405 410 415 Ser Arg Ser Val Cys Leu Glu Leu Tyr Ser Pro Ser Lys Asn Phe Leu 420 425 430 Arg Tyr Asp Val Leu Pro Cys Ser Gly Asp Tyr Ala Wing Met Phe Ser 435 440 445 Phe Wing Wing Gly Gly Arg Phe Pro Leu Val Leu Met Thr Arg He Arg 450 455 460 Tyr Pro Asn Gly Phe Cys Tyr Leu Wing His Cys Arg Tyr Wing Cys Wing 465 470 475 480 Phe Leu Leu Arg Gly Phe Asp Pro Lys Arg Phe Asp He Gly Wing Phe 485 490 495 Pro Thr Wing Wing Lys Leu Arg Asn Arg Met Val Ser Glu Leu Gly 500 505 510 Arg Ser Leu Gly Leu Asn Leu Tyr Gly Wing Tyr Thr Ser Arg Gly Val 515 520 525 Phe His Cys Asp Tyr Asp Ala Lys Phe He Lys Asp Leu Arg Leu Met 530 535 540 Ser Wing Val He Wing Gly Lys Asp Gly Val Glu Val Val Pro Pro 545 550 555 560 Asp He Thr Pro Wing Met Lys Gln Lys Thr He Glu Wing Val Tyr Asp 565 570 575 Arg Leu Tyr Gly Gly Thr Asp Ser Leu Leu Lys Leu Ser He Glu Lys 580 585 590 Asp Leu He Asp Phe Lys Asn Asp Val Gln Ser Leu Lys Lys Asp Arg 595 600 605 Pro He Val Lys Val Pro Phe Tyr Met Ser Glu Ala Thr Gln Asn Ser 610 615 620 Leu Thr Arg Phe Tyr Pro Gln Phe Glu Leu Lys Phe Ser His Ser Ser 625 630 635 640 His Ser Asp His Pro Ala Ala Ala Ala Ser Arg Leu Leu Glu Asn Glu 645 650 655 Thr Leu Val Arg Leu Cys Gly Asn Ser Val Ser Asp He Gly Gly Cys 660 665 670 Pro Leu Phe His Leu His Ser Lys Thr Gln Arg Arg Val His Val Cys 675 680 685 Arg Pro Val Le u Asp Gly Lys Asp Wing Gln Arg Arg Val Val Arg Asp 690 695 700 Leu Gln Tyr Ser Asn Val Arg Leu Gly Asp Asp Asp Lys He Leu Glu 705 710 715 720 Gly Pro Arg Asn He Asp He Cys His Tyr Pro Leu Gly Ala Cys Asp 725 730 735 His Glu Being Met Wing Met Met Met Val Gln Val Tyr Asp Wing Ser Leu 740 745 750 Tyr Glu He Cys Gly Wing Met He Lys Lys Ser Arg He Thr Tyr 755 760 765 Leu Thr Met Val Thr Pro Gly Glu Phe Leu Asp Gly Arg Glu Cys Val 770 775 780 Tyr Met Glu Ser Leu Asp Cys Glu He Glu Val Asp Val His Wing Asp 785 790 795 800 Val Val Met Tyr Lys Phe Gly Ser Ser Cys Tyr Ser His Lys Leu Ser 805 810 815 He He Lys Asp He Met Thr Thr Pro Tyr Leu Thr Leu Gly Gly Phe 820 825 830 Leu Phe Ser Val Glu Met Tyr Glu Val Arg Met Gly Val Asn Tyr Phe 835 840 845 Lys He Thr Lys Ser Glu Val Ser Pro Ser He Ser Cys Thr Lys Leu 850 855 860 Leu Arg Tyr Arg Arg Wing Asn Ser Asp Val Val Lys Val Lys Leu Pro 865 870 875 880 Arg Phe Asp Lys Arg Arg Met Cys Leu Pro Gly Tyr Asp Thr He 885 890 895 Tyr Leu Asp Be Lys Phe Val Ser Arg Val Phe Asp Tyr Val Val Cys 900 905 910 Asn Cys Ser Wing Val Asn Ser Lys Thr Phe Glu Trp Val Trp Ser Phe 915 920 925 He Lys Ser Ser Lys Ser Arg Val He He Ser Gly Lys He He His 930 935 940 Lys Asp Val Asn Leu Asp Leu Lys Tyr Val Glu Ser Phe Wing Wing Val 945 950 955 960 Met Leu Wing Ser Gly Val Arg Ser Arg Leu Wing Ser Glu Tyr Leu Wing 965 970 975 Lys Asn Leu Ser His Phe Ser Gly Asp Cys Ser Phe He Glu Wing Thr 980 985 990 Ser Phe Val Leu Arg Glu Lys He Arg Asn Met Thr Leu Asn Phe Asn 995 1000 1005 Glu Arg Leu Leu Gln Leu Val Lys Arg Val Wing Phe Wing Thr Leu Asp 1010 1015 1020 Val Being Phe Leu Asp Leu Asp Being Thr Leu Glu Being He Thr Asp Phe 1025 1030 1035 1040 Wing Glu Cys Lys Val Wing He Glu Leu Asp Glu Leu Gly Cys Leu Arg 1045 1050 1055 Wing Glu Wing Glu Asn Glu Lys He Arg Asn Leu Wing Gly Asp Ser He 1060 1065 1070 Wing Wing Lys Leu Wing Ser Glu He Val Val Asp He Asp Ser Lys Pro 1075 1080 1085 Ser Pro Lys Gln Val Gly Asn Ser Ser Ser Glu Asn Wing Asp Lys Arg 1090 1095 1100 Glu Val Gln Arg Pro Gly Leu Arg Gly Gly Ser Arg Asn Gly Val Val 1105 1110 1115 1120 Gly Glu Phe Leu His Phe Val Val Asp Be Ala Leu Arg Leu Phe Lys 1125 1130 1135 Tyr Ala Thr Asp Gln Gln Arg He Lys Ser Tyr Val Arg Phe Leu Asp 1140 1145 1150 Ser Wing Val Ser Phe Leu Asp Tyr Asn Tyr Asp Asn Leu Ser Phe He 1155 1160 1165 Leu Arg Val Leu Ser Glu Gly Tyr Ser Cys Met Phe Wing Phe Leu Wing 1170 1175 1180 Asn Arg Gly Asp Leu Ser Ser Arg Val Arg Ser Wing Val Cys Wing Val 1185 1190 1195 1200 Lys Glu Val Wing Thr Ser Cys Wing Asn Wing Val Ser Lys Wing Lys 1205 1210 1215 Val Met He Thr Phe Wing Wing Wing Val Cys Wing Met Met Phe Asn Ser 1220 1225 1230 Cyr Gly Phe Ser Gly Asp Gly Arg Glu Tyr Lys Ser Tyr He His Arg 1235 1240 1245 Tyr Thr Gln Val Leu Phe Asp Thr He Phe Phe Glu Asp Ser Ser Tyr 1250 1255 1260 Leu Pro He Glu Val Leu Ser Ser Wing He Cys Gly Wing He Val Thr 1265 1270 1275 1280 Leu Phe Ser Ser Gly Ser Be He Be Leu Asn Wing Phe Leu Leu Gln 1285 1290 1295 He Thr Lys Gly Phe Ser Leu Glu Val Val Val Arg Asn Val Val Arg 1300 1305 1310 Val Thr His Gly Leu Ser Thr Thr Wing Thr Asp Gly Val He Arg Gly 1315 1320 1325 Val Phe Ser Gln He Val Ser His Leu Leu Val Gly Asn Thr Gly Asn 1330 1335 1340 Val Wing Tyr Gln Wing Wing Phe Wing Wing Gly Val Val Pro Leu Leu Val 1345 1350 1355 1360 Lys Lys Cys Val Ser Leu He Phe He Leu Arg Glu Asp Thr Tyr Ser 1365 1370 1375 Gly Phe lie Lys His Gly He Ser Glu Phe Ser Phe Leu Be Ser He 13¡80 1385 1390 Leu Lys Phe Leu Lys Gly Lys Leu Val Asp Glu Leu Lys Ser He He 1395 1400 1405 Gln Gly Val Phe Asp Ser Asn Lys His Val Phe Lys Glu Ala Thr Gln 1410 1415 1420 Glu Ala He Arg Thr Thr Val Met Gln Val Pro Val Wing Val Val Asp 1425 1430 1435 1440 Wing Leu Lys Ser Wing Wing Gly Lys He Tyr Asn Asn Phe Thr Ser Arg 1445 1450 1455 Arg Thr Phe Gly Lys Asp Glu Gly Being Ser Asp Gly Wing Cys Glu 1460 1465 1470 Glu Tyr Phe Ser Cys Asp Glu Gly Glu Gly Pro Gly Leu Lys Gly Gly 1475 1480 1485 Ser Ser Tyr Gly Phe Ser He Leu Wing Phe Phe Ser Arg He Met Trp 1490 1 495 1500 Gly Wing Arg Arg Leu He Val Lys Val Lys His Glu Cys Phe Gly Lys 1505 1510 1515 1520 Leu Phe Glu Phe Leu Ser Leu Lys Leu His Glu Phe Arg Thr Arg Val 1525 1530 1535 Phe Gly Lys Asn Arg Thr Asp Val Gly Val Tyr Asp Phe Leu Pro Thr 1540 1545 1550 Gly He Val Glu Thr Leu Ser Ser He Glu Glu Cys Asp Gln He Glu 1555 1560 1565 Glu Leu Leu Gly Asp Asp Leu Lys Gly Asp Lys Asp Wing Ser Leu Thr 1570 1575 1580 Asp Met Asn Tyr Phe Glu Phe Ser Glu Asp Phe Leu Wing Be He Glu 1585 1590 1595 1600 Glu Pro Pro Phe Wing Gly Leu Arg Gly Gly Ser Lys Asn He Wing He 1605 1610 1615 Leu Wing He Leu Glu Tyr Wing His Asn Leu Phe Arg He Val Ala Ser 1620 1625 1630 Lys Cys Ser Lys Arg Pro Leu Phe Leu Wing Phe Wing Glu Leu Ser Ser 1635 1640 1645 Wing Leu He Glu Lys Phe Lys Glu Val Phe Pro Arg Lys Ser Gln Leu 1650 1655 1660 Val Ala He Val Arg Glu Tyr Thr Gln Arg Phe Leu Arg Ser Arg Met 1665 1670 1675 1680 Arg Ala Leu Gly Leu Asn Asn Glu Phe Val Val Lys Ser Phe Wing Asp 1685 1690 1695 Leu Leu Pro Ala Leu Met Lys Arg Lys Val Ser Gly Ser Phe Leu Wing 1700 1705 1710 Ser Val Tyr Arg Pro Leu Arg Gly Phe Ser Tyr Met Cys Val Ser Wing 1715 1720 1725 Glu Arg Arg Glu Lys Phe Phe Wing Leu Val Cys Leu He Gly Leu Ser 1730 1735 1740 Leu Pro Phe Phe Val Arg He Val Gly Ala Lys Ala Cys Glu Glu Leu 1745 1750 1755 1760 Val Ser Be Wing Arg Arg Phe Tyr Glu Arg He Lys He Phe Leu Arg 1765 1770 1775 Gln Lys Tyr Val Ser Leu Ser Asn Phe Phe Cys His Leu Phe Ser Ser 1780 1785 1790 Asp Val Asp Asp Ser Ser Wing Ser Wing Gly Leu Lys Gly Wing Ser 1795 1800 1805 Arg Met Thr Leu Phe His Leu Leu Val Arg Leu Wing Ser Wing Leu Leu 1810 1815 1820 Ser Leu Gly Trp Glu Gly Leu Lys Leu Leu Leu Being His His Asn Leu 1825 1830 1835 1835 1840 Leu Phe Leu Cys Phe Ala Leu Val Asp Asp Val Asn Val Leu He Lys 1845 1850 1855 Val Leu Gly Gly Leu Ser Phe Phe Val Gln Pro He Phe Ser Leu Phe 1860 1865 1870 Ala Ala Met Leu Leu Gln Pro Asp Arg Phe Val Glu Tyr Ser Glu Lys 1875 1880 1885 Leu Val Thr Ala Phe Glu Phe Phe Leu Lys Cys Ser Pro Arg Ala Pr or 1890 1895 1900 Wing Leu Leu Lys Gly Phe Phe Glu Cys Val Wing Asn Ser Thr Val Ser 1905 1910 1915 1920 Lys Thr Val Arg Arg Leu Leu Arg Cys Phe Val Lys Met Leu Lys Leu 1925 1930 1935 Arg Lys Gly Arg Gly Leu Arg Wing Asp Gly Arg Gly Leu His Arg Gln 1940 1945 1950 Lys Wing Val Pro Val He Pro Being Asn Arg Val Val Thr Asp Gly Val 1955 1960 1965 Glu Arg Leu Ser Val Lys Met Gln Gly Val Glu Ala Leu Arg Thr Glu 1970 1975 1980 Leu Arg He Leu Glu Asp Leu Asp Be Wing Val He Glu Lys Leu Asn 1985 1990 1995 2000 Arg Arg Arg Asn Arg Asp Thr Asn Asp Asp Glu Phe Thr Arg Pro Wing 2005 2010 2015 His Glu Gln Met Gln Glu Val Thr Thr Phe Cys Be Lys Wing Asn Be 2020 2025 2030 Wing Gly Leu Wing Leu Glu Arg Wing Val Leu Val Glu Asp Wing He Lys 2035 2040 2045 Ser Glu Lys Leu Ser Lys Thr Val Asn Glu Met Val Arg Lys Gly Ser 2050 2055 2060 Thr Thr Ser Glu Glu Val Wing Val Wing Leu Being Asp Asp Glu Wing Val 2065 2070 2075 2080 Glu Glu Lie Ser Val Wing Asp Glu Arg Asp Asp Ser Pro Lys Thr Val 2085 2090 2095 Arg He Ser Glu Tyr Leu Asn Arg Leu Asn Being Ser Phe Glu Phe Pro 2100 2105 2110 Lys Pro He Val Val Asp Asp Asn Lys Asp Thr Gly Gly Leu Thr Asn 2115 2120 2125 Wing Val Arg Glu Phe Tyr Tyr Met Gln Glu Leu Ala Leu Phe Glu He 2130 2135 2140 His Ser Lys Leu Cys Thr Tyr Tyr Asp Gln Leu Arg He Val Asn Phe 2145 2150 2155 2160 Asp Arg Ser Val Wing Pro Cys Ser Glu Asp Wing Gln Leu Tyr Val Arg 2165 2170 2175 Lys Asn Gly Ser Thr He Val Gln Gly Lys Glu Val Arg Leu His He 2180 2185 2190 Lys Asp Phe His Asp His Asp Phe Leu Phe Asp Gly Lys He Ser He 2195 2200 2205 Asn Lys Arg Arg Gly Gly Asn Val Leu Tyr His Asp Asn Leu Ala 2210 2215 2220 Phe Leu Wing Being Asn Leu Phe Leu Wing Gly Tyr Pro Phe Being Arg Ser 2225 2230 2235 2240 Phe Val Phe Thr Asn Ser Val Val Lep Leu Tyr Glu Ala Pro 2245 2250 2255 Pro Gly Gly Gly Lys Thr Thr Thu Leu He Asp Be Phe Leu Lys Val 2260 2265 2270 Phe Lys Lys Gly Glu Val Ser Thr Met He Leu Thr Wing Asn Lys Ser 2275 2280 2285 Ser Gln Val Glu He Leu Lys Lys Val Glu Lys Glu Val Ser Asn He 2290 2295 2300 Glu Cys Gln Lys Arg Lys Asp Lys Arg Ser Pro Lys Lys Ser He Tyr 2305 2310 2315 2320 Thr He Asp Wing Tyr Leu Met His His Arg Gly Cys Asp Wing Asp Val 2325 2330 2335 Leu Phe He Asp Glu Cys Phe Met Val His Wing Gly Ser Val Leu Wing 2340 2345 2350 Cys He Glu Phe Thr Arg Cys His Lys Val Met He Phe Gly Asp Ser 2355 2360 2365 Arg Gln He His Tyr He Glu Arg Asn Glu Leu Asp Lys Cys Leu Tyr 2370 2375 2380 Gly Asp Leu Asp Arg Phe Val Asp Leu Gln Cys Arg Val Tyr Gly Asn 2385 2390 2395 2400 Ile Ser Tyr Arg Cys Pro Trp Asp Val Cys Wing Trp Leu Ser Thr Val 2405 2410 2415 Tyr Gly Asn Leu He Wing Thr Val Lys Gly Glu Ser Glu Gly Lys Ser 2420 2425 2430 Ser Met Arg He Asn Glu He Asn Ser Val Asp Asp Leu Val Pro Asp 2435 2440 2445 Val Gly Ser Thr Phe Leu Cys Met Leu Gln Ser Glu Lys Leu Glu He 2450 2455 2460 Ser Lys His Phe He Arg Lys Gly Leu Thr Lys Leu Asn Val Leu Thr 2465 2470 2475 2480 Val His Glu Wing Gln Gly Glu Thr Tyr Wing Arg Val Asn Leu Val Arg 2485 2490 2495 Leu L ys Phe Gln Glu Asp Glu Pro Phe Lys Ser He Arg His He Thr 2500 2505 2510 Val Ala Leu Ser Arg His Thr Asp Ser Leu Thr Tyr Asn Val Leu Wing 2515 2520 2525 Wing Arg Arg Gly Asp Wing Thr Cys Asp Wing He Gln Lys Wing Wing Glu 2530 2535 2540 Leu Val Asn Lys Phe Arg Val Phe Pro Thr Ser Phe Gly Gly Ser Val 2545 2550 2555 2560 He Asn Leu Asn Val Lys Lys Asp Val Glu Asp Asn Ser Arg Cys Lys 2565 2570 2575 Wing Ser Ser Ala Pro Leu Ser Val He Asn Asp Phe Leu Asn Glu Val 2580 2585 2590 Asn Pro Gly Thr Wing Val He Asp Phe Gly Asp Leu Ser Wing Asp Phe 2595 2600 2605 Ser Thr Gly Pro Phe Glu Cys Gly Wing Ser Gly He Val Val Arg Asp 2610 2615 2620 Asn He Being Ser Asn He Thr Asp His Asp Lys Gln Arg Val 2625 2630 2635TION FOR SEQ ID NO: 4: (i) CHARACTERISTICS OF THE SEQUENCE: (A) Length: 1380 base pairs (B) Type: nucleic acid (C) Chain type: simple (D) Topology: linear (ii) MOLECULE TYPE: cDNA (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 4: AGCGTAGTTC GGTCGCAGGC GATTCCGCGT AGAAAACCTT CTCTACAAGA AAATTTGTAT 60 TCGTTTGAAG CGCGGAATTA TAACTTCTCG ACTTGCGACC GTAACACATC TGCTTCAATG 120 TTCGGAGAGG CTATGGCGAT GAACTGTCTT CGTCGTTGCT TCGACCTAGA TGCCTTTTCG 180 TCCCTGCGTG ATGATGTGAT TAGTATCACA CGTTCAGGCA TCGAACAATG GCTGGAGAAA 240 CGTACTCCTA GTCAGATTAA AGCATTAATG AAGGATGTTG AATCGCCTTT GGAAATTGAC 300 GATGAAATTT GTCGTTTTAA GTTGATGGTG AAGCGTGACG CTAAGGTGAA GTTAGACTCT 360 TCTTGTTTAA CTAAACACAG CGCCGCTCAA AATATCATGT TTCATCGCAA GAGCATTAAT 420 GCTATCTTCT CTCCTATCTT TAATGAGGTG AAAAACCGAA TAATGTGCTG TCTTAAGCCT 480 AACATAAAGT TTTTTACGGA GATGACTAAC AGGGATTTTG CTTCTGTTGT CAGCAACATG 540 CTTGGTGACG ACGATGTGTA CCATATAGGT GAAGTTGATT TCTCAAAGTA CGACAAGTCT 600 CAAGATGCTT TCGTGAAGGC TTTTGAAGAA GTAATGTATA AGGAACTCGG TGTTGATGAA 660 GAGTTGCTGG CTATCTGGAT GTGCGGCGAG CGGTTATCGA TAGCTAACAC TCTCGATGGT 720 CAGTTGTCCT TCACGATCGA GAATCAAAGG AAGTCGGGAG CTTCGAACAC TTGGATTGGT 780 AACTCTCTCG TCACTTTGGG TATTTTAAGT CTTTACTACG ACGTTAGAAA TTTCGAGGCG 840 TTGTACATCT CGGGCGATGA TTCTTTAATT TTTTCTCGCA GCGAGATTTC GAATTATGCC 900 GACGACATAT GCACTGACAT GGGTTTTGAG ACAAAATTTA TGTCCCCAAG TGTCCCGTAC 960 TTTTGTTCTA AATTTGTTGT TATGTGTGGT CATAAGACGT TTTTTGTTCC CGACCCGTAC 1020 AAGCTTTTTG TCAAGTTGGG AGCAGTCAAA GAGGATGTTT CAATGGATTT CCTTTTCGAG 1080 ACTTTTACCT CCTTTAAAGA CTTAACCTCC GATTTTAACG ACGAGCGCTT AATTCAAAAG 1140 CTCGCTGAAC TTGTGGCTTT AAAATATGAG GTTCAAACCG GCAACACCAC CTTGGCGTTA 1200 AGTGTGATAC ATTGTTTGCG TTCGAATTTC CTCTCGTTTA GCAAGTTATA TCCTCGCGTG 1260 AAGGGATGGC AGGTTTTTTA CACGTCGGTT AAGAAAGCGC TTCTCAAGAG TGGGTGTTCT 1320 CTCTTCGACA GTTTCATGAC CCCTTTTGGT CAGGCTGTCA TGGTTTGGGA TGATGAGTAG_1380_(2) INFORMATION FOR SEQ ID NO: 5 : (i) SEQUENCE CHARACTERISTICS: (A) Length: 45 9 amino acids (B) Type: amino acids (C) Chain type: (D) Topology: linear (ii) TYPE OF MOLECULE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 5: Ser Val Val Arg Ser Gln Ala Pro Arg Arg Lys Pro Ser Leu Gln 1 5 10 15 Glu Asn Leu Tyr Ser Phe Glu Wing Arg Asn Tyr Asn Phe Ser Thr Cys 20 25 30 Asp Arg Asn Thr Ser Ala Ser Met Phe Gly Glu Wing Met Wing Met Asn 35 40 45 Cys Leu Arg Arg Cys Phe Asp Leu Asp Wing Phe Ser Ser Leu Arg Asp 50 55 60 Asp Val He Ser He Thr Arg Ser Gly He Glu Gln Trp Leu Glu Lys 65 70 75 80 Arg Thr Pro Ser Gln He Lys Wing Leu Met Lys Asp Val Glu Ser Pro 85 90 95 Leu Glu He Asp Asp Glu He Cys Arg Phe Lys Leu Met Val Lys Arg 100 105 110 Asp Ala Lys Val Lys Leu Asp Ser Ser Cys Leu Thr Lys His Ser Wing 115 120 125 Wing Gln Asn He Met Phe His Arg Lys Ser He Asn Wing He Phe Ser 130 135 140 Pro He Phe Asn Glu Val Lys Asn Arg He Met Cys Cys Leu Lys Pro 145 150 155 160 Asn He Lys Phe Phe Thr Glu Met Thr Asn Arg Asp Phe Wing Ser Val 165 170 175 Val Ser Asn Met Leu Gly Asp Asp Asp Val Tyr His He Gly Glu Val 180 185 190 Asp Phe Ser Lys Tyr Asp Lys Ser Gln Asp Wing Phe Val Lys Wing Phe 195 200 205 Glu Glu Val Met Tyr L ys Glu Leu Gly Val Asp Glu Glu Leu Leu Wing 210 215 220 He Trp Met Cys Gly Glu Arg Leu Ser He Wing Asn Thr Leu Asp Gly 225 230 235 240 Gln Leu Ser Phe Thr He Glu Asn Gln Arg Lys Ser Gly Wing Ser Asn 245 250 255 Thr Trp He Gly Asn Ser Leu Val Thr Leu Gly He Leu Ser Leu Tyr 260 265 270 Tyr Asp Val Arg Asn Phe Glu Wing Leu Tyr He Ser Gly Asp Asp Ser 275 280 285 Leu He Phe Ser Arg Ser Glu He Ser Asn Tyr Wing Asp Asp He Cys 290 295 300 Thr Asp Met Gly Phe Glu Thr Lys Phe Met Ser Ser Pro Ser Val Pro Tyr 305 310 315 320 Phe Cys Ser Lys Phe Val Val Met Cys Gly His Lys Thr Phe Phe Val 325 330 335 Pro Asp Pro Tyr Lys Leu Phe Val Lys Leu Gly Ala Val Lys Glu Asp 340 345 350 Val Ser Met Asp Phe Leu Phe Glu Thr Phe Thr Ser Phe Lys Asp Leu 355 360 365 Thr Ser Asp Phe Asn Asp Glu Arg Leu He Gln Lys Leu Wing Glu Leu 370 375 380 Val Wing Leu Lys Tyr Glu Val Gln Thr Gly Asn Thr Thr Leu Ala Leu 385 390 395 400 Ser Val He His Cys Leu Arg Ser Asn Phe Leu Ser Phe Ser Lys Leu 405 410 415 Tyr Pro Arg Val Lys Gly Trp Gln Val Phe Tyr Thr Ser Val Lys Lys 420 425 430 Wing Leu Leu Lys Ser Gly Cys Ser Leu Phe Asp Ser Phe Met Thr Pro 435 440 445 Phe Gly Gln Wing Val Met Val Trp Asp Asp Glu 450 455 (2) INFORMATION FOR SEQ ID NO: 6: (i) SEQUENCE CHARACTERISTICS: (A) Length: 171 base pairs (B) Type: nucleic acid (C) Chain type: simple (D) Topology: linear (ii) TYPE OF MOLECULE: cDNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 6:AGG TTTTGCAGTT TGAATGTTTG TTTCTGCTGA ATCGGT TTTTGCTGTG 60 ACTTTCATTT TCATTCTTCT GGTCTTCCGC GTGATTAAGT CTTTCA GAAGGGTCAC 120 GAAGCACCTG TTCCCGTTGT GGCGGG GGTTTTTCAA CCGTAGTGTA G 171 (2) INFORMATION FOR SEQ ID N0: 7: (i) CHARACTERISTICS OF SEQUENCE: (A) LENGTH: 56 amino acids (B) Type: amino acids (C) Chain type: (D) Topology: linear (ii) TYPE OF MOLECULE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID N0: 7: Met Asn Gln Val Leu Gln Phe Glu Cys Leu Phe Leu Leu Asn Leu Wing 1 5 10 15 Val Phe Wing Val Thr Phe He Phe He Leu Leu Val Phe Arg Val He 20 25 30 Lys Ser Phe Arg Gln Lys Gly His Glu Ala Pro Val Pro Val Val Arg 35 40 45 Gly Gly Gly Phe Ser Thr Val Val 50 55 (2) INFORMATION FOR SEQ ID NO: 8: (i) CHARACTERISTICS OF THE SEQUENCE : (A) Length: 1800 base pairs (B) Type: nucleic acid (C) Chain type: simple (D) Topology: linear (ii) TYPE OF MOLECULE: cDNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 8: ATGGTAGTTT TTTGGA CTTTGGCACC ACATTCTCTA CGGTGTGTGT GTACAAGGAT 60 GGACGAGTTT TTTCATTCAA GCAGAATAAT CGTACA TCCCCACTTA CCTCTATCTC 120 TTCTCCGATT CTAACCACAT GACTTTTGGT TACGAGGCCG AATCACTGAT GAGTAATCTG 180 AAAGTTAAAG GTTTTA TAGAGATTTA AAACGTTGGG TGGGTTGCGA TGTAAC 240 CCGCGT ACCTTGACCG TTTAAAACCT CATTAC TCCGCTTGGT TAAGAC 300 TCTGGCTTGA ACGAAACTGT TTCAATTGGA AACTGG GCACTGTTAA GTCTGAGGCT 3 60 CATCTGCCAG GGTTGATAGC TCTCTTTATT AAGGCTGTCA TTAGTTGCGC GGAGGGCGCG 420 TTTGCGTGCA CTTGCACCGG GGTTATTTGT TCAGTACCTG CCAATTATGA TAGCGTTCAA 480 AGGAATTTCA CTGATCAGTG TGTTTCACTC AGCGGTTATC AGTGCGTATA TATGATCAAT 540 GAACCTTCAG CGGCTGCGCT ATCTGCGTGT AATTTG GAAAGAAGTC CGCAAATTTG 600 GCTGTTTACG ATTTGG TGGGACCTTC GACGTGTCTA TCATTTCATA CCGCAACAAT 660 ACTTTTGTTG TGCGAGCTTC TGGAGGCGAT CTAAATCGTGGAAGGGA TGTTGA 720 GCGTTTCTCA CGCACCTCTT CTCTTTAACA TGGAAC CTGACCTCAC TTTGGATATC 780 ATCTGA AAGAATCTTT ATCAAAAACG GACGCAGAGA TAGTTTACAC TTTGAGAGGT 840 GTGGAA GAAAAGAAGA CGTTAGAGTA AACAAAAACA TTCTTACGTC GGTGATGCTC 900 CCCTACGTGA ACAGAACGCT TAAGATATTA GAGTCAACCT TAAAAA TGCTAAGAGT 960 ATGAATGAGA GTGCGCGAGT TAAGTGCGAT TTAGTGCTGA TAGGAGGATC TTCATATCTT 1020 CCTGGCCTGG CAGACGTACT AACGAAGCAT CAGAGCGTTG AATCTT AAGAGTT1080 GATCCG CTGCCGTGGC CGTTGC GCATTATATT CTTCATGCCT CTCAGGATCT 1140 GGGGGGTTGC TACTGA CTGTGCAGCT CACACTGCTATAGCGGA CAGAAGTTGT 1200 CATCAAATCA TTTGCGCTCC AGCGGGGGCA CCGATCCCCT TTTCAGGAAG CATGCCTTTG 1260 TACTTAGCCA GGGTCAACAA GAACAG CGTGAAGCCGTGTTTGA AGGGGAGTAC 1320 GTTAAGTGCC CTAAGAACAG AAAGATCTGT GGAGCAAATA TAAGATTTTT TGATATAGGA 1380 GTGACGGGTG ATACGC ACCCGTTACC TTCTATATGG ATTTCTCCAT TTCAAGCGTA 1440 GGAGCCGTTT CATGGT GAGAGGTCCT GAGGGTAAGC AAGTGTCACT CACTGGAACT 1500 CCAGCGTATA ACTTTC TGTGGCTCTC GGATCACGCA GTGTCCGAGA ATTGCATATT 1560 AGTTTAAATA ATAAAGTTTT TCTTTG CTTCTACATA GAAAGGCGGA CGAATA 1620 CTTTTCACTA AGGATGAAGC GATTAC GCCGATTCAA TTGATA GGATGTGCTA 1680 AAGGAATATA AAAGTTACGC GGCCAGTGCC TTACCACCAG ACGAGGATGT CGAATTACTC 1740 CTGGGAAAGT CTGTTCAAAA AGTTTTACGG GGAAGCAGAC TGGAAGAAAT ACCTCTCTAG_1800_(2) INFORMATION FOR SEQ ID N0: 9: (i) SEQUENCE CHARACTERISTICS: (A) Length: 599 amino acids (B) Type: amino acids (C) Chain type: (D) Topology: linear (ii) TYPE OF MOLECULE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 9: Met Val Val Phe Gly Leu Asp Phe Gly Thr Thr Phe Ser Thr Val Cys 1 5 10 15 Val Tyr Lys Asp Gly Arg Val Phe Ser Phe Lys Gln Asn Asn Be Wing 20 25 30 Tyr He Pro Thr Tyr Leu Tyr Leu Phe Ser Asp Ser Asn His Met Thr 40 45 Phe Gly Tyr Glu Wing Glu Ser Leu Met Ser Asn Leu Lys Val Lys Gly 50 55 60 Ser Phe Tyr Arg Asp Leu Lys Arg Trp Val Gly Cys Asp Ser Ser Asn 65 70 75 80 Leu Asp Wing Tyr Leu Asp Arg Leu Lys Pro His Tyr Ser Val Arg Leu 85 90 95 Val Lys He Gly Ser Gly Leu Asn Glu Thr Val Ser He Gly Asn Phe 100 105 110 Gly Gly Thr Val Lys Ser Glu Wing His Leu Pro Gly Leu He Wing Leu 115 120 125 Phe He Lys Ala Val He Be Cys Ala Glu Gly Ala Phe Ala Cys Thr 130 135 140 Cys Thr Gly Val He Cys Ser Val Pro Wing Asn Tyr Asp Ser Val Gln 145 150 155 160 Arg Asn Phe Thr Asp Gln Cys Val Ser Leu Ser Gly Tyr Gln Cys Val 165 170 175 Tyr Met He Asn Glu Pro Be Ala Ala Ala Leu Be Ala Cys Asn Ser 180 185 190 He Gly Lys Lys Ser Ala Asn Leu Ala Val Tyr Asp Phe Gly Gly Gly 195 200 205 Thr Phe Asp Val Ser He He Ser Tyr Arg Asn Asn Thr Phe Val Val 210 215 220 Arg Wing Ser Gly Gly Asp Leu Asn Leu Gly Gly Arg Asp Val Asp Arg 225 230 235 240 Wing Phe Leu Thr His Leu Phe Ser Leu Thr Ser Leu Glu Pro Asp Leu 245 250 255 Thr Leu Asp He Being Asn Leu Lys Glu Ser Leu Ser Lys Thr Asp Wing 260 265 270 Glu He Val Tyr Thr Leu Arg Gly Val Asp Gly Arg Lys Glu Asp Val 275 280 285 Arg Val Asn Lys Asn He Leu Thr Ser Val Met Leu Pro Tyr Val Asn 290 295 300 Arg Thr Leu Lys He Leu Glu Ser Thr Leu Lys Ser Tyr Ala Lys Ser 305 310 315 320 Met Asn Glu Ser Ala Arg Val Lys Cys Asp Leu Val Leu He Gly Gly '325 330 335 Ser Ser Tyr Leu Pro Gly Leu Wing Asp Val Leu Thr Lys His Gln Ser 340 345 350 Val Asp Arg He Leu Arg Val Ser Asp Pro Arg Wing Wing Val Wing Val 355 360 365 Gly Cys Ala Leu Tyr Ser Ser Cys Leu Ser Gly Ser Gly Gly Leu Leu 370 375 380 Leu He Asp Cys Ala Ala His Thr Val Wing He Wing Asp Arg Ser Cys 385 390 395 400 His Gln He He Cys Ala Pro Wing Ala Gly Wing Pro Pro Pro Phe Ser Gly 405 410 415 Ser Met Pro Leu Tyr Leu Wing Arg Val Asn Lys Asn Ser Gln Arg Glu 420 425 430 Val Wing Val Phe Glu Gly Glu Tyr Val Lys Cys Pro Lys Asn Arg Lys 435 440 445 lie Cys Gly Wing Asn He Arg Phe Phe Asp He Gly Val Thr Gly Asp 450 455 460 Ser Tyr Wing Pro Val Thr Phe Tyr Met Asp Phe Ser Be Ser Ser Val 465 470 475 480 Gly Wing Val Ser Phe Val Val Arg Gly Pro Glu Gly Lys Gln Val Ser 485 490 495 Leu Thr Gly Thr Pro Ala Tyr Asn Phe Ser Ser Val Ala Leu Gly Ser 500 505 510 Arg Ser Val Arg Glu Leu His He Ser Leu Asn Asn Lys Val Phe Leu 515 520 525 Gly Leu Leu Leu His Arg Lys Wing Asp Arg Arg He Leu Phe Thr L ys 530 535 540 Asp Glu Wing He Arg Tyr Wing Asp Ser He Asp He Wing Asp Val Leu 545 550 555 560 Lys Glu Tyr Lys Ser Tyr Ala Wing Wing Wing Leu Pro Pro Asp Glu Asp 565 570 575 Val Glu Leu Leu Le Gly Lys Ser Val Gln Lys Val Leu Arg Gly Ser 580 585 590 Arg Leu Glu Glu He Pro Leu 595 (2) INFORMATION FOR SEQ ID NO: 10: (i) CHARACTERISTICS OF THE SEQUENCE: (A) Length: 1656 base pairs ( B) Type: nucleic acid (C) Chain type: simple (D) Topology: linear (ii) TYPE OF MOLECULE: cDNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 10: ATGTCGAATT ACTCCTGGGA AAGTCTGTTC AAAAAGTTTT ACGGGGAAGC AGACTGGAAG 60 AAATACCTCT CTAGGAGCAT AGCAGCACAC TCAAGTGAAA TTAAAACTCT ACCAGACATT 120 CGATTGTACG GCGGTAGGGT TGTAAAGAAG TCCGAATTCG AATCAGCACT TCCTAATTCT 180 TTTGAACAGG AATTAGGACT GTTCATACTG AGCGAACGGG AAGTGGGATG GAGCAAATTA 240 TGCGGAATAA CGGTGGAAGA AGCAGCATAC GATCTTACGA ATCCCAAGGC TTATAAATTC 300 ACTGCCGAGA CATGTAGCCC GGATGTAAAA GGTGAAGGAC AAAAATACTC TATGGAAGAC 360 GTGATGAATT TCATGCGTTT ATCAAATCTG GATGTTAACG ACAAGATGCT GACGGAACAG 420 TGTTGGTCGC TGTCCAATTC ATGCGGTGAA TTGATCAACC CAGACGACAA AGGGCGATTC 480 GTGGCTCTCA CCTTTAAGGA CAGAGACACA GCTGATGACA CGGGTGCCGC CAACGTGGAA 540 TGTCGCGTGG GCGACTATCT AGTTTACGCT ATGTCCCTGT TTGAGCAGAG GACCCAAAAA 600 TCGCAGTCTG GCAACATCTC TCTGTACGAA AAGTACTGTG AATACATCAG GACCTACTTA 660 GGGAGTACAG ACCTGTTCTT CACAGCGCCG GACAGGATTC CGTTACTTAC GGGCATCCTA 720 TACGATTTTT GTAAGGAATA CAACGTTTTC TACTCGTCAT ATAAGAGAAA CGTCGATAAT 780 TTCAGATTCT TCTTGGCGAA TTATATGCCT TTGATATCTG ACGTCTTTGT CTTCCAGTGG 840 GTAAAAC CCG CGCCGGATGT TCGGCTGCTT TTTGAGTTAA GTGCAGCGGA ACTAACGCTG 900 GAGGTTCCCA CACTGAGTTT GATAGATTCT CAAGTTGTGG TAGGTCATAT CTTAAGATAC 960 GTAGAATCCT ACACATCAGA TCCAGCCATC GACGCGTTAG AAGACAAACT GGAAGCGATA 1020 CTGAAAAGTA GCAATCCCCG TCTATCGACA GCGCAACTAT GGGTTGGTTT CTTTTGTTAC 1080 TATGGTGAGT TTCGTACGGC TCAAAGTAGA GTAGTGCAAA GACCAGGCGT ATACAAAACA 1140 CCTGACTCAG TGGGTGGATT TGAAATAAAC ATGAAAGATG TTGAGAAATT CTTCGATAAA 1200 CTTCAGAGAG AATTGCCTAA TGTATCTTTG CGGCGTCAGT TTAACGGAGC TAGAGCGCAT 1260 GAGGCTTTCA AAATATTTAA AAACGGAAAT ATAAGTTTCA GACCTATATC GCGTTTAAAC 1320 GTGCCTAGAG AGTTCTGGTA TCTGAACATA GACTACTTCA GGCACGCGAA TAGGTCCGGG 1380 TTAACCGAAG AAGAAATACT CATCCTAAAC AACATAAGCG TTGATGTTAG GAAGTTATGC 1440 GCTGAGAGAG CGTGCAATAC CCTACCTAGC GCGAAGCGCT TTAGTAAAAA TCATAAGAGT 1500 AATATACAAT CATCACGCCA AGAGCGGAGG ATTAAAGACC CATTGGTAGT CCTGAAAGAC 1560 ACTTTATATG AGTTCCAACA CAAGCGTGCC GGTTGGGGGT CTCGAAGCAC TCGAGACCTC 1620 GGGAGTCGTG CTGACCACGC GAAAGGAAGC GGTTGA 1656 (2) INFORMATION FOR SEQ ID NO: 11: (i) SEQUENCE CHARACTERISTICS: (A) Length: 551 amino acids (B) Type: amino acids (C) Chain type: (D) Topology: linear (ii) TYPE OF MOLECULE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: l 1: Met Ser Asn Tyr Ser Trp Glu Being Leu Phe Lys Lys Phe Tyr Gly Glu 1 5 10 15 Wing Asp Trp Lys Lys Tyr Leu Ser Arg Ser Wing Wing His Ser Being 20 25 30 Glu He Lys Thr Leu Pro Asp He Arg Leu Tyr Gly Gly Arg Val Val 35 40 45 Lys Lys Ser Glu Phe Glu Be Ala Leu Pro Asn Ser Phe Glu Gln Glu 50 55 60 Leu Gly Leu Phe He Leu Ser Glu Arg Glu Val Gly Trp Ser Lys Leu 65 70 75 80 Cys Gly He Thr Val Glu Glu Ala Ala Tyr Asp Leu Thr Asn Pro Lys 85 90 95 Wing Tyr Lys Phe Thr Wing Glu Thr Cys Ser Pro Asp Val Lys Gly Glu 100 105 110 Gly Gln Lys Tyr Ser Met Glu Asp Val Met Asn Phe Met Arg Leu Ser 115 120 125 Asn Leu Asp Val Asn Asp Lys Met Leu Thr Glu Gln Cys Trp Ser Leu 130 135 140 Ser Asn Ser Cys Gly Glu Leu He Asn Pro Asp Asp Lys Gly Arg Phe 145 150 155 160 Val Ala Leu Thr Phe Lys Asp Arg Asp Thr Ala Asp Asp Thr Gly Wing 165 170 175 Wing Asn Val Glu Cys Arg Val Gly Asp Tyr Leu Val Tyr Wing Met Ser 180 185 190 Leu Phe Glu Gln Arg Thr Gln Lys Ser Gln Ser Gly Asn He Ser Leu 195 200 205 Tyr Glu Lys Tyr Cys Glu Tyr He Arg Thr Tyr Leu Gly Ser Thr Asp 210 215 220 Leu Phe Phe Thr Ala Pro Asp Arg He Pro Leu Leu Thr Gly He Leu 225 230 235 240 Tyr Asp Phe Cys Lys Glu Tyr Asn Val Phe Tyr Ser Ser Tyr Lys Arg 245 250 255 Asn Val Asp Asn Phe Arg Phe Phe Leu Wing Asn Tyr Met Pro Leu He 260 265 270 Ser Asp Val Phe Val Phe Gln Trp Val Lys Pro Pro Wing Asp Val Arg 275 280 285 Leu Leu Phe Glu Leu Ser Wing Wing Glu Leu Thr Leu Glu Val Pro Thr 290 295 300 Leu Ser Leu He Asp Ser Gln Val Val Val Gly His He Leu Arg Tyr 305 310 315 320 Val Glu Ser Tyr Thr Ser Asp Pro Wing He Asp Wing Leu Glu Asp Lys 325 330 335 Leu Glu Wing He Leu Lys Ser Being Asn Pro Arg Leu Ser Thr Wing Gln 340 345 350 Leu Trp Val Gly Phe Phe Cys Tyr Tyr Gly Glu Phe Arg Thr Ala Gln 355 360 365 Ser Arg Val Val Gln Arg Pro Gly Val Tyr Lys Thr Pro Asp Ser Val 370 375 380 Gly Gly Ghe He Asn Met Lys Asp Val Glu Lys Phe Phe Asp Lys 385 390 395 400 Leu Gln Arg Glu Leu Pro Asn Val Ser Leu Arg Arg Gln Phe Asn Gly 405 410 415 Wing Arg Wing His Glu Wing Phe Lys He Phe Lys Asn Gly Asn He Ser 420 425 430 Phe Arg Pro He Ser Arg Leu Asn Val Pro Arg Glu Phe Trp T yr Leu 435 440 445 Asn He Asp Tyr Phe Arg His Wing Asn Arg Ser Gly Leu Thr Glu Glu 450 455 460 Glu He Leu He Leu Asn Asn He Ser Val Asp Val Arg Lys Leu Cys 465 470 475 480 Wing Glu Arg Wing Cys Asn Thr Leu Pro Ser Ala Lys Arg Phe Ser Lys 485 490 495 Asn His Lys Ser Asn He Gln Ser Ser Arg Gln Glu Arg Arg He Lys 500 505 510 Asp Pro Leu Val Val Leu Lys Asp Thr Leu Tyr Glu Phe Gln His Lys 515 520 525 Arg Wing Gly Trp Gly Ser Arg Ser Thr Arg Asp Leu Gly Ser Arg Wing 530 535 540 Asp His Wing Lys Gly Ser Gly 545 550 (2) INFORMATION FOR SEQ ID NO: 12: (i) SEQUENCE CHARACTERISTICS: (A) Length: 672 base pairs (B) Type: nucleic acid (C) Chain type: simple (D) Topology: linear (ii) TYPE OF MOLECULE: cDNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 12 : ATGAGTTCCA ACACAAGCGT GCCGGTTGGG GGTCTCGAAG CACTCGAGAC CTCGGGAGTC 60 GTGCTGACCA CGCGAAAGGA AGCGGTTGAT AAGTTTTTTA ATGAACTAAA AAACGAAAAT 120 TACTCATCAG TTGACAGCAG CCGATTAAGC GATTCGGAAG TAAAAGAAGT GTTAGAGAAA 180 AGTAAAGAAA GTTTCAAAAG CGAACTGGCC TCCACTGACG AGCACTTCGT CTACCACATT 240 ATATTTTTCT TAATCCGATG TGCTAAGATA TCGACAAGTG AAAAGGTGAA GTACGTTGGT 300 AGTCATACGT ACGTGGTCGA CGGAAAAACG TACACCGTTC TTGACGCTTG GGTATTCAAC 360 ATGATGAAAA GTCTCACGAA GAAGTACAAA CGAGTGAATG GTCTGCGTGC GTTCTGTTGC 420 GCGTGCGAAG ATCTATATCT AACCGTCGCA CCAATAATGT CAGAACGCTT TAAGACTAAA 480 GCCGTAGGGA TGAAAGGTTT GCCTGTTGGA AA GGAATACT TAGGCGCCGA CTTTCTTTCG 540 GGAACTAGCA AACTGATGAG CGATCACGAC AGGGCGGTCT CCATCGTTGC AGCGAAAAAC 600 GCTGTCGATC GTAGCGCTTT CACGGGTGGG GAGAGAAAGA TAGTTAGTTT GTATGATCTA 660 GGGAGGTACT AA 672 (2) INFORMATION FOR SEQ ID NO: 13: (i) CHARACTERISTICS OF SEQUENCE: (A) LENGTH: 223 amino acids (B) Type: amino acids (C) Chain type: (D) Topology: linear (ii) TYPE OF MOLECULE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 13: Met Ser Ser Asn Thr Ser Val Pro Val Gly Gly Leu Glu Ala Leu Glu 1 5 10 15 Thr Ser Gly Val Val Leu Thr Thr Arg Lys Glu Wing Val Asp Lys Phe 20 25 30 Phe Asn Glu Leu Lys Asn Glu Asn Tyr Ser Ser Val Asp Ser Ser Arg 35 40 45 Leu Ser Asp Ser Glu Val Lys Glu Val Leu Glu Lys Ser Lys Glu Ser 50 55 60 Phe Lys Ser Glu Leu Wing Ser Thr Asp Glu His Phe Val Tyr His He 65 70 75 80 He Phe Phe Leu He Arg Cys Ala Lys He Ser Thr Ser Glu Lys Val 85 90 95 Lys Tyr Val Gly Ser His Thr Tyr Val Val Asp Gly Lys Thr Tyr Thr 100 105 110 Val Leu Asp Ala Trp Val Phe Asn Met Met Lys Ser Leu Thr Lys Lys 115 120 125 Tyr Lys Arg Val Asn Gly Leu Arg Wing Phe Cys Cys Wing Cys Glu Asp 130 135 140 Leu Tyr Leu Thr Val Wing Pro He Met Ser Glu Arg Phe Lys Thr Lys 145 150 155 160 Wing Val Gly Met Lys Gly Leu Pro Val Gly Lys Glu Tyr Leu Gly Wing 165 170 175 Asp Phe Leu Ser Gly Thr Ser Lys Leu Met Ser Asp His Asp Arg Wing 180 185 190 Val Ser He Val Wing Wing Lys Asn Wing Val Asp Arg Ser Wing Phe Thr 195 200 205 Gly Gly Glu Arg Lys He Val Ser Leu Tyr Asp Leu Gly Arg Tyr 210 215 220 (2) INFORMATION FOR SEQ ID NO: 14: (i) SEQUENCE CHARACTERISTICS: (A) Longitude: 597 base pairs (B) Type: nucleic acid (C) Chain type: simple (D) Topology: linear (ii) TYPE OF MOLECULE: cDNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 14: ATGGAGTTGA TGTCCGACAG CAACCTTAGC AACCTGGTGA TAACCGACGC CTCTAGTCTA 60 AATGGTGTCG ACAAGAAGCT TTTATCTGCT GAAGTTGAAA AAATGTTGGT GCAGAAAGGG 120 GCTCCTAACG AGGGTATAGA AGTGGTGTTC GGTCTACTCC TTTACGCACT CGCGGCAAGA 180 ACCACGTCTC CTAAGGTTCA GCGCGCAGAT TCAGACGTTA TATTTTCAAA TAGTTTCGGA 240 GAGAGGAATG TGGTAGTAAC AGAGGGTGAC CTTAAGAAGG TACTCGACGG GTGTGCGCCT 300 CTCACTAGGT TCACTAATAA ACTTAGAACG TTCGGTCGTA CTTTCACTGA GGCTTACGTT 360 GACTTTTGTA TCGCGTATAA GCACAAATTA CCCCAACTCA ACGCCGCGGC GGAATTGGGG 420 ATTCCAGCTG AAGATTCGTA CTTAGCTGCA GATTTTCTGG GTACTTGCCC GAAGCTCTCT 480 GAATTACAGC AAAGTAGGAA GATGTTCGCG AGTATGTACG CTCTAAAAAC TGAAGGTGGA 540 GTGGTAAATA CACCAGTGAG CAATCTGCGT CAGCTAGGTA GAAGGGAAGT TATGTAA 597 (2) INFORMATION FOR SEQ ID NO: 15: (i) SEQUENCE CHARACTERISTICS: (A) Length: 198 amino acids (B) Type: amino acids (C) Chain type: (D) Topology: linear (ii) TYPE OF MOLECULE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 15: Met Glu Leu Met Ser Asp Ser Asn Leu Ser Asn Leu Val He Thr Asp 1 5 10 15 Wing Being Ser Leu Asn Gly Val Asp Lys Lys Leu Leu Ser Wing Glu Val 20 25 30 Glu Lys Met Leu Val Gln Lys Gly Wing Pro Asn Glu Gly He Glu Val 40 45 Val Phe Gly Leu Leu Leu Tyr Wing Leu Wing Wing Arg Thr Thr Ser Pro 50 55 60 Lys Val Gln Arg Wing Asp Ser Asp Val He Phe Ser Asn Ser Phe Gly 65 70 75 80 Glu Arg Asn Val Val Val Thr Glu Gly Asp Leu Lys Lys Val Leu Asp 85 90 95 Gly Cys Wing Pro Leu Thr Arg Phe Thr Asn Lys Leu Arg Thr Phe Gly 100 105 110 Arg Thr Phe Thr Glu Wing Tyr Val Asp Phe Cys He Wing Tyr Lys His 115 120 125 Lys Leu Pro Gln Leu Asn Wing Wing Wing Glu Leu Gly He Pro Wing Glu 130 135 140 Asp Ser Tyr Leu Wing Wing Asp Phe Leu Gly Thr Cys Pro Lys Leu Ser 145 150 155 160 Glu Leu Gln Gln Ser Arg Lys Met Phe Ala Ser Met Tyr Ala Leu Lys 165 170 175 Thr Glu Gly Gly Val Val Asn Thr Pro Val Ser Asn Leu Arg Gln Leu 180 185 190 Gly Arg Arg Glu Val Met 195 (2) INFORMATION FOR SEQ ID NO: 16: (i) CHARACTERISTICS OF SEQUENCE: (A) Length: 486 base pairs (B) Type: nucleic acid (C) Chain type: simple (D) Topology: linear (ii) TYPE OF MOLECULE: cDNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO : 16: AT GGAAGATT ACGAAGAAAA ATCCGAATCG CTCATACTGC TACGCACGAA TCTGAACACT 60 ATGCTTTTAG TGGTCAAGTC CGATGCTAGT GTAGAGCTGC CTAAACTACT AATTTGCGGT 120 TACTTACGAG TGTCAGGACG TGGGGAGGTG ACGTGTTGCA ACCGTGAGGA ATTAACAAGA 180 GATTTTGAGG GCAATCATCA TACGGTGATC CGTTCTAGAA TCATACAATA TGACAGCGAG 240 TCTGCTTTTG AGGAATTCAA CAACTCTGAT TGCGTAGTGA AGTTTTTCCT AGAGACTGGT 300 AGTGTCTTTT GGTTTTTCCT TCGAAGTGAA ACCAAAGGTA GAGCGGTGCG ACATTTGCGC 360 ACCTTCTTCG AAGCTAACAA TTTCTTCTTT GGATCGCATT GCGGTACCAT GGAGTATTGT 420 TTGAAGCAGG TACTAACTGA AACTGAATCT ATAATCGATT CTTTTTGGGA AGAAAGAAAT 480 CGTTAA 486 (2) INFORMATION FOR SEQ ID NO: 17: (i) SEQUENCE CHARACTERISTICS: (A) Length: 161 amino acids (B) Type: amino acids (C) Chain type: (D) Topology: linear (ii) TYPE OF MOLECULE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 17: Met Glu Asp Tyr Glu Glu Lys Ser Glu Ser Leu He Leu Leu Arg Thr 1 5 10 15 Asn Leu Asn Thr Met Leu Leu Val Val Lys Ser Asp Ala Ser Val Glu 20 25 30 Leu Pro Lys Le u Leu He Cys Gly Tyr Leu Arg Val Ser Gly Arg Gly 35 40 45 Glu Val Thr Cys Cys Asn Arg Glu Glu Leu Thr Arg Asp Phe Glu Gly 50 55 60 Asn His His Thr Val He Arg Ser Arg He He Gln Tyr Asp Ser Glu 65 70 75 80 Ser Wing Phe Glu Glu Phe Asn Asn Ser Asp Cys Val Val Lys Phe Phe 85 90 95 Leu Glu Thr Gly Ser Val Phe Trp Phe Phe Leu Arg Ser Glu Thr Lys 100 105 110 Gly Arg Ala Val Arg His Leu Arg Thr Phe Phe Glu Wing Asn Asn Phe 115 120 125 Phe Phe Gly Ser His Cys Gly Thr Met Glu Tyr Cys Leu Lys Gln Val 130 135 140 Leu Thr Glu Thr Glu Ser He He Asp Ser Phe Cys Glu Glu Arg Asn 145 150 155 160 Arg (2) INFORMATION FOR SEQ ID NO: 18: (i) SEQUENCE CHARACTERISTICS: (A) Length: 618 base pairs (B) Type: nucleic acid (C) Chain type: simple (D) Topology: linear ( ii) MOLECULE TYPE: cDNA (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 18: ATGAGGGTTA TAGTGTCTCC TTATGAAGCT GAAGACATTC TGAAAAGATC GACTGACATG 60 TTACGAAACA TAGACAGTGG GGTCTTGAGC ACTAAAGAAT GTATCAAGGC ATTCTCGACG 120 ATAACGCGAG ACCTACATTG TGCGAAGGCT TCCTACCAGT GGGGTGTTGA CACTGGGTTA 180 TATCAGCGTA ATTGCGCTGA AAAACGTTTA ATTGACACGG TGGAGTCAAA CATACGGTTG 240 GCTCAACCTC TCGTGCGTGA AAAAGTGGCG GTTCATTTTT GTAAGGATGA ACCAAAAGAG 300 CTAGTAGCAT TCATCACGCG AAAGTACGTG GAACTCACGG GCGTGGGAGT GAGAGAAGCG 360 GTGAAGAGGG AAATGCGCTC TCTTACCAAA ACAGTTTTAA ATAAAATGTC TTTGGAAATG 420 GCGTTTTACA TGTCACCACG AGCGTGGAAA AACGCTGAAT GGTTAGAACT AAAATTTTCA 480 CCTGTGAAAA TCTTTAGAGA TCTGCTATTA GACGTGGAAA CGCTCAACGA ATTGTGCGCC 540 GAAGATGATG TTCACGTCGA CAAAGTAAAT GAGAATGGGG ACGAAAATCA CGACCTCGAA 600 CTCCAAGACG AATGTTAA 6 18 (2) INFORMATION FOR SEQ ID NO: 19: (i) SEQUENCE CHARACTERISTICS: (A) Length: 205 amino acids (B) Type: amino acids (C) Chain type: (D) Topology: linear (ii) TYPE OF MOLECULE: protein (xi) DESCRIPTION OF SEQUENCE: SEQ ID NO: 19: Met Arg Val He Val Ser Pro Tyr Glu Ala Glu Asp He Leu Lys Arg 1 5 10 15 Ser Thr Asp Met Leu Arg Asn He Asp Ser Gly Val Leu Being Thr Lys 20 25 30 Glu Cys He Lys Ala Phe Being Thr He Thr Arg Asp Leu His Cys Wing 35 40 45 Lys Wing Being Tyr Gln Trp Gly Val Asp Thr Gly Leu Tyr Gln Arg Asn 50 55 60 Cys Wing Glu Lys Arg Leu He Asp Thr Val Glu Ser Asn He Arg Leu 65 70 75 80 Wing Gln Pro Leu Val Arg Glu Lys Val Wing Val His Phe Cys Lys Asp 85 90 95 Glu Pro Lys Glu Leu Val Wing Phe He Thr Arg Lys Tyr Val Glu Leu 100 105 110 Thr Gly Val Gly Val Arg Glu Ala Val Lys Arg Glu Met Arg Ser Leu 115 120 125 Thr Lys Thr Val Leu Asn Lys Met Ser Leu Glu Met Wing Phe Tyr Met 130 135 140 Ser Pro Arg Wing Trp Lys Asn Wing Glu Trp Leu Glu Leu Lys Phe Ser 145 150 155 160 Pro Val Lys He Phe Arg Asp Leu Leu Leu Asp Val Glu Thr Leu Asn 165 170 175 Glu Leu Cys Wing Glu Asp Asp Val His Val Asp Lys Val Asn Glu Asn 180 185 190 Gly Asp Glu Asn His Asp Leu Glu Leu Gln Asp Glu Cys 195 200 205 (2) INFORMATION FOR SEQ ID NO: 20: (i) CHARACTERISTICS OF THE SEQUENCE: (A) Length: 21 base pairs (B) Type: nucleic acid (C) Chain type: simple (D) Topology : linear (ii) TYPE OF MOLECULE: cDNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 20: TGCTGGAGCT TGAGGTTCTG C 21 (2) INFORMATION FOR SEQ ID NO: 21: (i) SEQUENCE CHARACTERISTICS: (A) Length: 31 base pairs (B) Type: nucleic acid (C) Chain type: simple (D) Topology: linear (ii) TYPE OF MOLECULE: cDNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 21: CGGAATTCAC CATGGAGTTG ATGTCCGACA G 31 (2) INFORMATION FOR SEQ ID NO: 22: (i) SEQUENCE CHARACTERISTICS: (A) Length: 33 base pairs (B) Type: nucleic acid (C) Chain type: simple (D) Topology: linear (ii) TYPE MOLECULE: cDNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 22: AGCGGATCCA TGGCAGATTC GTGCGTAGCA GTA 33 (2) INFORMATION FOR SEQ ID NO: 23: (i) SEQUENCE CHARACTERISTICS: (A) Length: 216 base pairs (B) Type: nucleic acid (C) Chain type: simple (D) Topology: linear (ii) TYPE OF MOLECULE: cDNA (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 23: ACATTGGTTA AGTTTAACGA AAATGATTAG TAAATAATAA ATCGAACGTG GGTGTATCTA 60 CCTGACGTAT CAACTTAAGC TGTTACTGAG TAATTAAACC AACAAGTGTT GGTGTAATGT 120 GTATGTTGAT GTAGAGAAAA ATCCGTTTGT AGAACGGTGT TTTTCTCTTC TTTATTTTTA 180 AAAAAAAAAT AAAAAAAAAA AAAAAAAAAGC GGCCGC 216

Claims (78)

1. KEIVI DICATIONS 1. An isolated protein or polypeptide corresponding to a protein or polypeptide of a virus of the vine leaf roll (type 2). 2. An isolated protein or polypeptide according to claim 1, wherein the protein or polypeptide is selected from a group consisting of a polyprotein, an RNA-dependent RNA polymerase, a heat shock protein 70, a heat shock protein 90 , a diverged coating protein, and a coating protein. 3. An isolated protein or polypeptide according to claim 2, wherein the protein or polypeptide is a polyprotein. 4. An isolated protein or polypeptide according to claim 3, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 3. An isolated protein or polypeptide according to claim 2, wherein the protein or polypeptide is an RNA-dependent RNA polymerase having a molecular weight of about 50 to about 54 kDa. 6. An isolated protein or polypeptide according to claim 5, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 5. An isolated protein or polypeptide according to claim 2, wherein the protein or polypeptide is a heat shock protein 70 having a molecular weight of about 63 to about 67 kDa. 8. An isolated protein or polypeptide according to claim 7, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 9. An isolated protein or polypeptide according to claim 2, wherein the protein or polypeptide is a heat shock protein 90 having a molecular weight of about 61 to about 65 kDa. 10. An isolated protein or polypeptide according to claim 9, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 11. An isolated protein or polypeptide according to claim 2, wherein the protein or polypeptide is a coat protein having a molecular weight of from about 20 to about 24 kDa. 12. An isolated protein or polypeptide according to claim 11, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 15. An isolated protein or polypeptide according to claim 2, wherein the protein or polypeptide is a diverged coat protein having a molecular weight of from about 23 to about 27 kDa. 14. An isolated protein or polypeptide according to claim 13, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 13. An isolated protein or polypeptide according to claim 1, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 7. An isolated protein or polypeptide according to claim 1, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 17. An isolated protein or polypeptide according to claim 1, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 19. 18. An isolated protein or polypeptide according to claim 1, wherein the protein or polypeptide is purified. 19. An isolated protein or polypeptide according to claim 1, wherein the protein or polypeptide is recombinant. 20. An isolated RNA molecule encoding a protein or polypeptide according to claim 1. 21. An isolated RNA molecule according to claim 20, wherein the protein or polypeptide is selected from a group consisting of a polyprotein, an RNA-dependent RNA polymerase, a heat shock protein 70, a heat shock protein 90, a diverged coat protein, and a coating protein. 22. An isolated DNA molecule encoding a protein or polypeptide according to claim 1. 23. An isolated DNA molecule according to claim 22, wherein the protein or polypeptide is selected from a group consisting of a polyprotein, an RNA-dependent RNA polymerase, a heat shock protein 70, a heat shock protein 90, a diverged coat protein, and a coat protein. 24. An isolated DNA molecule according to claim 23, wherein the protein or polypeptide is a polyprotein comprising conserved regions of a helicase, a protease similar to papain, and a methyltransferase. 25. An isolated DNA molecule according to claim 24, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 3. An isolated DNA molecule according to claim 25, wherein the DNA molecule has a nucleotide sequence corresponding to SEQ. ID. DO NOT.
2. 2. An isolated DNA molecule according to claim 23, wherein the protein or polypeptide is an RNA-dependent RNA polymerase having a molecular weight of about 50 to about 54 kDa. 28. An isolated DNA molecule according to claim 27, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 5. An isolated DNA molecule according to claim 28, wherein the DNA molecule has a nucleotide sequence corresponding to SEQ. ID. DO NOT. 4. An isolated DNA molecule according to claim 23, wherein the protein or polypeptide is a heat shock protein 70 having a molecular weight of from about 63 to about 67 kDa. 31. An isolated DNA molecule according to claim 30, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 9. An isolated DNA molecule according to claim 31, wherein the DNA molecule has a nucleotide sequence corresponding to SEQ. ID. DO NOT. 8. An isolated DNA molecule according to claim 23, wherein the protein or polypeptide is a heat shock protein 90 having a molecular weight of about 61 to about 65 kDa. 34. An isolated DNA molecule according to claim 33, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 11. 35. An isolated DNA molecule according to claim 34, wherein the DNA molecule has a nucleotide sequence corresponding to SEQ. ID. DO NOT. 10. 36. An isolated DNA molecule according to claim 23, wherein the protein or polypeptide is a coating protein having a molecular weight of from about 20 to about 24 kDa. 37. An isolated DNA molecule according to claim 36, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 15. 38. An isolated DNA molecule according to claim 37, wherein the DNA molecule comprises a nucleotide sequence corresponding to SEQ. ID. DO NOT. 14. 39. An isolated DNA molecule according to claim 23, wherein the protein or polypeptide is a diverged coat protein having a molecular weight of from about 23 to about 27 kDa. 40. An isolated DNA molecule according to claim 39, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 13. 41. An isolated DNA molecule according to claim 40, wherein the DNA molecule comprises a nucleotide sequence corresponding to SEQ. ID. DO NOT. 12. An isolated DNA molecule according to claim 22, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 7. An isolated DNA molecule according to claim 42, wherein the DNA molecule comprises a nucleotide sequence corresponding to SEQ. ID. DO NOT. 6. 44. An isolated DNA molecule according to claim 22, wherein the protein or polypeptide comprises a nucleotide sequence corresponding to SEQ. ID. DO NOT. 17. 45. An isolated DNA molecule according to claim 44, wherein the DNA molecule comprises a nucleotide sequence corresponding to SEQ. ID. DO NOT. 16. 46. An isolated DNA molecule according to claim 22, wherein the protein or polypeptide comprises an amino acid sequence corresponding to SEQ. ID. DO NOT. 19. 47. An isolated DNA molecule according to claim 46, wherein the DNA molecule comprises a nucleotide sequence corresponding to SEQ. ID. DO NOT. 18. 48. An isolated DNA molecule according to claim 22, wherein the DNA molecule comprises a nucleotide sequence corresponding to SEQ. ID. DO NOT. 23. 49. An expression system comprising a DNA molecule according to claim 22, in a vector heterologous to the DNA molecule. 50. An expression system according to claim 49, wherein the protein or polypeptide is selected from a group consisting of a polyprotein, an RNA-dependent RNA polymerase, a heat shock protein 70, a heat shock protein 90, a diverged coat protein, and a coat protein. 51. A host cell transformed with a heterologous DNA molecule according to claim 22. 52. A host cell according to claim 51, wherein the host cell is selected from the group consisting of Agrobacterium vitis and Agrobacterium tumefaciens. 53. A host cell according to claim 51, wherein the host cell is selected from a group consisting of a grape cell, a citrus cell, a beet cell, and a tobacco cell. 54. A host cell according to claim 51, wherein the protein or polypeptide is selected from a group consisting of a polyprotein, an RNA-dependent RNA polymerase, a heat shock protein 70, a heat shock protein 90, a diverging coating protein, and a coating protein. 55. A cultivable variety of transgenic plant, comprising the DNA molecule according to claim 22. 56. A cultivable variety of transgenic plant according to claim 55, wherein the cultivable plant variety is selected from a cultivable variety of the vine plant, a cultivable variety of a citrus plant, a cultivable variety of a beet plant, and a cultivable variety of a tobacco plant. 57. A cultivable plant strain of transgenic plant according to claim 55, wherein the protein or polypeptide is selected from a group consisting of a polyprotein, an RNA-dependent RNA polymerase, a heat shock protein 70, a heat shock protein 90, a diverged coating protein, and a coating protein. 58. A method of imparting resistance to the virus of the vine leaf roll to a cultivable variety of stem or root material of Vitis or a cultivable variety of Nicotiana, which comprises: transforming a cultivable variety of stem or root material of Vitis or a cultivable variety of Nicotiana with a DNA molecule according to claim 22. 59. A method according to claim 58, wherein the protein or polypeptide is selected from a group consisting of a polyprotein, a polymerase-dependent RNA polymerase. RNA, a heat shock protein 70, a heat shock protein 90, a diverged coat protein, and a coat protein. 60. A method according to claim 58, wherein the vine leaf roll virus is GLRaV-2. 61. A method according to claim 58, wherein said transformation is mediated by Agrobacterium. 62. A method according to claim 58, wherein said transformation comprises: driving particles to vine or tobacco plant cells under conditions effective for the particles to penetrate into the interior of the cells, and introducing an expression vector comprising the DNA molecule inside the cells. 63. A method of imparting resistance to beet yellowing virus to arable beet variety, which comprises: transforming a cultivable beet variety with a DNA molecule according to claim 22. 64. A method according to claim 63, wherein the protein or polypeptide is selected from a group consisting of a polyprotein, an RNA-dependent RNA polymerase, a heat shock protein 70, a heat shock protein 90, a diverged coat protein, and a coating. 65. A method according to claim 63, wherein said transformation is mediated by Agrobacterium. 66. A method according to claim 63, wherein said transformation comprises: driving particles to beet plant cells under effective conditions for the particles to penetrate inside the cells, and introducing an expression vector comprising the DNA molecule into the cells. 67. A method of imparting resistance to the sadness virus to a cultivable variety of scion or cultivable variety of citrus root material, which comprises: transforming a cultivable variety of scion or cultivable variety of citrus root material with a molecule of citrus root. DNA according to claim 22. 68. A method according to claim 67, wherein the protein or polypeptide is selected from a group consisting of a polyprotein, an RNA-dependent RNA polymerase, a heat shock protein 70, a heat shock protein 90, a diverging coat protein, and a coat protein. 69. A method according to claim 67, wherein said transformation is mediated by Agrobacterium. 70. A method according to claim 67, wherein said transformation comprises: driving particles to citrus plant cells under conditions effective for the particles to penetrate into the cells, and introducing an expression vector comprising the DNA molecule inside the cells. 71. An antibody or binding portion thereof or probe that recognizes the protein or polypeptide according to claim 1. 72. An antibody or binding portion thereof or probe according to claim 71, wherein the protein or The polypeptide is selected from a group consisting of a polyprotein, an RNA-dependent RNA polymerase, a heat shock protein 70, a heat shock protein 90, a diverged coat protein, and a coat protein. 73. A method for detecting virus from the vine leaf roll in a sample, said method comprising: providing an antibody or binding portion thereof recognizing the protein or polypeptide according to claim 1; contacting the sample with the antibody or portion that is ligated thereon; and detect any reaction that indicates that the vine leaf roll virus is present in the sample using a test system. 74. A method according to claim 73, wherein said assay system is selected from a group consisting of assayed enzyme-linked immuno-adsorbent, radio-immunoassay, precipitin reaction assay by gel diffusion, immunoassay assay. diffusion, agglutination assay, fluorescent immunoassay, immunoassay of protein A, and assay of immuno-electrophoresis. 75. A method for detecting virus from the vine leaf roll in a sample, said method comprising: providing a nucleotide sequence of the DNA molecule according to claim 22 as a probe in a nucleic acid hybridization assay; contact the sample with the probe; and detect any reaction that indicates that the vine leaf roll virus is present in the sample. 76. A method according to claim 75, wherein the assay for nucleic acid hybridization is selected from a group consisting of dot blot hybridization, tissue printing, Southern hybridization, and Northern hybridization. 77. A method for detecting virus from the vine leaf roll in a sample, comprising: providing a nucleotide sequence of the DNA molecule according to claim 22 as a probe in a gene amplification detection method; contact the sample with the probe; and detect any reaction that indicates that the virus of the vine leaf roll is present in the sample. 78. A method according to claim 77, wherein the method of detecting gene amplification is selected from a group consisting of polymerase chain reaction and immuno-capture polymerase chain reaction.