MXPA97009781A - Induced resistance of hypersensitive response in plan - Google Patents

Abstract

The present invention relates to a method for imparting pathogen resistance to plants, characterized in that it comprises: externally applying to a plant a hypersensitive response-inducing bacterium, which does not cause disease in said plant, or a polypeptide or response-inducing protein hypersensitive, wherein the hypersensitive response-inducing protein or polypeptide corresponds to that derived from a pathogen selected from the group consisting of Erwinia amylovora, Erwinia chrysanthemi, Pseudomonas syringae, Pseudomonas solanacearum, Xanthomonas campestris and mixtures of the

Description

INDUCED RESISTANCE OF HYPERSENSITIVE RESPONSE IN PLANTS FIELD OF THE INVENTION The present invention relates to the delivery of induced resistance of hypersensitive response to plants.

BACKGROUND OF THE INVENTION Living organisms have evolved into a complex arrangement of biochemical pathways that make it possible for them to recognize and respond to environmental signals. These pathways include the receptor organs, the hormones, the second messengers, and the enzymatic modifications. To date, little is known about the signal transduction pathways that are activated during the response of a plant to attack by a pathogen, although this knowledge is central to an understanding of susceptibility and resistance to disease. A common form of plant resistance is the restriction of the proliferation of pathogens to a small area surrounding the site of infection. In many cases, this restriction is accompanied by REF: 26368 localized death (e.g., necrosis) of host tissues. Together, pathogen restriction and local tissue necrosis characterize the hypersensitive response. In addition to local defense responses, many plants respond to infection by activating defenses in uninfected parts of the plant. As a result, the whole plant is more resistant to a secondary infection. This acquired systemic resistance can persist for several weeks or more (REF Matthews, Plant Virology (Academic Press, New York, ed.2, 1981)) and frequently confers cross-resistance to unrelated pathogens (J. Kuc, in Innovative Approaches to Plant Disease Control, I. Chet, Ed. (Wiley, New York, 1987), pp. 255-274, which are incorporated by reference herein). The expression of acquired systemic resistance is associated with the failure of normally virulent pathogens to enter immunized tissue (Kuc, J., "Induced I munity to Plant Disease", Bioscience, 32: 854-856 (1982), which incorporated by reference herein). The establishment of acquired systemic resistance is correlated with systemic increases in cell wall hydroxyproline levels and peroxidase activity (Smith, JA, et al., "Comparative Study of Acidic Peroxidases Associated with Induced Resistance in Cucumber, Musk Elon and Watermelon, "Physiol, Mol Plant Pathol, 14: 329-338 (1988), which is incorporated by reference herein) and with the expression of a group of nine families of the so-called acquired systemic resistance gene (Ward , ER, and collaborators, "Coordinate Gene Activity in Response to Agents that Induce Systemic Acquired Resistance", Plant Cell 3: 49-59 (1991), which is incorporated by reference herein). Five of these families of defense genes code for proteins related to pathogenesis, whose physiological functions have not been established. However, some of these proteins have antifungal activity in vi tro (Bol., JF et al., "Plant Pathogenesis-Related Proteins Induced by Virus Infection", Ann. Rev. Phytopathol. 28: 113-38 (1990), which is incorporated by reference herein) and the constitutive expression of a bean chitinase gene in transgenic tobacco, protects against infection by the fungus Rhi zoctoni a sol ani (Broglie, K., et al., "Transgenic Plants with Enhanced Resistance to the Fungal Pathogen Rhizoctonia Solani ", Science 254: 1194-1197 (1991), which is incorporated by reference herein), suggesting that these acquired systemic resistance proteins may contribute to the immunized state (Uknes, S. et al. , "Acquired Resistance in Arabi dopsis", Plant Cell 4: 645-656 (1992), which is incorporated by reference herein). Salicylic acid seems to play a signal function in the induction of acquired systemic resistance, since endogenous levels increase after immunization (Malamy, J. et al., "Salicylic Acid: A Likely Endogenous Signal in the Resistance Response of Tobacic to Viral Infection", Science 250: 1002-1004 (1990), which is incorporated by reference herein) and exogenous salicylate induces the acquired systemic resistance genes (Yalpani, N. et al., "Salicylic Acid is a Systemic Signal and an Inducer of Pathogenesis-Related Proteins in Virus-Infected Tobacco", Plant Cell 3: 809-818 (1991), which is incorporated herein by reference), and the acquired resistance (Uknes, S. et al., "Acquired resistance in Arabidopsies", Plant Cell 4: 645-656 (1992), which is incorporated by reference herein). In addition, transgenic tobacco plants in which the salicylate is destroyed by the action of a bacterial transgene encoding salicylate-hydroxylase, do not show acquired systemic resistance (Gaffney, T. et al., "Requirement of Salicylic Acid for the Induction. of Systemic Acquired Resistance ", Science 261: 754-296 (1993), which is incorporated by reference herein). However, this effect may reflect the inhibition of a rather local instead of a systemic signal function, and the detailed kinetic analysis of cucumber signal transmission suggests that salicylate may not be essential for long-distance signaling ( Rasmussen, JB et al., "Systemic Induction of Salicylic Acid Accumulation in Cucumber after Inoculation with Pseudomonas Syringae pv. Syringae", Plant Physiol. 97: 1342-1347) (1991), which is incorporated by reference herein). Immunization using biotic agents has been extensively studied. The green beans were systemically immunized against the disease caused by pathogenic strains for the cultures of Col l etotri chum lindemu thi an um through previous infection with non-pathogenic strains for the culture (Rahe, JE, "Induced Resistance in Phaseol us Vulgari s to Bean Anthracnose ", Phytopathology 59: 1641-5 (1969); Elliston, J. et al., "Induced Resistance to Anthracnose at a Distance from the Site of the Inducing Interaction," Phytopathology 61: 1110-12 (1971); Skipp, R. et al, "Studies on Cross Protection in the Anthracnose Disease of Bean" Physiological Plant Pathology 3: 299-313 (1973), which is incorporated by reference herein), pathogenic strains for heat attenuated cultures in the host tissue, before the onset of the symptom (Rahe, JE et al, "Metabolic Nature of the Infection-Limiting Effect of Heat on Bean Anthracnose", Phytopathology 60: 1005-9 (1970), which is incorporated by reference in the present) or non-pathogenic bean. The anthracnose cucumber pathogen, Coll etotri chum lagenari um, was equally effective as the non-pathogenic strains, as an inducer of systemic protection against all strains of bean anthracnose. The protection was induced by C. lagenari um in crops resistant to one or more strains of C. linde? Thianum, as well as in crops susceptible to all the reported strains of the fungus, and which had consequently been termed as' lack of resistance. genetics to the pathogen (Elliston, J. et al., "Protection of Bean Against Anthracnose by Coll etotrichum Species Nonpathogenic on Bean", Phytopathologische Zeitschrift 86: 117-26 (1976); Elliston, J. et al., "A Comparative Study on the Development of Compatible, Incompatible and Induced Incompatible Interactions Between Collectotrichum Species and Phaseolus Vulgaris ", Pytopathologische Zeitschrift 87: 289-303 (1976), which is incorporated by reference herein). These results suggest that the same mechanisms can be induced in crops reported as 'possessors' or 'lacking' genes of resistance (Elliston, J. et al., "Relation of Phytoalexin Accumulation to Local and Systemic Protection of Bean Against Anthracnose", Phytopathologische Zeitschrift 88: 114-30 (1977), which is incorporated by reference herein). It is also apparent that cultures susceptible to all strains of C. lindemuthianum do not lack genes for mechanisms of resistance against the pathogen. Kuc, J. et al., "Protection of Cucumber Against Coll ectotri chum Lagenari um by Coll ec totri ch um Lagenari um "Physiological Plant Pathology 7: 195-9 (1975), which is incorporated by reference herein), showed that cucumber plants could be systemically protected against the disease caused by Coll etotri chum lagenari um by prior inoculation of the cotyledons or the first true leaf with the same fungus. Subsequently, cucumbers have been systemically protected against mycotic, bacterial, and viral diseases by localized prior infection with any fungus, bacteria, or virus (Hammerschmidt, R. et al., "Protection of Cucumbers Against Colletotrichum lagenarium and Cladosporium Cucumerinu", Phytopathology 66: 790-3 (1976); Jenns, AE et al., "Localized Infection with Tobacco Necrosis Virus Protects Cucumber Against Colletotrichum lagenarium", Physiological Plant Pathology 11: 207-12 (1977); Caruso, FL et al., "Induced Resistance of Cucumber to Anthracnose and Angular Leaf Spot by Pseudomonas Lachrymans and Colletotrichum lagenari um ", Physiological Plant Pathology 14: 191-201 (1979); Staub, T. et al.," Systemic Protection of Cucumber Plants Against Disease Caused by Cladospori um cucumerinum and Colletotrichum lagenarium by Prior Localized Infection with Either Fungus ", Physiological Plant Pathology, 17: 389-93 (1980); Berg strom, G.C. et al., "Effects of Local Infection of Cucumber by Coll etotrichum l agenari um, Pseudomonas Lachrymans or Tobacco Necrosis Virus on Systemic Resistance to Cucumber Mosaic Virus", Phytopathology 72: 922-6 (1982); Gessler, C. et al., "Induction of Resistance to Fusarium um Wilt in Cucumber by Root and Foliar Pathogens", Phytopathology 72: 1439-41 (1982); Basha, B. et al., "Tobacco Necrosis Virus Induces Systemic Resistance in Cucumbers Against Sphaerotheca fuli ginea", Physiological Plant Pathology 23: 137-44 (1983), which is incorporated by reference herein). The non-specific protection induced by infection with C. lagenarium or the tobacco necrosis virus was effective against at least 13 pathogens, including obligatory and facultative parasitic fungi, local lesion and systemic viruses, wild fungi, and bacteria . Similarly, protection was induced and was also effective against root pathogens. Other curcurbitaceas, including watermelon and cantaloupe have been systemically preferred against C. Lagenari um (Caruso, FL et al., "Protection of Watermelon and Muskmelon Against Col le to tri ch um l agenari um by Colletotrichura Lagenari um", Phytopahology 67: 1285-9 (1977), which is incorporated by reference herein). Systemic protection in tobacco has also been induced against a wide variety of diseases (Kuc J. et al., "Immunization for Disease Resistance in Tobacco" Recent Advances in Tobacco Science 9: 179-213 (1983), which is incorporated by reference at the moment) . The necrotic lesions caused by the tobacco mosaic virus increased the resistance in areas superior to the disease caused by the virus (Ross, AF et al., "Systemic Acquired Resistance Induced by Localized Virus Infections in Plants", Virology 14: 340-58 (1961); Ross, AF et al., "Systemic Effects of Local Injury Formation," In: Viruses of Plants pp. 127-50 (1966), which is incorporated by reference herein). Phytophthora parasí tica var. Neither cotianae, P. tabacina and Pseudomonas tabaci reduced the reproduction of the aphid Myzus persi cae (Mclntyre, JL et al., "Induction of Localized and Systemic Protection Against Phytophthora Parasí ti ca var. Nicotianae by Tobacco Mosaic Virus Infection of Tobacco Hypersensitive to the Virus ", Physiological Plant Pathology 15: 321-30 (1979); Mclntyre, JL et al.," Effects of Localized Infections of Ni cotiana Tabacum by Tobacco Mosaic Virus on Systemic Resistance Against Diverse Pathogens and an Insect ", Phytopathology 71: 297-301 (1981), which is incorporated by reference herein). The infiltration of P. tabaci died by heat. { Lovrekovich, L. et al., "Induced Reaction Against Wildfire Disease in Tobacco Leaves Treated with Heat-Killed Bacteria", Nature 205: 823-4 (1965), which is incorporated by reference herein), and Pseudomonas solanacearum (Sequeira , L. et al. "Interaction of Bacteria and Host Cell Walls: Its Relation to Mechanisms of Induced Resistance", Physiological Plant Pathology 10: 43-50 (1977), which is incorporated by reference herein), into tobacco leaves , induced resistance with the same bacteria used for infiltration. The tobacco plants were also protected by the nematode Pra tyl enchus penetrans against P. parasí tica var. ni coti ana (Mclntyre, JL et al. "Protection of Tobacco Against Phytophthora Parasitic var. Nicotianae by Cultivar-Nonpathogenic Races, Cell-Free Sonicates and Pra tyl enchus Penetrans", Phytopathology 68: 235-9 (1978), which is incorporated by reference herein). Cruikshank, I.A.M. and collaborators, "The Effect of Stem Infestation of Tobacco with Peronospora Tabacina Adam on Foliage Reaction to Blue Mold ", Journal of the Australian Institute of Agricultural Science 26: 369-72 (1960), which is incorporated by reference herein, were the first to report the immunization of tobacco foliage against blue mold (eg, P. tabaci na) by injection into the stem with the fungus, which also it involved dwarfism and premature senescence. It was recently discovered that injection external to the xylem not only alleviated atrophy but also promoted growth and development. The immunized tobacco plants, in greenhouse and field experiments, were approximately 40% higher, had a 40% increase in dry weight, 30% increase in fresh weight, and 4-6 more leaves than plants control (Tuzun, S. et al, "The Effect of Stem Injections with Peronospora Tabacine and Metalaxyl Treatment on Growth of Tobacco and Protection Against Blue Mold in the Field", Phytopathology 74: 804 (1984), which is incorporated by reference in the present) . These plants bloomed approximately 2 to 3 weeks earlier than the control plants (Tuzun, S. et al., "Movement of a Factor in Tobacco Infected with Peronospora Tabacina Adam which Systemically Protects Against Blue Mold", Physiological Plant Pathology 26: 321-30 (1985), which is incorporated by reference herein). Systemic protection does not confer absolute immunity against infection, but it reduces the severity of the disease and delays the development of the symptom. The number of lesions, the size of the lesions, and the degree of sporulation of the pathogenic fungi are all diminished. The diseased area can be reduced by more than 90%.

When the cucumbers were given a 'booster' inoculation 3 to 6 weeks after the initial inoculation, immunization induced by C. lagenarium lasted through flowering and fruiting (Kuc, J. et al., " Aspects of the Protection of Cucumber Against Coll etotri chum Lagenari um by Colletotrichum Lagenari um ", Phytopathology 67: 533-6 (1977), which is incorporated by reference herein.) The protection could not be induced once the plants had given fruits, the tobacco plants were immunized for the season. of growth by injection into the stem with sporangia of P. tabacina, however, to prevent the systemic development of blue mold, this technique was only effective when the plants were greater than 20 cm in height. Immunized cucumber plants did not reduce the level of immunization of the preexisting expanded leaves, however, the leaves that emerged subsequently from the apical bud were progressively less protected than their predecessors (Dean, RA et al., "Induced Systemic Protection in Cucumber: Time of Production and Movement of the 'Signal' ", Phytopathology 76: 966-70 (1986), which is incorporated by reference herein). Similar results by Ross, A.F., "Systemic Effects of Local Injury Formation", In: Viruses of Plants pp. 127-50 (1986), which is incorporated by reference herein, with tobacco (local injury host) immunized against tobacco mosaic virus by previous infection with the tobacco mosaic virus. In contrast, the new leaves that emerged from the extirpated shoots of the tobacco plants immunized by injection into the stem with P. tabacina were highly protected (Tuzun, S. et al., "Transfer of Induced Resistance in Tobacco to Blue Mold"). Peronospora Tabacina Adam.) Via Callus ", Phytopathology 75: 1304 (1985), which is incorporated by reference herein). Plants regenerated via tissue culture from the leaves of immunized plants showed a significant reduction in blue mold compared to plants regenerated from the leaves of unimmunized progenitors. The young regenerants only showed reduced sporulation. As the plants aged, the development of the lesion and sporulation were reduced. Other researchers, however, did not reach the same conclusion, although a significant reduction in sporulation was reported in one experiment (Lucas, JA et al., "Nontransmissibility to Regenerants from Protected Tobacco Explants of Induced Resistance to Peronospora Hyoscyami", Phytopathology 75 : 1222-5 (1985), which is incorporated by reference herein). The protection of cucumber and watermelon is effective in the greenhouse and in the field (Caruso, F.L. et al., "Field Protection of Cucumber Against Coll etotri chum Lagenari um by C. Lagenari um", Phytopathology 67: 1290-2 (1977), which is incorporated by reference herein). In another test, the total lesion area of C. Lagenari um on protected cucumber was less than 2% of the lesion areas on the unprotected control plants. Similarly, only 1 to 66 protected, challenged plants died, while unprotected watermelons died, 47 out of 69. In extensive field trials in Kentucky and Puerto Rico, tobacco stem injection with P sporangia was killed. Tabacina was at least as effective in controlling blue mold as the best fungicide, metalaxyl. The plants were protected 95 to 99%, based on the necrotic area and the degree of sporulation, leading to an increase in yield of 10-25% in the cured tobacco. The resistance induced against bacteria and viruses seems to be expressed as the suppression of the symptoms of the disease or the multiplication of pathogens or both (Caruso, FL et al., "Induced Resistance of Cucumber to Anthracnose and Angular Leaf Spot by Pseudomonas Lachrymans and Coll etotri ch um Lagenari um ", Physiological Plant Pathology 14: 191-201 (1979); Doss, M., and collaborators, "Systemic Acquired Resistance of Cucumber to Pseudomonas Lachrymans as Expressed in Suppression of Symptoms, but not in Multiplication of Bacteria", Acta Phytopa thologia Academiae Sci entiarum Hungari falls 16: (3-4), 269- 72 (1981); Jenns, A.E. and collaborators, "Non-Specific Resistance to Pathogens Induced Systemically by Local Infection of Cucumber with Tobacco Necrosis Virus, Coll etotri chum Legenari um or Pseudomonas Lachrymans "Mediterranean Phytopathology 18: 129-34 (1979), which is incorporated by reference herein.) As described above, research concerning acquired systemic resistance involves the infection of plants with infectious pathogens Although studies in this area are useful in understanding how acquired systemic resistance works, causing such resistance with infectious agents is not commercially useful, because such contact with the plant pathogen can weaken or kill the pathogens. The present invention is directed to overcome this deficiency.

BRIEF DESCRIPTION OF THE INVENTION The present invention relates to a method for imparting resistance against pathogens to plants. This method involves the application of a hypersensitive response promoter protein or polypeptide in a non-infectious manner, to a plant under conditions where the protein or polypeptide comes into contact with the cells of the plant. Another aspect of the present invention relates to a plant resistant to pathogens, with cells in contact with the non-infectious hypersensitive response protein or polypeptide. Yet another aspect of the present invention relates to a composition for imparting resistance against pathogens to plants. The composition includes a non-infectious hypersensitive response promoter protein or polypeptide and a carrier. The present invention has the potential to: treat plant diseases which were previously intractable; treat diseases systemically that someone would not want to treat separately because of the cost; and avoid the use of infectious agents to treat diseases. The present invention can impart resistance without using pathogens to the plants being treated, or to plants located near those treated. Since the present invention involves the use of a natural product that is completely biodegradable, the environment could not be contaminated.

BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 shows the genetic organization of the genetic cluster that codes for the protein or the hypersensitive response promoter polypeptide, for Erwinia amylovora (for example hrpN). The upper line shows the restriction enzyme map of the plasmid vector pCPP430, where E = EcoRI, B = BamHI, and H = HindIII. The rectangles represent the transcriptional units, and the arrows under the rectangles indicate the directions of transcription. The larger arrow indicates the region necessary for the final translation of the protein or the hypersensitivity response promoting polypeptide. pCPP430 hrpN "is the derivative of pCPP430 in which hrpN is mutated by the transposon insertion TnStac.

Figure 2 is a map of the plasmid vector pCPP9. The significant characteristics are the mobilization site (mob) for the conjugation; the cohesive site of? (eos); and the division region (pair) for stable inheritance of the plasmid. B, BamHI; E, EcoRI; H, HindIII; P, PstI; S, I left; Sm / Smal; oriV, origin of replication; Spr, spectinomycin resistance; Smr, resistance to streptomycin.

DETAILED DESCRIPTION OF THE INVENTION The present invention relates to a method for imparting resistance against pathogens to plants. This method involves the application of a hypersensitive response promoter protein or polypeptide, in a non-infectious manner to all or part of a plant, under conditions where the protein or polypeptide makes contact with all or part of the cells of the plant. Yet another aspect of the present invention relates to a plant resistant to pathogens, with cells in contact with a non-infectious, hypersensitive, responsive protein or polypeptide. Yet another aspect of the present invention relates to a composition for imparting resistance against pathogens to plants. The composition includes a non-infectious, hypersensitive response promoter protein or polypeptide, and a carrier. The protein or hypersensitive response promoter polypeptide used in the present invention may correspond to proteins or polypeptides that elicit hypersensitive responses, derived from a wide variety of pathogens. Such proteins or polypeptides are capable of causing local necrosis in the plant tissue that comes in contact with the provoker. Preferred pathogens include Erwinia amylovora, Erwinia chrysanthemi, Pseudomonas syringae, Pseudomonas solancearum, Xan thomonas campestri s, or mixtures thereof. For purposes of the present invention, the non-infectious forms of the hypersensitive response promoter protein or polypeptide can induce a hypersensitive response, without causing disease in the plant with which the polypeptide or protein is contacted. This can be accomplished in a number of ways, including: 1) the application of an isolated provocative polypeptide or protein; 2) the application of bacteria that do not cause disease and are transformed with genes that code for a protein or polypeptide promoter of hypersensitive response; and 3) the application of bacteria that cause disease in some plant species (but not in those in which they are applied) and naturally contain a gene that codes for the protein or the hypersensitive response promoter polypeptide. In one embodiment of the present invention, the hypersensitive response promoter proteins or polypeptides can be isolated from their corresponding organisms and applied to plants. Such isolation procedures are well known, as described in Arlat, M., F. Van Gijsegem, J.C. Huet, J.C. Pemollet, and C.A. Boucher, "PopAl, to Protein which Induces to Hypersensitive-like Response in Specific Petunia Genotypes is Secreted via the Hrp Pathway of Pseudomonas sol anacearum" EMBO J. 13: 543-553 (1984); He, SY, HC Huang, and A. Collmer, "Pseudomonas syringae pv. Syringae Harpin->,: a Protein that is Secreted via the Hrp Pathway and Elicits the Hypersensitive Response in Plants", Cell 73: 1255-1266 ( 1993); and Wei, Z. -M., R.J. Laby, C.H. Zumoff, D.W. Bauer, S. -Y. He, A. Collmer, and S.V. Beer, "Harpin Elicitor of the Hypersensitive Response Produced by the Plant Pathogen Erwini a amyl ovora, Science 257: 85-88 (1992), which is incorporated herein by reference. See also co-pending US Patent Application Ser. 08 / 200,024 and 08 / 062,024, which are incorporated by reference herein Preferably, however, the hypersensitive response promoter proteins or polypeptides, isolated from the present invention, are recombinantly produced and purified as described below. In other embodiments of the present invention, the protein or hypersensitive response promoter polypeptide of the present invention can be applied to plants by the application of bacteria containing genes encoding the protein or the hypersensitive response promoter polypeptide. Such bacteria must be capable of secreting or exporting the protein or polypeptide, so that the provoker can come into contact with plant cells. In these embodiments, the protein or hypersensitive response promoter polypeptide is produced by the bacteria in plants or just before the introduction of the bacteria to plants. In one embodiment of the bacterial application mode of the present invention, the bacteria do not cause disease and have been transformed (e.g., recombinantly) with genes encoding a hypersensitive response promoter protein or polypeptide. For example, E. coli, which does not elicit a hypersensitive response in plants, can be transformed with genes encoding a hypersensitive response promoter protein or polypeptide and then applied to plants. Bacterial species (other than E. coli) can also be used in this embodiment of the present invention. In yet another embodiment of the bacterial application mode of the present invention, the bacteria do cause disease and naturally contain a gene encoding a hypersensitive response promoter protein or polypeptide. Examples of such bacteria are those noted above. However, in this modality these bacteria are applied to plants that are not susceptible to the disease carried by the bacteria. For example, Erwini to amyl ovora causes disease in apple or pear, but not in tomato. However, such bacteria will promote a hypersensitive response in tomatoes. Accordingly, according to this embodiment of the present invention, Erwinia amyl ovora can be applied to the tomato to impart resistance to pathogens, without causing disease in that species. The protein or hypersensitive response promoter polypeptide from Erwini to chrysanthejpi has an amino acid sequence corresponding to SEQ ID No. 1 as follows: Met Gln lie Thr lie Lys Wing His lie Gly Gly Asp Leu Gly Val Ser 1 5 10 15 Gly Leu Gly Wing Gln Gly Leu Lys Gly Leu Asn Being Wing Wing Being Ser 20 25 30 Leu Gly Ser Ser Val Asp Lys Leu Ser Ser Thr lie Asp Lys Leu Thr 35 40 45 Be Wing Leu Thr Ser Met Met Phe Gly Gly Wing Leu Wing Gln Gly Leu 50 55 60 Gly Ala Ser Ser Lys Gly Leu Gly Met Ser Asn Gln Leu Gly Gln Ser 65 70 75 80 Phe Gly Asn Gly Wing Gln Gly Wing Being Asn Leu Leu Being Val Pro Lys 85 90 95 Ser Gly Gly Asp Ala Leu Ser Lys Met Phe Asp Lys Ala Leu Asp Asp 100 105 110 Leu Leu Gly His Asp Thr Val Thr Lys Leu Thr Asn Gln Ser Asn Gln 115 120 125 Leu Ala Asn Ser Met Leu Asn Ala Ser Gln Met Thr Gln Gly Asn Met 130 135 140 Asn Ala Phe Gly Ser Gly Val Asn Asn Ala Leu Ser Ser lie Leu Gly 145 150 155 160 Asn Gly Leu Gly Gln Being Met Being Gly Phe Being Gln Pro Being Leu Gly 165 170 175 Wing Gly Gly Leu Gln Gly Leu Ser Gly Wing Gly Wing Phe Asn Gln Leu 180 185 190 Gly Asn Wing He Gly Met Gly Val Gly Gln Asn Ala Wing Leu Ser Wing 195 200 205 Leu Ser Asn Val Ser Thr His Val Asp Gly Asn Asn Arg His Phe Val 210 215 220 Asp Lya Glu Asp Arg Gly Met Wing Lys Glu He Gly Gln Phe Met Asp 225 230 235 240 Gln Tyr Pro Glu He Phe Gly Lys Pro Glu Tyr Gln Lys Asp Gly Trp 245 250 255 Ser Ser Pro Lys Thr Asp Asp Lys Ser Trp Ala Lys Ala Leu Ser Lys 260 265 270 Pro Asp Asp Asp Gly Met Thr Gly Ala As Met Asp Lys Phe Arg Gln 275 280 285 Wing Met Gly Met He Lys Ser Wing Val Wing Gly Asp Thr Gly Asn Thr 290 295 300 Asn Leu Asn Leu Arg Gly Wing Gly Gly Wing Being Leu Gly He Asp Wing 305 310 315 320 Ala Val Val Gly Asp Lys He Ala Asn Met Ser Leu Gly Lys Leu Ala 325 330 335 Asn Ala This hypersensitive response promoter protein or polypeptide has a molecular weight of 34 kDa, is heat stable, has a glycine content greater than 16%, and does not substantially contain cysteine. The protein or hypersensitive response promoter polypeptide of Erwinia chrysan themi is encoded by a DNA molecule having a nucleotide sequence corresponding to SEQ ID No. 2 as follows: CGATTTTACC CGGGTGAACG TGCTATGACC GACAGCATCA CGGTATTCGA CACCGTTACG 60 GCGTTTATGG CCGCGATGAA CCGGCATCAG GCGGCGCGCT GGTCGCCGCA ATCCGGCGTC 120 GATCTGGTAT TTCAGTTTGG GGACACCGGG CGTGAACTCA TGATGCAGAT TCAGCCGGGG 180 CAGCAATATC CCGGCATGTT GCGCACGCTG CTCGCTCGTC GTTATCAGCA GGCGGCAGAG 240 TGCGATGGCT GCCATCTGTG CCTGAACGGC AGCGATGTAT TGATCCTCTG GTGGCCGCTG 300 CCGTCGGATC CCGGCAGTTA TCCGCAGGTG ATCGAACGTT TGTTTGAACT GGCGGGAATG 360 ACGTTGCCGT CGCTATCCAT AGCACCGACG GCGCGTCCGC AGACAGGGAA CGGACGCGCC 420 CGATCATTAA GATAAAGGCG GCTTTTTTTA TTGCAAAACG GTAACGGTGA GGAACCGTTT 480 CACCGTCGGC GTCACTCAGT AACAAGTATC CATCATGATG CCTACATCGG GATCGGCGTG 540 GGCATCCGTT GCAGATACTT TTGCGAACAC CTGACATGAA TGAGGAAACG AAATTATGCA 600 AATTACGATC AAAGCGCACA TCGGCGGTGA TTTGGGCGTC TCCGGTCTGG GGCTGGGTGC 660 TCAGGGACTG AAAGGACTGA ATTCCGCGGC TTCATCGCTG GGTTCCAGCG TGGATAAACT 720 GAGCAGCACC ATCGATAAGT TGACCTCCGC GCTGACTTCG ATGATGTTTG GCGGCGCGCT 780 GGCGCAGGGG CTGGGCGCCA GCTCGAAGGG GCTGGGGATG AGCAATCAAC TGGGCCAGTC 840 TTTCGGCAAT GGCGCGCAGG GTGCGAGCAA CCTGCTATCC GTACCGAAAT CCGGCGGCGA 900 TGCGTTGTCA AAAATGTTTG ATAAAGCGCT GGACGATCTG CTGGGTCATG ACACCGTGAC 960 CAAGCTGACT AACCAGAGCA ACCAACTGGC TAATTCAATG CTGAACGCCA GCCAGATGAC 1020 CCAGGGTAAT ATGAATGCGT TCGGCAGCGG TGTGAACAAC GCACTGTCGT CCATTCTCGG 1080 CCAGGGTCTC GGCCAGTCGA TGAGTGGCTT CTCTCAGCCT TCTCTGGGGG CAGGCGGCTT 1140 GCAGGGCCTG AGCGGCGCGG GTGCATTCAA CCAGTTGGGT AATGCCATCG GCATGGGCGT 1200 GGGGCAGAAT GCTGCGCTGA GTGCGTTGAG TAACGTCAGC ACCCACGTAG ACGGTAACAA 1260 CCGCCACTTT GTAGATAAAG AAGATCGCGG CATGGCGAAA GAGATCGGCC AGTTTATGGA 1320 TCAGTATCCG GAAATATTCG GTAAACCGGA ATACCAGAAA GATGGCTGGA GTTCGCCGAA 1380 GACGGACGAC AAATCCTGGG CTAAAGCGCT GAGTAAACCG GATGATGACG GTATGACCGG 1440 CGCCAGCATG GACAAATTCC GTCAGGCGAT GGGTATGATC AAAAGCGCGG TGGCGGGTGA 1500 TACCGGCAAT ACCAACCTGA ACCTGCGTGG CGCGGGCGGT GCATCGCTGG GTATCGATGC 1560 GGCTGTCGTC GGCGATAAAA TAGCCAACAT GTCGCTGGGT AAGCTGGCCA ACGCCTGATA 1620 ATCTGTGCTG GCCTGATAAA GCGGAAACGA GGGGAAGCCT GTCTCTTTTC 1680 TTATTATGCG GTTTATGCGG TTACCTGGAC CGGTTAATCA TCGTCATCGA TCTGGTACAA 1740 ACGCACATTT TCCCGTTCAT TCGCGTCGTT ACGCGCCACA ATCGCGATGG CATCTTCCTC 1900 GTCGCTCAGA TTGCGCGGCT GATGGGGAAC GCCGGGTGGA ATATAGAQAA ACTCGCCGGC 1860 CAGATGGAGA CACGTCTGCG ATAAATCTGT GCCGTAACGT GTTTCTATCC GCCCCTTTAG_1920_CAGATAGATT GCGGTTTCGT AATCAACATG GTAATGCGGT TCCGCCTGTG CGCCGGCCGG 1980 GATCACCACA ATATTCATAG AAAGCTGTCT TGCACCTACC GTATCGCGGG AGATACCGAC 2040 AAAATAQGGC AGTTTTTGCG TGGTATCCGT GGGGTGTTCC GGCCTGACAA TCTTGAGTTG 2100 GTTCGTCATC ATCTTTCTCC ATCTGOGCGA CCTGATCGGT T 2141 The protein or hypersensitive response promoter polypeptide of Erwinia amylovora has an amino acid sequence corresponding to SEQ ID No. 3 as follows: Met Ser Leu Asn Thr Ser Gly Leu Gly Ala Ser Thr Met Gln He Ser 1 5 10 15 He Gly Gly Wing Gly Gly Asn Asn Gly Leu Leu Gly Thr Being Arg Gln 20 25 30 Asn Wing Gly Leu Gly Gly Asn Wing Wing Leu Gly Leu Gly Gly Gly Asn 35 40 45 Gln Asn Asp Thr Val Asn Gln Leu Wing Gly Leu Leu Thr Gly Met Met 50 55 60 Met Met Met Met Met Met Gly Gly Gly Gly Lely Met Gly Gly Gly Leu 65 70 75 80 Gly Gly Gly Leu Gly Gly Asn Glu Lely Gly Gly Be Gly Glu Leu Glu 85 90 95 Gly Leu Ser Asn Ala Leu Asn Asp Met Leu Gly Gly Ser Leu Asn Thr 100 105 110 Leu Gly Ser Lys Gly Gly Asn Asn Thr Thr Ser Thr Thr Asn Ser Pro 115 120 125 Leu Asp Gln Wing Leu Gly He Asn Ser Thr Ser Gln Asn Asp Asp Ser 130 135 140 Thr Ser Gly Thr Asp Ser Thr Ser Asp Ser Ser Asp Pro Met Gln Gln 145 150 155 160 Leu Leu Lys Met Phe Ser Glu He Met Gln Ser Leu Phe Gly Asp Gly 165 170 175 Gln Asp Gly Thr Gln Gly Be Ser Gly Gly Lyn Gln Pro Thr Glu 180 185 190 Gly Glu Gln Asn Wing Tyr Lys Lys Gly Val Thr Asp Wing Leu Ser Gly 195 200 205 Leu Met Gly Asn Gly Leu Ser Gln Leu Leu Gly Asn Gly Gly Leu Gly 210 215 220 Gly Gly Gln Gly Gly Asn Wing Gly Thr Gly Leu Asp Gly Ser Ser Leu 225 230 235 240 Gly Gly Lye Gly Leu Gln Asn Leu Ser Gly Pro Val Asp Tyr Gln Gln 245 250 255 Leu Gly Asn Wing Val Gly Thr Gly He Gly Met Lys Wing Gly He Gln 260 265 270 Ala Leu Asn Asp He Gly Thr His Arg His Being Ser Thr Arg Ser Phe 275 280 285 Val Asn Lys Gly Asp Arg Ala Met Ala Lys Glu He Gly Gln Phe Me? 290 295 300 Asp Gln Tyr Pro Glu Val Phe Gly Lys Pro Gln Tyr Gln Lys Gly Pro 305 310"315 320 Gly Gln Glu Val Lys Thr Asp Asp Lys Ser Trp Ala Lys Ala Leu Ser 325 330 335 Lys Pro Asp Asp Asp Gly Met Thr Pro Wing Ser Met Glu Gln Phe Asn 340 345 350 Lya Ala Lys Gly Met He Lyu Arg Pro Met Ala Gly Asp Thr Gly Asn 355 360 365 Gly Asn Leu Gln His Wing Val Pro Val Val Leu Arg Trp Val Leu Met 370 375 380 Pro 385 This hypersensitive response promoter protein or polypeptide has a molecular weight of about 37 kDa, has a pl of about 4.3, and is heat stable at 100 ° C for at least 10 minutes. This protein or hypersensitive response promoter polypeptide has substantially no cysteine. The protein or hypersensitive response promoter polypeptide derived from Erwinia amylovora is described more fully in Wei, Z. -M., R. J. Laby, C. H. Zumoff, D. W. Bauer, S.-Y. He, A. Collmer, and S. V. Beer, "Harpin, Elicitor of the Hypersensitive Response Produced by the Plant Pathogen Erwinia amylovora", Science 257: 85-88 (1992), which is incorporated by reference herein. The DNA molecule encoding this protein or polypeptide has a nucleotide sequence corresponding to SEQ ID No. 4 as follows: ATOAOTCTOA AXAC ?? aV8 (SCTOO?? OCO TCAACOATOC AAATTTCTAT COQCOOTOCO CO? QQXl ??? T? ACQQU? "1UCT QQUTACC? UT CQCCACl? ATQ CTOOOTTOOQ TOOCAATTCT 120 OCACTOOOOC t8ac8o8 TAATCAAAAT OATACCOTCA ATCAOCTOOC TOOCTTACTC 180 ACCQQCATGA TO? TO? Q? T aAOCATOATO: OR COQTOXI to 8CTXaATOGC COOTQOCTT? 240 oacosroocT TAOOTAATOO CTTOQOTQOC TCMOTOQCC TOOOCOX? OO ACTOTCOAAC 300 rcacTOAAco ATATsrtAßa cwn? Ucru AACACGCTOQ acrcaAAAos COOCAACAAT 360 ACCACTTCAA C ?? C ??? TTC CCCOCTOOAC C? OOCOC 8 OTATTAACTC AACOTCCCAA 420 AACOAGOATT CCACCTCO8 CACAOATTCC ACCTCAOACr CCAOCOACCC OATßCAOCAß 480 CTQCTGAAO? TOTTCAOCOA QATAATOCAA AOCCTOTTTQ OTOATCXMCA AO? TOOC? CC 540 CAaaacAiOTT ccTcraarjoa CA? OC? Occa ACCOAAOOCO AOCASAACOC CTATAAAAAA 600 OX3AOTCACTa ATOOOCTOTC OXIACCTOATO OOTAAT8TC TGMOCCAGCT CCT OOCAAC 660 Q9QQQAGTQQ OAOOTOOTCA OOOOOOTAAT OCTQQCAGQQ OTCTTOAOOQ TTCßTCOC O 720 oacaac ??? o QOCTOCAAAA CCTOAOCOOO CC8T8ACT ACCAQCAOTT AOQTAACOCC 780 wi # uu *. »T > v.vu mimwfc? n. MAJVJ MXWT CvaU ACOCAC 840 AOOCACAOTT CAACCCOTTC TTTOOTCAAT AAAOQCaATC OOX? COATOOC (sA? QOA? AXC 900 OOTCAO CA TQQACCAOX? CCTOAOOTO L'i'ivOO? OC CQCAOTACCA fflA AOQCPCTl 960 rMT AOOAOa Ta ?? ACOa? TaACAAATCA TsOOCAAAAQ CACTO? ßCA? ßCCAdATOAC 1020 a? O8AATO? CACCAOCCAO TATOCJAOCAß TTCAACAA? A CCAAOOOCAT O? TC ???? Oa 1080 CCCATOQCOO OTOATACCOß OUkC8CAAC CTOCAOCACO CßßTOCCOOT OOTTCTTCOC OOOTAT 1140 OA 1158 TSCCATOA The protein or polypeptide promoter hypersensitive response derived from Pseudomonas syringae has an amino acid sequence corresponding to SEQ ID No. 5 as follows: Mat Oln Ser Leu Being Leu Aan Being Ser Leu Qln Thr Pro? La Met 1 5 10 15? The Lau Val Leu Val? Rg Pro aiu? La Olu Thr Thr Oly Sar Thr Ser 20 25 30 Ser Lya? The Leu Oln Olu Val Val Val Ly? Leu? The Olu Olu Lau Met 35 40 45? Rg? an Oly Oln Lau? ap? ap Sar Ser Pro Leu.-Ql.y-Lys-Leu-L? u- la- 50 SS 60 Lya Ser Mat? la? la? sp Qy Lys? the Oly Oly Oly lie Olu? ap Val 65 70 75 80 He? La? Leu? Ap Lya Lau Xl? His Olu Lys Leu Oly? Sp? Sn Phe 85 90 95 Qly? La?? Ser? La Ser Oly Thr Qly Oln Qln? Ap Lau Met 100 105 110 Thr Qln Val Lau? Sn Oly Leu? The Lya Sar Met Leu? Sp? ßp Leu Leu 115 120 125 Thr Lys Oln? Sp Qly Oly Thr Ser Phe Ser Olu? ßp? ßp Met Pro Met 130 135 140 Leu? sn Lyß lie? the Oln Phe Met? sp? sp? sn Pro? the Oln Phe Pro 145 150 155 160 Lyß Pro? ßp Ser Oly Ser Trp Val? An Qlu Leu Lya Qlu? Sp? ßn Phe 165 170 175 Leu? ßp Oly? Sp Olu Thr? La? The Phe? Rg Ser? La Leu? Ap lia Ha 180 185 190 Oly Qln Oln Lau Oly? Sn Qln Oln Ser? Sp? The Oly Ser Leu? The Oly 195 200 205 Thr Qly Oly Oly Lau Oly Thr Pro Ser Ser Pha Ser? Sn? Sn Sar Sar 210 215 220 Val Met Qly? ß Pro Leu I? SSPs? the? SSNs Thr QLY Pro QLY? SSPs Ser 225230235240 QLY? SSNs Thr? rg Oly Qlu? the QLY QLn Leu Zla QLY Qlu Leu He? SSPs 245250255? rs Qv Lau QLn Sar Val Leu? the QLY QLY QLY Lau QLY Thr Pro Val ^ J 260265270? SSN Thr Pro QLn Thr Oly Thr Ser? the? SSN QLY QLY QLn Ser? the QLn 275280285? SSP Leu? SSPs QLn Leu Leu Oly QLY Leu Leu Leu Lyß Qly Leu Q u? La 290 295 300 Thr Lau Lya? Ap? La Qly Qln Thr Qly Thr? ßp Val Oln Ser Sar? La 305 310 315 320? The Qln Ha? The Thr Leu Leu Val Ser Thr Lau Lau Qn Oly Thr? Rg 325 330 335? ßn Qln? The? La? This protein or hypersensitive response promoter polypeptide has a molecular weight of 34 to 35 kDa. It is rich in glycine (approximately 13.5%) and lacks cysteine and tyrosine. Additional information regarding the hypersensitive response promoter derived from Pseudomonas syringae, is found in He, SY, HC Huang, and A. Collmer, "Pseudomonas syringae pv. Syringae HarpinPs!,: A Protein that is Secreted via the Hrp Pathway and Elicits the Hypersensitive Response in Plants ", Cell 73: 1255-1266 (1993), which is incorporated by reference herein. The DNA molecule encoding the hypersensitive response promoter of Pseudomonas syringae has a nucleotide sequence corresponding to SEQ ID No. 6 as follows: ATQCAQ? OTC TC? QTCTTA? CAQC? QCTOO CTOCAAACCC CQQC ?? TQQC CCTTQTCCTO 60 ßTACOTCCTO ?? QCOQ? Q? C QCTQQC? OT ACOTCQAQC? AQQCQCTTCAQQQQTTQTC 120 ßTß? AQCTQO COQAQQAACT QATQCQCAAT OOTCAACTCO ACOACAQCTC OCCATTQQQA 180 A ?? CTQTTQQ CCAAOTCOAT QQCOOC? Q? T QOCAAQßCQQ QCaaCQQTAT TQ? QQ? TQTC 240 ATCQcracoc TQa? CAAQCT OATCCATOAA AAQCTOQOTß ACAACTTCOa CQOSTCTQCQ 300 OACAQCOCCT CQQQT? OOQQ AC? QCAQaAC CTOATOACTC AQQTQCTCA? TQQCCTQQCC 360 A? QTCQ? TQC TCQATQATCT TCTQACC ?? Q CAOOATOOCO OOACAAOCTT CTOCQAAQ? C 420 OATATOCCOA TQCTß ?? C ?? Q? TOQOQC? Q TTCATQQ? TQ 480 AAOCCOßACT ACAATCCCOC ACAßTTTCCC cocKicmrm OQTQAACAA CTCAAQß ACAACTU Q ?? G ?? ACQQCTO Q TaATOOCOAC 540 TC OOCACTCQAC witaw ATCATTOOCC? CTQQQ TAATCAQCAQ 600 BC ?? AQTQAOQCTQ OCAQTCTOQC AQQQ? CQQflT QUUnTCTQQ OCACTCCOAQ C-660 AQTTTTTCC AACAACTCQT COQTßATOOQ TOATCCßCTQ ATCOACQCCA? TAOCQQTOC CQQTßACAQC 720 QQCAAT? CCC QTQQTQAAQC QQaac ?? CTQ ATcaacoAac TTATCQACCQ TQQOCTOCAA 780 TOQST? TTQQ COQQTQQTQQ ACTOOOCACA CCOQT ??? C? cccoac? a? c oaaT? OQTca 840 QOQAATQOOQ QACAQTCCOC TCAOQATCTT to? TCAQTTQC TßQQCQQCTT QCTOCTCAAQ OOOCTQG- 900? M CAAOOCTCAA OSAXOOOCMQ CAAACAOOC? CCOACOTOCA ßTOCDVOOQCT 960 acsc ?? ATcrj CCACCTQCT QOTCAQT? Oa CTOC OCAAO OCACCCOCAA TCAOOCTOCA 1020 GCCTGA 1026 The protein or the polypeptide promoter of hypersensitive response derived from Pseudomonas solanacearum has an amino acid sequence corresponding to SEQ ID No. 7 as follows: Met Ser Val Gly? Sn He Gln Ser Pro Be Asn Leu Pro Gly Leu Gln 1 5 10 1S Asn Leu Asn Leu Asn Thr Asn Thr Asn Ser Gln Gln Ser Gly Gln Ser 20 - 25 30 Val Gln Asp Leu He Lys Gln Val Glu Lya Asp? Le Le Asn Zle He 35 40 45 Ala Ala Leu Val Gln Lys Ala Ala Gln Ser? La Gly Gly Asn Thr Gly 50 55 60 Asn Thr Gly? Sn? The Pro Ala Lys Asp Gly? Sn? The Asn Ala Gly Wing 65 70 - 75 T0 Asn Asp Pro Ser Lys Asn Asp Pro Ser Lys Ser Gln Ala Pro Gln Ser 85 90 95 Wing Asn Lyß Thr Gly Asn Val Asp Asp Wing Asn Aßn Gln Asp Pro Met 100 105 lio Gln Ala Leu Met Gln Leu Leu Glu Asp Leu Val Lys Leu Leu Lys Wing 115 120 125 Wing Leu Hia Met Gln Gln Pro Gly Gly Asn Asp Lya Gly Asn Gly Val 130 135 140 Gly Gly Wing Asn Oly Wing Lys Gly Wing Gly Gly Gln Gly Gly Leu Wing 145 150 155 160 Glu Ala Leu Gln Glu lie Glu Gln He Leu? The Gln Leu Gly Gly Gly 165 170 175 Gly Wing Gly Wing Gly Gly Wing Gly Gly Gly Val Gly Gly Wing Gly Gly 180 165 190 Wing Asp Gly Gly Ser Gly? Gly Gly Wing Gly Wing Wing Asn Gly Wing 195 200 205 Asp Gly Gly Asn Oly Val Aßn Gly Asn Oln Wing Asn Gly Pro G n Asn 210 215 220 Wing Gly Asp Val Asn Gly Wing Asn Gly Wing Asp Asp Gly Ser Glu Asp 225 230 235 240 Gln Gly Gly Leu Thr ßly Val Leu Gln Lys Leu Met Lys? Le Leu Asn 245 250 255 Wing Leu Val Gln Met Mee Gln Gln Gly Gly Leu Gly Oly Gly Asn Gln 2 (0 265 270 Wing Gln Gly Gly Ser V / t Gly Wing Gly Asn Wing Pro Wing Ser Gly 275 280 265 Wing SG Pro Gly Wing Asn Gln Pro Gly Ser Wing Asp Asp Gln Ser Ser 290 295 300 Gly Gln Asn Asn Leu Gln Ser ßln? Le Met Asp Val Val Lys Glu Val 305 310 315 320 Val Gln? Le Leu Gln Gln Met Leu Ala Wing Oln? Sn Gly Gly Ser Qln 325 330 335 Oln Ser Thr Ser Thr Gln Pro Met 340 This is encoded by a DNA molecule having a nucleotide sequence corresponding to SEQ ID No. 8 as follows: ATOTCAOTCO OAAACATCCA QAGCCCGTCO AACCTCCCGO OTCTOCAGAA CCTGAACCTC 60 AACACCAACA CCAACAGCCA GCAATCGGGC CAGTCCGTQ? AAGACCTGAT CAAGCAGGTC 120 GAGAAGGACA TCCTCAACAT CATCGC? OCC CTCGTOCAGA AGGCCGCACA GTCGGCGOOC 180 GGCAACACCG GTAACACCGG CAACGCGCCG GCGAAGGACG GCAATGCCAA CGCGGGCGCC 240 AACGACCCGA GCAAGAACGA CCCGAGCAAG AOCCAOGCTC CGCAGTCGGC CAACAAGACC 300 GGCAACGTCG ACGACOCCAA CAACCAGGAT CCGATGCAAO CGCTOATGCA GCTGCTGGAA 360 GACCTOGTGA AGCTGCTGAA GGCOGCCCTG CACATGCAGC AOCCCOGCGG CAATGACAAß 420 GGCAACGGCG TGGOCOOTOC CAACOGCOCC AAGGOTOCCG OCGGCCAOOG CGOCCTGGCC 80 GAAGCGCTGC AGOAGATCGA OCAGATCCTC GCCCAGCTCG OCGGCGOCGO TGCTssCGCC 540 GGCGGCGCGG GTOOCOGTGT CGGCGGTGCT GGTGGCGCGG ATGGCOGCTC CGGTGCGGGT 600 GGCGCAGGCO GTGCGAACGG CGCCGACGGC GOCAATGGCG TGAACGGCAA CCAGGCGAAC 660 GOCCCGCAGA ACOCAGOCGA TGTCAACGGT ßCCAACGGCG CGGATGACGG CAGCGAAGAC 720 CAOOOCGGCC TCACCOOCGT GCTGCAAAAG CTGATGAAGA TCCTGAACGC GCTGGTGCAG 780 ATGATQC? GC AAOOCGOCCT CCßCOGCOOC AACCAGGCGC AGGGCGGCTC GAAGGOTGCC 840 GGCAACGCCT COCCOGCTTC CGGCGCGAAC CCGOGCGCGA ACCAGCCCGG TTCGGCOGAT 900 GATCAATCGT CCOOCCAGAA CAATCTGCAA TCCCAGATCA TOGATGTOGT GAAGGAGOTC 960 OTCCAOATCC TO-CAGCAGAT OCTOGCGGCG CAGAACGGCG GCAGCCAOCA GTCCACCTCG 1020 ACOCAGCCGA TOTAA 2,035 Additional information regarding the hypersensitive response protein or polypeptide derived from Pseudomonas solanacearum is described in Arlat, M., F. Van Gijsegem, J.C. Huet, J.C. Pemollet, and CA Boucher, "PopAl, a Protein which Induces a Hypersensitive-like Response in Specific Petunia Genotypes, is Secreted via the Hrp Pathway of Pseudomonas solanacearum" EMBO J. 13: 543-533 (1994), which is incorporated by reference in the present. The protein or hypersensitive response promoter polypeptide of Xanthomonas campestri s pv. Glycine, has an amino acid sequence corresponding to SEQ ID No. 9 as follows: Thr Leu Leu Glu Met He Val Val Ala He He Ala Ala Leu Ala 1 5 10 15 Ala He Ala Leu Pro Ala Tyr Gln Asp Tyr 20 25 This sequence is an amino terminal sequence that has 26 residues only from the protein or the hypersensitive response promoter polypeptide of Xan thomonas campestri s pv. Wisteria This is coupled with the proteins of the fimbrial subunit determined in other pathogenic variants of Tan thomouas campestri s.

The above promoters are exemplary. Other promoters can be identified by the development of bacteria that promote a hypersensitive response under which the genes encoding a promoter are expressed. Cell-free preparations from culture supernatants can be tested for promoter activity (eg, local necrosis) by using them to infiltrate the appropriate plant tissues. It is also possible to use fragments of the aforementioned hypersensitive response promoter proteins or polypeptides, as well as fragments of full length promoters from other pathogens, in the method of the present invention. Suitable fragments can be produced by various means. In the first, subclones of the gene that codes for a known promoter protein are produced by conventional molecular genetic manipulation, by subcloning genetic fragments. The subclones are then expressed in vi tro or in vi in bacterial cells, to produce a smaller protein or a peptide that can be tested for promoter activity according to the procedure described below.

As an alternative, fragments of a promoter protein can be produced by digestion of a full-length promoter protein, with proteolytic enzymes similar to chymotrypsin or proteinase A from Staphylococcus, or trypsin. It is likely that different proteolytic enzymes break the promoter proteins at different sites, based on the amino acid sequence of the promoter protein. Some of the fragments that result from proteolysis can be active resistance promoters. In yet another procedure, based on knowledge of the primary structure of the protein, fragments of the promoter protein gene can be synthesized by using the PCR technique, together with specific groups of primers chosen to represent the particular portions of the protein. These could then be cloned into an appropriate vector to increase and express a truncated peptide protein. The variants can also (or alternatively) be modified by, for example, deleting or adding amino acids that have minimal influence on the properties, secondary structure and hydropathic nature of the polypeptide.

For example, a polypeptide can be conjugated to a signal sequence (or leader) at the N-terminus of the protein, which co-translationally or post-translationally directs the transfer of the protein. The polypeptide can also be conjugated to a linker or to another sequence to facilitate the synthesis, purification or identification of the polypeptide. The protein or polypeptide of the present invention are preferably produced in purified form (preferably at least 80%, more preferably 90%, pure) by conventional techniques. Typically, the protein or polypeptide of the present invention is secreted into the growth medium of recombinant E. coli. To isolate the protein, the host cell of E. coli having a recombinant plasmid is propagated, homogenized, and the homogenate is centrifuged to remove the bacterial waste. The supernatant is then subjected to sequential precipitation with ammonium sulfate. The fraction containing the polypeptide or protein of the present invention is subjected to gel filtration on a dextran or polyacrylamide column of suitable size, to separate the proteins. If needed, the protein fraction can also be purified by HPLC. The DNA molecule encoding the hypersensitive response promoter protein or polypeptide can be incorporated into the cells using conventional recombinant DNA technology. In general, this involves the insertion of the DNA molecule into an expression system for which the DNA molecule is heterologous (for example it is not normally present). The heterologous DNA molecule is inserted into the expression system or vector in the proper sense orientation and in the correct reading structure. The vector contains the elements necessary for the transcription and translation of the inserted sequences that code for the protein. The North American Patent No. 4, 237,224 to Cohen and Boyer, which is incorporated by reference herein, describes the production of expression systems in the form of recombinant plasmids using cleavage by restriction enzymes and ligation with DNA ligase. These recombinant plasmids are then introduced by means of transformation and replicated into unicellular cultures including prokaryotic organisms and eukaryotic cells grown in tissue culture. Recombinant genes can also be introduced into viruses, such as vaccinia virus. Recombinant viruses can be generated by transfection of plasmids into 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 plasmid vectors such as pBR322, pBR325, pACYC177, pACYC184, pUC8, pUC9, pUC18, pUC19, pLG339, pR290, pKC37, pKClOl, SV 40, pBluescript IISK +/- or KS +/- (see "Stratagene Cloning Systems" Catalog (1993) by Stratagene, La Jolla, California, which is incorporated by reference in the present), pQE, pIH821, pGEX, the pET series (see FW Studier et al., "Use of T7 RNA Polymerase to Direct Expression of Cloned Genes", Gene Expression Technology vol.185 (1990), which is incorporated by reference in the present), and any derivatives thereof. Recombinant molecules can be introduced into cells via transformation, particularly 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 Cloning: A Laboratory Manual, Cold Springs Laboratory, Cold Springs Harbor, New York (1982), which is incorporated by reference herein. A variety of host-vector systems can be used to express the sequence (s) that code for the protein. Primarily, the vector system must be compatible with the host cell used. Host-vector systems that include but are not limited to the following: bacteria transformed with bacteriophage DNA, plasmid DNA, or cosmid DNA; microorganisms such as yeast containing yeast vectors; mammalian cell systems infected with virus (eg, vaccinia virus, adenovirus, etc.); insect cell systems infected with viruses (eg, baculovirus); and plant cells infected by bacteria. The expression elements of these vectors vary in their resistance and specificities. Depending on the host-vector system used, any of a number of suitable transcription and translation elements may 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 DNA is dependent on the presence of a promoter, which is a DNA sequence that directs the binding of RNA polymerase and thereby promotes the synthesis of mRNA. The DNA sequences of the eukaryotic promoters differ from those of the prokaryotic promoters. In addition, eukaryotic promoters and accompanying genetic signals can not be recognized, or can not function, in a prokaryotic system, and, in addition, prokaryotic promoters are not recognized if they do not work in eukaryotic cells. Similarly, the translation of mRNA into prokaryotes depends on the presence of the appropriate prokaryotic 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 codes for the amino-terminal methionine of the protein. SD sequences are complementary to the 3 'end of 16S rRNA (ribosomal RNA) and probably promote the binding of mRNA to ribosomes, by duplication with rRNA, to allow correct ribosome placement. For a review on the maximization of gene expression, see Roberts and Lauer, Methods in Enzymology, 68: 473 (1979), which is incorporated by reference herein. The promoters vary in their "resistance" (for example, their ability to promote transcription). For purposes of expressing a cloned gene, it is desirable to use strong promoters in order to obtain a high level of transcription and, therefore, expression of the gene. Depending on the system of the host cell used, any of a number of suitable promoters may be used. For example, when they are cloned into E. coli, their bacteriophages or plasmids, promoters such as the phage T7 promoter, the l ac promoter, the trp promoter, the recA promoter, the ribosomal RNA promoter, the PR promoters and PL lambda coliphage and others, including but not limited to lacUV5, ompF, bla, lpp, and the like, can be used to direct high levels of transcription of adjacent DNA segments. In addition, a trp-JacUVS hybrid promoter (tac) or other E. coli promoters produced by recombinant DNA or other synthetic DNA techniques can be used to provide transcription of the inserted gene. Bacterial host cell strains and expression vectors can be chosen, which inhibit the action of the promoter, unless specifically induced. In certain operations, the addition of specific inductors is necessary for the efficient transcription of the inserted DNA. For example, the l ac operon is induced by the addition of lactose or IPTG (isopropylthio-beta-D-galactoside). A variety of other operons, such as trp, pro, etc., are under different controls. Specific start signals are also required for efficient transcription and translation of the gene in prokaryotic cells. These signals of transcription and translation initiation may vary in "resistance" as measured by the amount of the specific messenger RNA of the gene, and the protein synthesized, respectively. The DNA expression vector, which contains a promoter, can also contain any combination of various "strong" start transcription and / or translation signals. For example, efficient translation in E. coli requires a Shine-Dalgarno (SD) sequence of approximately 7-9 bases, 5 'to the start codon (ATG) to provide a ribosome binding site. In this way, any combination of SD-ATG that can be used by the ribosomes of the host cell can be used. Such combinations include, but are not limited to, the SD-ATG combination from the ero gene or the N gene of the lambda coliphage, or from the E, D, C, B or A genes of E. coli tryptophan. Also, any combination of SD-ATG produced by the AD? Recombinant or other techniques that involve the incorporation of synthetic nucleotides, can be used. Once the AD molecule? Isolated that encodes the protein or polypeptide promoter of the hypersensitive response, has been cloned into an expression system, it is ready to be incorporated into a host cell. Such incorporation can be carried out by various forms of the aforementioned transformation, depending on the vector / host cell system. The host cells include, but are not limited to, bacteria, viruses, yeast, mammalian cells, insect cells, plant cells and the like. The method of the present invention can be used to treat a wide variety of plants, to impart resistance against pathogens. Suitable plants include dicotyledons and monocotyledons.

More particularly, useful crop plants may include: rice, wheat, barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, bean, peas, chicory, lettuce, endives, cabbage, cauliflower, broccoli, turnip, radish , spinach, onion, garlic, eggplant, pepper, celery, carrot, squash, pumpkins, courgettes, cucumber, apple, pear, melon, strawberry, grape, raspberry, pineapple, soybeans, tobacco, tomato, sorghum and sugarcane . Examples of suitable ornamental plants are: Arabidopsis thaliana, Sain tpa uli a, petunia, pelargonium, fire flower, chrysanthemum, carnation and zinia. The method for imparting pathogen resistance to plants according to the present invention is useful for imparting resistance to a wide variety of pathogens, including viruses, bacteria and fungi. Resistance, among others, to the following viruses, can be achieved by the method of the present invention: tobacco mosaic virus and tomato mosaic virus. The resistance, among others, to the following bacteria, can also be imparted to the plants according to the present invention: Pseudomonas so-Zancearmp, Pseudomonas syringae pv. Tabaci, and Xanthamonas campestris pv. pelargonii. The plants can be made resistant, inter alia, to the following fungi, by using the method of the present invention: Fusari um oxy sporum and Phytoph thora infestans. The method of the present invention can be carried out through a variety of methods for the application of the hypersensitive response promoter protein or polypeptide to all or part of the plant being treated. This may involve (but not necessarily) the infiltration of the hypersensitive response promoter protein or polypeptide into the plant. Suitable application methods include high or low pressure spraying, injection, and sheet abrasion, close to when the promoter application takes place. Other suitable methods of application may be considered by those skilled in the art, with the proviso that they are capable of effecting contact of the hypersensitive response promoter protein or polypeptide with the cells of the plant. The hypersensitive response promoter protein or polypeptide can be applied in plants according to the present invention, alone or in a mixture with other materials.

One aspect of the present invention involves a composition for imparting resistance against pathogens to plants that contain a hypersensitive response promoter protein or polypeptide in a promoter. Suitable carriers include water or aqueous solutions. In this embodiment, the composition contains more than 500 nM of hypersensitive response promoter protein or polypeptide.

Although not required, this composition may contain additional additives including fertilizers, insecticides, fungicides, and mixtures thereof. Suitable fertilizers include (NH4) 2NO < . An example of a suitable insecticide is Malathion Useful fungicides include Captan.

Other suitable additives include damping agents, wetting agents, and abrasion agents. These materials can be used to facilitate the process of the present invention.

EXAMPLES Example 1 - Resistance induced by Harpina to Tomato, against the Disease of the Bacterial Wilt of the South (Pseudomonas solanacearum) Two-week-old tomato seedlings, grown in 8 x 15 cm containers in the greenhouse, were treated as follows: 20 plants were used for each of the six treatments, which were designated A through F, and described as follows: A) Approximately 100 μl of a crude harpina preparation at 200 μg / ml (for example, the protein or hypersensitive response promoter polypeptide) (ZM Wei, "Harpin, Elicitor of the hypersensitive Response Produced by the Plant Pathogen Erwinia amyl ovora ", Science 257: 85-88 (1992), which is incorporated by reference herein) was infiltrated within the lowest true leaf of each of the seedlings.

B) The same preparation of harpina that is used in (A), was sprayed with 400 mesh carborundum on the surface of the leaf of the seedlings, and then rubbed gently with the thumb.

C) E. coli DH5 (pCPP430) was developed (see Figure 1 for the plasmid vector map pCPP430) in LB medium at a D062o = 0.7. The culture was centrifuged and then resuspended in 5 nM potassium phosphate buffer, pH 6.5. Approximately 100 μl of the cell suspension infiltrated each leaf of the seedlings. D) E.coli DH5 (pCPP430:: hrpfiT) was used (see Figure 1 for the map of the plasmid vector pCPP430:: hrpN) as in (C). The cells were developed, and the suspension and the amount of inoculum used were the same as described in (C).

E) For E. coli DH5 (pCPP9) (see Figure 2), the cells were developed and the suspension and the amount of inoculum used were the same as described in (C). F) The infiltration of leaves with 5 mM potassium buffer was as described in (C).

The pathogenic challenge bacteria, Pseudomonas solanacearum strain K60, was developed in King B medium at a D062o = 0.7 (approximately 108 cfu / ml). The culture was centrifuged and resuspended in 100 volumes of 5 mM potassium phosphate buffer, to a final concentration of 1 x 106 cfu / ml. Three days later the tomato seedlings were treated with harpina or bacteria, these were unearthed and approximately one centimeter of the roots was cut with scissors. The seedlings were then immersed in the suspension of P. solanacearum K60 for 3 minutes. The inoculated plants were replanted in the same pots. The plants were left in a greenhouse, and the incidence of the disease was recorded 7 days after the inoculation.

A. Effect of harpina treatment After 24 hours, only those portions of leaves that had been infiltrated with harpina or E. coli DH5 (pCPP430) had become detached. The leaves sprayed with harpina and carborundum showed only dotted necrosis.

B. Effect of harpina treatment on the development of Southern Bacterial Wilt None of the 20 plants infiltrated with harpina showed any symptoms one week after inoculation with P. sol anacearum K60 (Table 1). One of the 20 seedlings showed symptoms of atrophy. Treatment with E. coli DH5 (cPP430-) (a mutant induced by transposon unable to promote hypersensitive collapse) or E. coli (pCPP9) showed no significant difference compared to plants treated with buffer. These results suggest that harpina or E. coli DH5 (pCPP430"), which produces harpina, induced resistance in tomato plants for the bacterial wilt of the south caused by P. solanacearum K60.

Table 1. Incidence of tomato seedling disease 7 and 14 after inoculation with P. sol anacearum K60.

Number of Plants Day 7 Day 14 Healthy Atrophied Healthy Atrophied A. Infiltration with 0 20 2 18 Harpina B. Dew of harpina 1 19 3 17 C. E. coli DH5 2 18 3 17 (pCPP430) D. E. coli DH5 16 13 (pCPP430 ~) E. E. coli DH5 15 6 + 1 se 13 (pCPP9) wilted F. Shock absorber 13 8 + 1 wilted 11 Non-pathogenic 20 0 20 Four weeks after the inoculation, the plants treated with the harpina or E. coli DH5 (pCPP430) were higher and broader compared to those treated with buffer. The average heights of the 10 plants that had been infiltrated with harpina or buffer are given in Table 2.

Table 2. Height (cm) of tomato plants four weeks after inoculation with Pseudomonas sol anacearum K60, after treatment with harpina or the buffer.

Infiltrate with Infiltrate with Harpina Infiltrate with Shock Absorber Inoculated with K60 Inocule Shock Inoculate with K60 36 32 11 41 29 21 35 38 33 34 35 12 39 37 15 35 33 32 36 22 25 35 35 15 41 40 37 37 29 38 Average 36.9 33 23.9 Example 2 - Resistance of the Tomato, induced by Harpina against the Disease of the Bacterial Wilt of the South, by Psßudomonas solancearum All methods used for infiltration and inoculation were the same as described in Example 1, except that the concentration of P. solanacearum K60 was approximately 5 x 104 cfu / ml. Plants infiltrated by buffer showed symptoms 15 days after inoculation with P. sol anacerarum K60. Six of 20 plants showed symptoms of atrophy after 15 days; 2 plants withered after 21 days. Wilted plants died sooner or later. However, none of the 20 plants treated with harpina showed symptoms of atrophy. Three weeks after the inoculation, 3 of the 20 plants treated with harpina showed symptoms of atrophy. It is possible that after three weeks, the plants may have lost their induced resistance. As in the first experiment, the full circumference and the heights of the plants treated with harpina were greater than those treated with buffer.

Example 3 - Resistance of the Tomato, induced by Harpina against the Disease of the Bacterial Wilt of the South, by Pseudomonas solanacearum This experiment was similar to Example 1, except that an additional inoculum of Pseudomonas solanacearum K60 was added to the pots containing the treated tomato plants. Harpina was infiltrated into two-week-old tomato seedlings. Two panels of each plant were infiltrated with approximately 200 μl of harpina suspended in 5 mM potassium phosphate buffer, at the concentration of approximately 200 μg / ml. A total of 20 tomato seedlings were infiltrated. The same number of tomato seedlings were infiltrated with buffer. After two days, the plants were inoculated with Pseudomonas solanacearum K60 by root immersion. Plants infiltrated with harpina or buffer were extracted from the soil mix and small amounts of roots were cut with scissors, and then the remaining roots were submerged in a suspension of P. Solanacearum K60 for three minutes. The concentration of the bacterial cell suspension was approximately 5 x 108 cfu / ml. The seedlings were replanted in the same pot. An additional 3 ml of bacterial suspension was added to the soil of each individual pot of 10 cm diameter (4 inches). The incidence of the disease was rated after one week. All the experiments were performed in the greenhouse with limited temperature control. After three weeks, 11 of the 20 tomato plants infiltrated with buffer, had died, and two plants that had withered recovered, but remained severely atrophied. Only 4 plants were grown normally compared to non-inoculated tomatoes. However, 15 of the plants inoculated with harpina seemed healthy; three plants were atrophied and two plants withered three weeks after inoculation. These results are summarized in Table 3 below.

Table 3. Resistance of the tomato, induced by harpina, against the bacterial wilt disease caused by P. solanacearum Weeks After Inoculation Treatment 1 2 3 Healthy Harpina 20 17 15 Withering 0 1 2 Atrophied 0 2 3 Healthy Shock Absorber 8 5 4 Withered 8 12 13 Atrophied 4 3 3 Example 4 - Resistance of Tobacco, induced by Harpina, against the Tobacco Mosaic Virus A panel of a lower leaf tobacco seedling of four weeks of age (culture, Xanthi, with the N gene) was infiltrated with E. amylovora harpina at the concentration of 200 μg / ml. After three days, the plants were treated with tobacco mosaic virus ("TMV"). Two concentrations of the viruses (5 μg and 100 μg / ml) were used. Approximately 50 μl of the viral suspension was deposited on an upper leaf of the tobacco. The leaf was powdered with 400 mesh carborundum and the leaves were gently rubbed. Each concentration was tested on three plants. The necrotic lesions were counted 4 days after the inoculation and in two subsequent days, and the average number is reported on three sheets (Table 4). It was difficult to distinguish the individual lesions by day 10, because some of the necrotic lesions had merged. Therefore, the number of recorded lesions seemed smaller than that recorded on day 7. The size of the necrotic lesions on the leaves treated with buffer, was much larger than the leaves treated with harpina.

Table 4. Resistance of tobacco, induced by harpina, against TMV from inoculation with 5 μg / ml of virus Average Number of Injuries / Treatment Sheet Day 4 Day 7 Day 10 Harpina 21 32 35 Shock Absorber 67 102 76 There was no significant difference in the number of local lesions that developed on tobacco treated with harpina and treated with buffer, when the concentration of the tobacco mosaic virus inoculum was 100 μg / ml.

Example 5 - Resistance of the Tomato, induced by Harpina, against the Fusarium Wilt Disease Six-week-old tomato plants were treated with harpina as described for Example 3. The fungal pathogen Fusari um oxysporum was developed on Lima bean agar medium for 5 days at 27 ° C. Two agar plates complete with mycelia were mixed for 2 minutes in 20 ml of 5 mM potassium phosphate buffer. The roots of the tomato plants treated with harpina or shock absorber were wounded when a wooden stake was buried inside the soil of the pots. Subsequently, 3 ml of the mushroom suspension was emptied into the soil of each 10 cm (4 inch) pot. The inoculated plants remained in a controlled environment chamber at 24 ° C with 16 hours of light per day. The incidence of the disease was recorded 7 days after the inoculation. Each treatment was applied to 10 plants. The results are shown in Table 5 below.

Table 5. Effect of harpina treatment or buffer on the Fusarium wilt disease of tomato Number of plants (out of 10) that show wilting symptoms at the time of post-inoculation indicated Treatment Day 7 Day 10 Day 15 Day 20 Harpina 1 2 4 4 (1 died) Shock absorber 3 6 7 7 (4 died) Example 6 - Resistance of Tobacco, induced by Harpina, against the Wildfire Disease (Pseudomonas syr ± ngae pv. Tabaci) Harpina was infiltrated within simple panels of the lower leaves of tobacco plants of 4 weeks of age (20 cm high). After three days, the suspensions of Pseudomonas syringae pv. Tabaci were infiltrated in simple panels of upper leaves. Four days later, the incidence of the disease was recorded, as described in Table 6.

Table 6. Symptoms of infection by Wildfire disease in tobacco leaves inoculated with Pseudomonas syringae pv. tabaci after the treatment of the lower leaves with harpina Concentration of P. s. tabaci Treated with harpina Not treated with harpina 104 cfu / ml without symptoms necrosis and soaking with water 105 cfu / ml without symptoms necrosis and soaking with water 106 cfu / ml without symptoms necrosis and soaking with water 107 cfu / ml without symptoms necrosis and soaking with water 10 u cfu / ml Necrosis necrosis and soaking with water Example 7 - Resistance induced by Harpina of Geranium (Pelargoniuro hortorum) against the Bacterial Stain on Leaves (Xanthamonas campestris pv, pelargonii) This experiment was performed with geranium root cuttings that were grown in individual pots of 10 cm (4 inches) or 15 cm (6 inches) in a mixture of artificial soil in a greenhouse. Two lower leaves on each plant were infiltrated either with 0.05 M potassium phosphate buffer, pH 6.5 (control), or harpina or a suspension of Escherichia coli DH5 (pCPP430) (the cloned hrp gene cluster, complete with E. amyl ovora). Two to seven days after the infiltration, all the plants were inoculated with a pure culture of the bacterial pathogen of the leaves, Xanthamonas campestri s pv. Pelargoni i. A suspension of the bacteria (5 x 106 cfu / ml) was atomized on the upper and lower surfaces of the leaves of the plants, at low pressure. Each treatment was applied to two plants (designated "A" and "B" in Table 7). The plants were kept in a closed chamber for 48 hours with supplementary nebulization supplied by cold mist nebulizers. Subsequently, the plants were kept on the greenhouse bench subject to environmental humidity and at a temperature of 23 ° C to 32 ° C for 10 days before the development of the disease was evaluated.

Table 7. Effect of harpina and the hrp gene cluster from Erwini to amyl ovora, on the development of bacterial leaf spot, geranium Time between treatment and inoculation with Xanthomonas campestris pv. Pelargonii Treatment 7 Days 5 Days 4 Days 3 Days 2 Days Plant Plant Plant Plant Plant A B A B A B A .B A B Shock absorber Harpina 0 0 NT NT 0 H5 (pCPP430) * The numbers in the table are the number of leaves showing symptoms of the disease (pronounced necrosis, chlorosis or wilting) 10 days after inoculation.

Example 8 - Activity of several harpinas in the induction of resistance to Wildfire Disease, caused by Pseudomonas syringae pv. tabaci Tobacco plants (Ni cotiana tabacum var Xanthi) were developed in the greenhouse. At 4 weeks of age, the harpina preparations were infiltrated into a simple panel of two lower leaves of each plant. Twelve plants were treated with each harpina preparation, and three were treated with the same potassium phosphate buffer that was used to prepare the harpinas. The hypersensitive necrosis developed within 24 hours in the panels of the leaves infiltrated with the harpina preparations, but not with the buffer. At 7, 10, 11 and 12 days after the treatment with harpina, all the plants were inoculated with suspensions of 104 to 106 cells / ml of Pseudomonas syringae pv. Tabaci through the infiltration of panels on the upper leaves. The plants were incubated in the greenhouse for 7 days before the development of the disease was evaluated. The results are tabulated as follows in Table 8: Harpina source Days between treatment and inoculation 12 11 10 _7 log [Inoc.] 4 5 6 4 5 6 4 5 6 4 5 6 None + + + + + + + + + + + + + + + + (shock absorber) P. syringae - - + - - + - - + - - + Harpina source Dias between treatment and inoculation 12 11 10 _7 log [Inoc] 4 5 6 4 5 6 4 5 6 4 5 6 E. chrysanthemi - - + - - + - - + - - + E. amylovora - - + _ _ _ _ _ + _ _ + - = No symptoms + = Necrosis with yellow halo, typical of wildfire disease ++ = Severe necrosis with yellow halo, typical of wildfire disease The results indicate that the harpina preparations from the three bacteria are effective in inducing resistance to the wildfire pathogen. The plants treated with either harpina showed no symptoms with the two minor inoculum concentrations used. At the highest concentration, the symptoms were more severe on the plants treated with buffer than on the plants treated with harpina.

Example 9 - Resistance induced by Harpina against Late Rolla Disease caused by Phytophthora infestans The pathogen of late rolla affects potatoes and tomatoes mainly. This is responsible for the famous famine of the Irish popes. The activity of harpina in the induction of resistance to this pathogen was tested on tomato seedlings developed in the greenhouse. The three-week-old seedlings ('Mama Mia' culture of approximately 15.2 to 20.3 cm (6 to 8 inches) in height) were treated with harpina, and subsequently inoculated with Phythoph thora infestans. Two panels of a lower leaf of each plant were infiltrated with a solution of harpina, a suspension of Escheri chia coli DH5 (pCPP430), which produces and secretes harpina, or potassium phosphate buffer.

Two, three or four days after the infiltration, the plants were inoculated with a mycelial suspension of Phythoph thora infestans. The strain U.S. 7 was used, which is highly virulent for tomato. The mycelial suspension was carried out by gently mixing the contents of two plates of barley flour agar on and in which the fungus had developed for 2 weeks at 21 ° C. The suspension was brushed on the upper part and the lower parts of one leaf per treated plant, with a wide brush for artistic painting.

The treated and inoculated plants were incubated in a specially constructed fog chamber, designed to maintain a temperature of 20-23 ° C in the greenhouse, while maintaining high relative humidity. Humidity was provided by several cold fog nebulizers, operating at full speed over purified water. The incidence of the disease was evaluated 13 days after inoculation with Phytoph thora infestans, and the results are shown in Table 9. Each treatment was applied to four individual plants.

Table 9. Late roll lesion numbers, which were present on tomato leaves 13 days after inoculation Treatment Days between treatment and inoculation 4 3 2 Floor A B C D A B C D A B C D Shock absorber 3 2 0 0 1 2 2 0 0 0 4 1 Harpina 0 0 1 0 0 0 0 1 2 1 0 0 DH5 (pCPP430) 0 0 0 1 0 2 2 1 0 1 1 0 Harpin treatment reduced the number of lesions that developed in the plants at all intervals between treatment and inoculation. The number of late rolla lesions that developed was also reduced by the previous treatment with DH5 (pCPP430), which produces and secretes harpina. Although the invention has been described in detail for purposes of illustration, it is understood that such detail is solely for that purpose, and variations may be made therein by those skilled in the art, without departing from the spirit and scope of the invention, the which is defined by the following claims.

LIST OF SEQUENCES GENERAL INFORMATION: i) APPLICANT: Cornell Research Foundation, Inc., ii) TITLE OF THE INVENTION: INDUCED RESISTANCE OF HYPERSENSITIVE RESPONSE IN PLANTS iii) NUMBER OF SEQUENCES: 9 iv) DOMICILE FOR CORRESPONDENCE: A) RECIPIENT: Nixon, Hargrave, Devans &; Doyle LLP B) STREET: Clinton Square, P.O. Box 1051 C) CITY: Rochester D) STATE: New York E) COUNTRY: E.U.A. F) POSTAL CODE: 14603 v) COMPUTER LEGIBLE FORM: A) TYPE OF MEDIUM: Flexible disk B) COMPUTER: PC compatible with IBM C) OPERATING SYSTEM: PC-DOS / MS-DOS D) SOFTWARE: Patentln Relay # 1.0, Version # 1.30 vi) DATA OF THE CURRENT APPLICATION: A) NUMBER OF THE APPLICATION: B) DATE OF PRESENTATION: C) CLASSIFICATION: vii) DATA OF THE PREVIOUS APPLICATION: A) NUMBER OF THE APPLICATION: US 08 / 475,775 B) DATE OF SUBMISSION: 07-JUNIO-1995 viii) ATTORNEY / AGENT INFORMATION: A) NAME: Goldman, Michael L. B) REGISTRATION NUMBER: 30,727 C) REFERENCE NUMBER / CASE: 19603/10051 ix) INFORMATION FOR TELECOMMUNICATIONS A) TELEPHONE: (716) 263-1304 B) TELEFAX: (716) 263-1600 INFORMATION FOR THE SEQUENCE: SEQ ID No. 1: i) CHARACTERISTICS OF THE SEQUENCE: A) LENGTH: 338 amino acids B) TYPE: amino acid C) TYPE OF HEBRA: D) TOPOLOGY: linear ii) TYPE OF MOLECULE: protein xi) DESCRIPTION OF THE SEQUENCE: SEQ ID No. 1: Mee Gln He Thr He Lyß Ala Kiß He Gly Gly Asp Leu Gly Val Ser 1 5 10 15 Gly Leu Gly Wing Gln Gly Leu Lyß Gly Leu Asn Wing Wing Being Ser 20 25 30 Leu Gly Ser Ser Val Aßp Lyß Leu Ser Ser Thr? e Asp Lys Leu Thr 35 40 45 Be Ala Leu Thr Ser Met Mee Phe Gly Gly Ala Leu Ala Gln Gly Leu 50 55 60 Gly Ala Ser Ser Lys Gly Leu Gly Met Ser Asn Gln Leu Gly Gln Ser 65 70 75 80 Phe Gly Aßn Gly Wing Gln Gly Wing Being Aßn Leu Leu Ser Val Pro Lyß 85 90 95 Being Gly Gly Aßp Ala Leu Being Lyß Met Phe Aßp Lyß Ala Leu Aßp Asp 100 105 not Leu Leu Gly Hiß Aßp Thr Val Thr Lya Leu Thr Asn Gln Ser Asn Gln 1X5 120 125 Leu Ala Aßn Ser Met Leu Aßn Ala Be Gln Met Thr Gln Gly Asn Met 130 135 140 Aßn Ala Phe Gly Ser Gly Val Aßn Aßn Ala Leu Ser Ser He Leu Gly 145 150 155 160 Aßn Gly Leu Gly Gln Ser Met Ser Gly Phß Ser Gln Pro Ser Leu Gly 165 _ 170 175 Wing Gly Gly Leu Gln Gly Leu Ser Gly Wing Gly Wing Phe Asn Gln Leu 180 185 190 Gly Aßn Wing He Gly Met Gly Val Gly Gln Aßn Wing Wing Leu Wing 195 200 205 Leu Ser Aßn Val Ser Thr Hiß Val Aßp Gly Asn Asn Arg His Phe Val 210 215 220 Asp Lyß Glu Aßp Arg Gly Met Ala Lyß Glu He Gly Gln Phß Met Asp 225 230 235 240 Gln Tyr Pro Glu He Phß Gly Lyß Pro Glu Tyr Gln Lyß Aßp Gly Trp 245 250 255 Be Ser Pro Lyß Thr Aßp Aßp Lyß Ser Trp? The Lyß Ala Leu Ser Lyß 260 265 270 Pro Aßp Aßp Aßp Gly Met Thr Gly Ala Met Met Aßp Lyß Phe Arg Oln 275 280 285 Ala Met Gly Met He Lyß Ser Ala Ala Ala Ala Aßp Thr Gly Asn Thr 290 295 300 Aßn Leu Aßn Leu Arg Gly Wing Gly Gly? The Ser Leu Oly He Aßp Wing 305 310 315 320 Wing Val Val Gly Aßp Lyß He Wing Asn Met Ser Leu Gly Lyß Leu Wing 325 330 335 INFORMATION FOR THE SEQUENCE: SEQ ID No. 2: i) CHARACTERISTICS OF THE SEQUENCE: A) LENGTH: 2141 base pairs B) TYPE: nucleic acid C) TYPE OF HEBRA: simple D) TOPOLOGY: linear ii) TYPE OF MOLECULE: DNA (genomic) xi) DESCRIPTION OF THE SEQUENCE: SEQ ID No. 2: CGATTTTACC CGGGTGAACG TGCTATGACC GACAGCATCA CGGTATTCGA CACCGTTACO 60 GCOTTTATGG CCGCGATGAA CCGGCATCAG GCGOCGCGCT GGTCGCCGCA ATCCGGCGTC 120 GATCTGGTAT TTCAGTTTGG GGACACCGGG CGTGAACTCA TGATGCAGAT TCAGCCGGGG 180 CAOCAATATC CCGGCATGTT GCGCACGCTG CTCGCTCGTC GTTATCAGCA GGCGGCAGAG 240 TGCOATGGCT GCCATCTGTG CCTGAACGGC AGCGATGTAT TGATCCTCTG GTGGCCGCTG 300 CCGTCGGATC CCGGCAGTT? TCCGCAGGTG ATCGAACGTT TGTTTGAACT GGCGGGAATG 360 ACGTTGCCGT CGCTATCCAT AGCACCGACG OCGCGTCCGC AGACAGGGAA CGGACGCGCC 420 CGATCATTAA GATAAAGGCG OCTTTTTTTA TTGCAAAACG GTAACssTGA GGAACCGTTT 480 CACCGTCGGC GTCACTCAGT AACAAGTATC CATCATGATG CCTACATCGG GATCGGCGTO 540 GGCATCCGTT GCAGATACTT TTGCGAACAC CTGACATGAA TGAGGAAACG AAATTATGCA 600 AATTACGATC AAAGCGCACA TCGGCGGTGA TTTGGGCGTC TCCGGTCTGG GGCTGGGTGC 660 TCAGGGACTG AAAGGACTGA ATTCCGCGGC TTCATCGCTG GGTTCCAGCG TGGATAAACT 720 OAGCAGCACC ATCOATAAOT TGACCTCCGC GCTGACTTCG ATGATGTTTG GCOGCGCGCT 780 OGCOCAOGGG CTGGGCGCCA GCTCGAAGGG GCTGGGGATG AGCAATCAAC TGGGCCAGTC 840 TTTCGGCAAT GGCGCGCAGO OTGCGAGCAA CCTGCTATCC GTACCGAAAT CCGGCGGCGA 900 TGCOTTGTCA AAAATsTTTs ATAAAGCGCT OGACGATCTG CTGGGTCATG ACACCGTGAC 960 CAAOCTGACT AACCAGAGCA ACCAACTGGC TAATTCAATG CTGAACGCCA GCCAGATGAC 1020 CCAOOGT ?? T? TG ?? TGCGT TCGGC? GCGG TGTGAACAAC GCACTGTCGT CCATTCTCGO 1080 C? CGGTCTC GGCC? GTCG? TGAGTGGCTT CTCTCAGCCT TCTCTGGGGG CAGGCGGCTT 1140 GCAGGGCCTG AGCGGCGCGG GTGCATTCAA CCAGTTGGGT AATGCCATCG GCATGGGCGT 1200 GGGGCAG ?? T GCTGCGCTG? GTGCGTTGAG TAACGTCAGC ACCCACGTAG ACGGTAACAA 1260 CCsCCACTTT GTAG? T ??? G AAGATCGCGG CATGGCGAAA GAGATCGGCC AGTTTATGGA 1320 TC? GT? TCCG G ?? TATTCO OTAA? CCOG? ATACC? GAAA GATGOCTGG? GTTCGCCGA? 1380 G? CGG? CGAC AAATCCTOOG CTAAAGCGCT GAGTAAACCG GATG? TG? CO GT? TG? CCGO 1440 CGCC? GCATG GAC? ATTCC GTCAGGCGAT GGGTATGATC A ??? GCGCGs TGGCGGGTG? 1500 T? CCGGCAAT ACCAACCTG? ? CCTGCGTGG CGCOOGCGGT GCATCGCTGG GTATCG? TGC 1560 GGCTGTCGTC GGCG? T ???? T? GCCA? C? T GTCGCTGGGT? AGCTGGCCA ACGCCTGATA 1620? TCTGTGCTG GCCTG? TA ?? GCGG? AACGA? AAAAG? G? C GGGGAAGCCT GTCTCTTTTC 1680 TTATT? TGCG GTTT? TGCGG TT? CCTGG? C CGGTT? ATCA TCGTCATCGA TCTGGTACA? 1740? CGC? C? TTT TCCCGTTC? T TCGCGTCGTT? CGCGCC? CA ATCGCG? TGG CATCTTCCTC 1800 OTCGCTCAGA TTscsCGGCT G? TGGGG ?? C GCCGGGTGG? ? T? T? GAGAA ACTCGCCGGC 1860 CAG? TGG? G? C? CGTCTGCG? T ??? TCTGT GCCGT? ACGT GTTTCTATCC GCCCCTT? G 1920 C? G? T? G? TT GCGGTTTCOT ?? TC ?? C? TG GT ?? TGCGGT TCCGCCTGTG CGCCGGCCGG 1980 G? TC? CC? C? T? TTC? T? G ??? GCTGTCT TGCACCTACC GT? TCGCGGG AG? TACCG? C 2040 AAAAT? GGGC AGTTTTTGGT TGGT? TCCGT GGGGTGTTCC GGCCTG? CAA TCTTGAGTTG 2100 GTTCGTC? TC? TCTTTCTCC? TCTGGGCG? CCTG? TCGGT T 2141 INFORMATION FOR THE SEQUENCE: SEQ ID No. 3: i) CHARACTERISTICS OF THE SEQUENCE: A) LENGTH: 385 amino acids B) TYPE: amino acid C) TYPE OF HEBRA: D) TOPOLOGY: linear ii) TYPE OF MOLECULE: protein xi) DESCRIPTION OF THE SEQUENCE: SEQ ID No. 3: Met Ser Leu? ßn Thr Ser Oly Leu Gly? The Ser Thr Met Gln He Ser 1 5 10 as He Gly Oly? The Oly Oly? ßn? ßn Gly Leu Leu Gly Thr Ser? Rg Gln 20 25 30? ßn? The Gly Leu Oly Gly? Sn Ser? The Leu Gly Leu Gly Gly Gly? Sn 35 40 45 Oln? Sn? ßp Thr Val? ßn Gln Leu? The Gly Leu Leu Thr Gly M? T Met 50 55 60 Met Met M? T Ser M? T Met Oly Oly Gly Oly Leu Met Oly Oly Gly Leu 65 70 75 80 Gly Gly Gly Leu Gly? ßn Gly Leu Gly Gly Gly Gly Leu Gly Glu 85 90 95 Gly Leu Ser? ßn? The Leu? ßn? ßp Met Leu Gly Gly Ser Leu? Sn Thr 100 105 110 Leu Gly Ser Lyß Gly Gly? ßn? Sn Thr Thr Ser Thr Thr? Sn Ser Pro 115 120 125 Leu? Sp Gln The Leu Gly He? sn Ser Thr Ser Gln? sn? sp? sp Ser 130 135 140 Thr Ser Gly Thr? sp Ser Thr Ser? ßp Ser Ser? sp Pro Met Gln Qln 145 150 155 160 Leu Leu Lyß Met Phe Ser Glu He Met Gln Ser Leu Phe Gly? Sp Oly 165 170 175 Gln? ßp Gly Thr Oln Oly Ser Being Oly Oly Lyß Gln Pro Thr Qlu 180 1T5 190 Gly Glu Gln? ßn? The Tyr Lyß Lyß Gly Val Thr? Sp Ala Leu Ser ßly 195 200 205 Leu Met ßly and Aan Gly Leu- Ser Oln Leu Leu Gly? Sn Oly Gly Leu Oly 210 215 220 Gly Gly Oln Oly Oly? ßn? The Gly Thr Gly Leu? Sp Gly Ser Ser Leu 225 230 235 240 Oly Oly Lyß Oly Leu Gln? ßn Leu Ser Gly Pro Val Asp Tyr Gln Oln 245 250 255 Leu Oly Aßn? The Val Gly Thr Gly He Oly Met Lyß? The Gly He ßln 260 265 27? The Leu? ßn? ßp He Gly Thr Kiß? Rg Hiß Ser Ser Thr? Rg Ser Ph? 275 280 285 Val? ßn Lyß Gly ? ßp? rg? the Met? the Lyß Glu He Gly oln Phe Met 290 295 300? ßp Oln Tyr Pro Olu Val Ph? Oly Ly? Pro Oln Tyr Ol? Ly? Oly Pro 305 310 315 320 Oly Oln Glu Val Lys Thr? ßp? ßp Lys Ser Trp? The Lys? The Leu Ser 325 330 335 Lyß Pro? ßp? ßp? ßp Gly Met Thr Pro? The Ser Met Glu Gln Phe? ßn 340 345 350 Lyß? The Lyß Oly Mßt He Lyß? Rg Pro Met? The Gly? Sp Thr Gly? ßn 355 360 365 Gly? ßn Leu Gln His? Val Val Val Leu? rg Trp Val Leu Met 370 375 380 Pro 385 INFORMATION FOR SEQUENCE: SEQ ID No. 4 i) SEQUENCE CHARACTERISTICS: A) LENGTH: 1158 base pairs B) TYPE : nucleic acid C) TYPE OF HEBRA: simple D) TOPOLOGY: linear ii) TI PO OF MOLECULE: DNA (genomic) xi) DESCRI PTION OF THE SEQUENCE: SEQ ID No.

ATOAOTTACA ATACAAOTOa OCTO8? ßCO TCAACOATOC AAATTTCTAT C00CQQ QO3 60 OOCOa? AATA ACOaOTTOCT ßOOTACCAOT COCCAOAATE CTQOQTTCWa TOOCAATTCT 130 OCACT88C T8OCOOO8 T ?? TC ???? T OATACCOTCA ATCAOCTOßC TOOCTTACTC 180 ACCOOCATOA TOATOATOAT OAOCATOATa aOCOQT8TO OaCTOATOOa COOTOOCTTA 240 QOCOOTOOCT TAOOTAAToa CTToosrooc TCAOOTOOCC ToaßcoAAOo ACTOTCOAAC 300 scscTOAAca ATATOTTAOO caspcacTQ AACACOCTOO ocrcaAAAOQ COOCAACAAT 3ßo ACCACTTCAA CAACAAATTC CCCOCTOOAC CAOOCOCTOQ QTATTAACTC AACOTCCCAA 420 AACOACOATT CCACCTO0QO CACAflATTCC ACCTCAOACT CCAOCOACCC ßATßCAßCAfl 480 crocTO? AQA TOTTCAOCO? OATAATOCAA AOCCTOTTTO oTOATqqcA AGATOOCACC 540 C? 8OCA tr CCTCTOOOOO CMOCMCOQ ACCOAAOOCO AaCAOAACOC CT? T ??? AAA 600 OOAOTCACTO ATOOOCTO C 8aCCTO? TO OOTAATOOTC TOAGCCAaCT CCTTOOCAAC 660 QosoaAcToa O? OOTOOTCA OOOOOOTAAT OCTOOCACOO otcttoAcoa ttcstcacro 720 aocoocAa? A ooc OCA ??? CCTOAOCOOO ccoerrsaACT? CC? QCAOTT AO TAACOCC 7ßo OTOOOTACCa sT? TCOOTAT aAAAOCOOOC ATTCAOOCOC TOAATO? TAT COOTACOCAC 840 AOOCACAOTT CAACCCOTTC TTTCOTCAAT ?? AOQCOATC GOOCOATOOC OAAOaAAATC 900 OOTCAOTTCA TOOACCAßTA TCCTOAOOTO TTrOOCAAOC CßCAOTACCA OAAAOOCCCO 960 OOTCAOß? OG TaAAA? C03A tS? C ??? TC? TsOOCA ??? a CACTOAOCAA OCCAOATGAC 1020 a? O8? TOA CACCAaCCAO TATOaAOCAO TTCAACA ?? a CCAAGOOCAT aATCAAAAOß 1080 CCCAT8C8 OTOATACOOQ CAACOOCAAC CTOCAOCAca caoTOCca r oattcttcac 1140 TOOTOPATHY TOCCATOA HSß i) CHARACTERISTICS OF THE SEQUENCE: A) LENGTH: 341 amino acids B) TYPE: amino acid C) TYPE OF HEBRA: D) TOPOLOGY: linear ii) TI PO OF MOLECULE: protein xi) DESCRITION OF THE SEQUENCE: SEQ ID Do not Met Oln Ser Leu Sar Leu? An Ser Ser Ser Leu Oln Thr Pro? La Met 1 S 10 15? The Lau Val Leu Val? Rg Pro Olu? The Olu Thr Thr Oly be Thr Ser 20 25 30 Ser Lya? The Leu Oln Olu Val Val Val Lya Lau? The Qlu Olu Leu Mat 35 40 45? Rg? an Oly Oln Lau Aßp? ap Sar Ser Pro Leu.Oly.Lya.Lau-Leu-? la. 50 55 60 Lya Sar Met? La? La? Ap Oly Lya? Oly Oly oly Xla Olu? Ap Val «5 70 75 80 Has the? The Leu? Ap Lya Lau Xla Hia Olu Lya Leu Oly? Ap Aan Pha 85 90 95 ßly? The Ser? La? Ap 8w? The Ser Oly Thr Oly Oln Oln? Ap Leu Met 100 105 110 Thr Oln Val Leu? An Oly Leu? The Lya Ser Met Leu? Ap? ßp Leu Leu 115 120 125 Thr Lya Oln? Ap Oly Oly Thr Ser Phe 8er Olu? Ap? Ap Met Pro Met 130 135 140 Leu? an Lya He? the Oln Phe Met? ßp? ßp? ßn Pro? the Qln Pha Pro 145 150 155 160 Lyß Pro? ßp Ser Oly Ser Trp Val Aßn Olu Leu Lyß Olu? Ap? An Pha 165 170 175 Leu? Ap Oly? Ap Olu Thr? La? The Ph? Rg? Ser? La Leu? Ap He He 180 165 190 Oly Oln Oln Leu Oly? ßn Oln Oln Ser? ßp? The Oly Sar Lau? La Oly 195 200 205 Thr Qly Oly Oly Oly Oly Thr Pro Ser Ser Pha Ser? An? ßn Sar Ser 210 215 220 Val Met Oly? A Pro Leu He A? P? La? ßn Thr Oly Pro Oly? ßp Ser 225 230 235 240 Oly? ßn Thr? Rg Oly Olu? The Oly Oln Leu He Oly Olu Leu He? ßp 245 250 255? Ra Oly Leu Oln Ser Val Leu? The Oly Qly Oly Lau Qly Thr Pro Val 260 «270? ßn Thr Pro Oln Thr Oly Thr Ser? La? An Oly Oly Qln Ser? La Qln 275 280 285? Ap Lau? Ap Qln Leu Qi Oly Oly Lau Lau Liu Qly Leu Qlu? 290 295 300 Thr Lau Lya? Ap? Oly Oln Thr Qly Thr? ßp Val Qln Ser Ser? La 305 310 315 320? Oln xla? Thr Leu Leu Val Ser Thr Leu Leu Qln Qly Thr? Rg 325 330 335? ßn Oln? La? La? INFORMATION FOR THE SEQUENCE: SEQ ID No. 6: i) CHARACTERISTICS OF THE SEQUENCE: A) LENGTH: 1026 base pairs B) TYPE: nucleic acid C) TYPE OF HEBRA: simple D) TOPOLOGY: linear ii) TYPE OF MOLECULE: DNA (genomic) i) DESCRIPTION OF THE SEQUENCE: SEQ ID No. 6: ATsCAßAßTC TCAOTCTTAA CAßCAOCTCO CTOCAAACCC CßOCAATOQC CCTTOTCCTO 60 CGAGACUTCCIO ?? co? ß? C OACTOOCAOT ACOTCOAOCA AOOCOCGTCA GOAAOTGOTC 120 OTOAAOCTOO OOQAOOAACT Q? TOOOC ?? T OOTCAACTCO? CO? CAOCTC OCC? TTOOOA 180 AAACTOTTsO CCAAOTCOAT OOCCOCAGAT OOCAAßOCOO OCOOCOOTAT TOAOSATOTC 240 ATCOCTOCsC TQO? C ?? QCT aATCCATOAA AAOCTCOQTO ACAACTTCOO CQOQTCTOCO 300 OACAOOOCCT COOOTACCOO AC? OC? AaAC CTOATOACTC AOOTOCTCAA TO0CCTO3CC 360 A? OTCO? TOC TCOATOATCT TCTOACCAAO CAOGATOOCO OO? C ?? OCTT CTCCOAAOAC 420 OATATOCCOA TOCTQA? C ?? OAT0QO0CAO TTCATOOATO ACAATCCCOC ACAOTTTCCC 480 AAOCCOQACT COOOCTCCTO OOTOAACOAA CTCAAOaAAß ACAACTTCCT TOATOßCaAC 540 a ??? COOCTO itfnXA.Wm OOCACTCOAC ATCATTOOCC AßCAACTOOß TAATCAOCAa 600 AOTOAOOCTO OCAOTCTOOC? AOO? OosoT aoAOQTCTßo OCACTCCOAO OUITTTTTCC ßßo A? CAACTOQT CCOTOATOOO TOATCCOCTQ ATCOACOCCA ATACCOOTCC CaaTOACAOC 720 OOCAATACCC OTOQTO ?? OC QOXWCAACTO ATCOOCOAOC TT? TCO? CCO TOsCCTOC ?? 780 TCOOTATTOQ CCOQTOOTOO? CTOOQC? C? CCCOTAAACA CCCOOCAO? C COOTACUTCO 840 oaiAATOßco or? C? OTCCoc TCAOOATCTT aATCAOTToc ToaacaocTT OCTOCTCAAO 900 OQCCT OAOO CAACOCTCAA OGLATOCCOOO CAAACAOOCA CCOACQTsC? OTOOMßCOCT 960 OCOCAAATCO CCACCTTOCT OßTCAOTACO CTOCTOCAAO OCACCCOCAA TCAOOCTOCA 1020 GTCCTGA 1026 ) INFORMATION FOR THE SEQUENCE: SEQ ID No. 7: i) CHARACTERISTICS OF THE SEQUENCE: A) LENGTH: 344 amino acids B) TYPE: amino acid C) TYPE OF HEBRA: D) TOPOLOGY: linear ii) TYPE OF MOLECULE: protein xi) DESCRIPTION OF THE SEQUENCE: SEQ ID No. 7: Met Ser Val Oly? ßn He Gln Ser Pro Ser? ßn Leu Pro Gly Leu Gln 1 5 10 15? ßn Leu? ßn Leu? ßn Thr? ßn Thr? Sn Ser Oln Oln Ser Gly Gln Ser 20 - 25 30 Val Gln? ßp Leu He Lyß Gln Val Glu Lys? ßp He Leu? ßn He He 35 40 45? The? Leu Val Gln Lyß? The? The Gln Ser? The Gly Gly? Sn Thr Gly 50 55 60? Sn Thr Gly? ßn? The Pro? La Ly?? P Gly? Sn? The? Sn? The Gly ? the 65 70 75 80? ßn? ßp Pro Ser Lyß? ßn? ßp Pro Ser Lys Ser Qln? the Pro Oln Ser 85 90 95? the? sn Lyß Thr Gly? sn Val? sp? ap? la? ßn? sn Gln Asp Pro Met 100 105 110 Gln Ala Leu Met Gln Leu Leu Glu Aap Leu Val Lyß Leu Leu Lyß? The 115 120 125? The Leu Hiß Met Gln Gln Pro Gly Gly Asn? Sp Lys Gly Asn Gly Val 130 13S 140 Gly Gly ? the? sn Gly Ala Lyß Gly? the Gly Gly Gln Gly Gly Leu? the 145 150 155 160 Glu? The Leu Gln Glu He Glu Gln He Leu? The Gln Leu Gly Gly Gly 165 170 175 Giy? The Gly? The Gly Gly? The Gly Gly Gly Val Gly Gly Wing Gly Gly 180 185 190 Wing? ßp Gly Cly Ser Cly Wing Gly Gly Wing Gly O and Wing Asn Gly Wing 195 2C0 205 Asp Gly Oly? ßn Oly Val ? ßn Gly? ßn Gln? la? sn Gly Pro G n Asn 210 215 220 Wing Gly Aßp Val Aßn Gly Wing Asn Gly Wing Aßp Aßp Gly Ser Glu Asp 225 230 235 240 Gln Gly Cly Leu Thr Gly Val Leu Gln Lys Leu Met Lys lie Leu Asn 245 250 255 Ala Leu Val Gln Met Met Oln Gln Gly Gly Leu Gly Gly Gly Asn Gln 2 (0 265 270 Wing Gln Gly Gly Ser / a Gly Wing Gly Asn Wing Pro Wing Ser Gly 275 280 285 Wing Aßr Pro Gly The Asn Glr Pro Gly Ser? La? ßp Asp Gln Ser Ser 293 295 300 Gly Gln Aßn Aßn Leu Gln Ser Gln He Met Aßp Val Val Lyß Glu Val 305 310 315 320 Val Gln He Leu Gln Gln Met Leu? La? Oln? ßn Gly Oly Ser Oln 325 330 335 ßln Ser Thr Ser Thr Gln Pro Met 340) 'INFORMATION FOR THE SEQUENCE: SEQ ID No. 8: i) CHARACTERISTICS OF THE SEQUENCE : A) LENGTH: 1035 base pairs B) TYPE: nucleic acid C) TYPE OF HEBRA: simple D) TOPOLOGY: l ineal ii) T MOLECULATION IPO: DNA (genomic) xi) SEQUENCE DESCRITION: SEQ ID No . 8:? TOTCAOTCG GA ?? CATCC? ß? GCCCGTCG ?? CCTCCCGO sTCTOC? G ?? CCTG? CCTC 60? AC? CC ?? CA CCAACAGCCA OCAATCGGGC CAGTCCGTGC ?? G? CCTG? T CAAGCAGGTC 120 OAGA? GG? C? TCCTCAACAT C? TCGCAGCC CTCGTGCAG? GOCCGCACA GTCGOCGGOC 180 GOCAACACCG OTA? CACCGG C? CGCGCCO GCGA? GG? C? GC ?? TGCC ?? CGCßOOCOCC 240 ?? CG? CCCC? OCAAGA? CG? CCCGAGC? AO? OCC? GGCTC CßC? ßTCGGC CAAC ?? G? CC 300 ßGC ?? CGTCG? CG? COCC ?? C? CC? GG? T CCG? TGC? Or CGCTG? TGC? GCTGCTGOAA 360 O? CCTGGTG? ? OCTGCTG ?? GGCGOCCCTG C? C? TGCAGC? OCCCOGCGG CAATGACAAO 420 GGC ?? CGGCG TGOGCOGTOC CAACGGCGCC A? GOGTGCCG OCGGCC? GOG CGGCCTGGCC O ?? GCOCTGC? OO? O? TCG? ßCAGATCCTC OCCCAGCTCO GCOGCOOCGG TGCTGOCGCC GGCGGCsCGG GTOOCOOTOT CGGCGOTOCT GOTGGCGCOO? TOGCGOCTC CGGTGCGGQT 600 OGCGC? OGCG GTGCGAACOG CGCCGACGGC GOCAATGGCG TG ?? CGOCA? CCAOOCGAAC 660 GGCCCGC? G? COCAGOCGA TGTCAACGGT OCC ?? CGGCG CGG? TG? COG CAGCQ ?? G? C 720 C? OOOCGGCC TC? CCOOCGT CCtGC? AAAG CTGATGAAOA TCCTO ?? CGC GCTOGTsC? A 780 ATOATOC? GC ?? OOCOOCCT CGOCOOCOGC ?? CC? OGCGC? OOOCGßCTC G? GGOTGCC 840 OOCAACOCCT COCCOOCTTC CGGCGCGAAC CCOGGCGCGA? CC? GCCCOG TTCGGCOO? T 900 O? TC ?? TCGT CCGGCCAGA? CAATCTGC ?? TCCC? GATCA TOG? TGTOGT G? AGG? OOTC 960 GTCCAG? TCC TOCAGCAG? T GCTGGCOGCG C? G ?? CGGCO OCAOCCAOCA GTCCACCTCO 1020? COCAGCCG? TGT ?? 1035 ) INFORMATION FOR THE SEQUENCE: SEQ ID No. 9 i) CHARACTERISTICS OF THE SEQUENCE: A) LENGTH: 26 amino acids B) TYPE: amino acid C) TYPE OF HEBRA: D) TOPOLOGY: linear ii) TYPE OF MOLECULE: peptide xi) DESCRIPTION OF SEQUENCE: SEQ ID No. 9: Thr Leu He Glu Leu Met He Val Val Ala He He Ala Ala Leu Ala 1 5 10 15 Ala Lie Ala Leu Pro Ala Tyr Gln Asp Tyr 20 25 It is noted that in relation to this date, the best method known to the applicant to carry out the aforementioned invention, is that which is clear from the present description of the invention.

Having described the invention as above, property is claimed as contained in the following:

Claims (61)

1. A method for imparting resistance against pathogens to plants, characterized in that it comprises: the application of a hypersensitive response promoter protein or polypeptide, in a non-infectious form to a plant, under conditions where the protein or polypeptide makes contact with the cells of the plant .

2. A method according to claim 1, characterized in that the protein or hypersensitivity response promoter polypeptide corresponds to that derived from a pathogen selected from the group consisting of Erwinia amyl ovora, Erwinia chrysanthemi, Pseudomonas syringae, Pseudomonas solancearum, Xan thomonas campestris, and mixtures thereof.

3. A method according to claim 2, characterized in that the protein or polypeptide promoter of hypersensitivity response corresponds to that derived from Erwini to chrysanthemi.

4. A method according to claim 3, characterized in that the hypersensitive response promoter protein or polypeptide has an amino acid sequence corresponding to SEQ ID No. 1.

5. A method according to claim 3, characterized in that the hypersensitive response promoter protein or polypeptide has a molecular weight of 34 kDa.

6. A method according to claim 2, characterized in that the protein or hypersensitive response promoter polypeptide corresponds to that derived from Erwinia amyl ovora. 1 . A method according to claim 6, characterized in that the hypersensitive response promoter protein or polypeptide has an amino acid sequence corresponding to the

SEQ ID No. 3

8. A method according to claim 6, characterized in that the hypersensitive response promoter protein or polypeptide has a molecular weight of 37 kDa.

9. A method according to claim 2, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derived from Pseudomonas syringae.

10. A method according to claim 9, characterized in that the protein or hypersensitive response promoter polypeptide has an amino acid sequence corresponding to SEQ ID No. 5.

11. A method according to claim 9, characterized in that the hypersensitive response promoter protein or polypeptide has a molecular weight of 34-35 kDa.

12. A method according to claim 2, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derived from Pseudomonas solanacearum.

13. A method according to claim 12, characterized in that the hypersensitive response promoter protein or polypeptide has an amino acid sequence corresponding to SEQ ID No. 7.

14. A method according to claim 2, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derivative of Xan thomonas campestris.

15. A method according to claim 14, characterized in that the protein or hypersensitive response promoter polypeptide has an amino acid sequence corresponding to SEQ ID No. 9.

16. A method according to claim 1, characterized in that the plant is selected from the group consisting of dicotyledons and monocotyledons.

17. A method according to claim 16, characterized in that the plant is selected from the group consisting of rice, wheat, barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, bean, chicory, chicory, lettuce, chicory, cabbage, cauliflower, broccoli, turnip, radish, spinach, onion, garlic, eggplant, pepper, celery, carrot, zucchini, pumpkin, zucchini, cucumber, apple, pear, melon, strawberry, grape, raspberry, pineapple, soybeans, tobacco, tomato, sorghum, and sugar cane.

18. A method according to claim 16, characterized in that the plant is selected from the group consisting of Arabidopsi s thal i ana, Sain tpa ulia, petunia, pelargonium, fire flower, chrysanthemum, carnation, and zinia.

19. A method according to claim 1, characterized in that the pathogen to which the plant is resistant is selected from the group consisting of a virus, bacteria, fungi and combinations thereof.

20. A method according to claim 1, characterized in that the application is carried out by spraying, injecting, or abrading the sheets at a time close to when the application takes place.

21. A method according to claim 1, characterized in that the hypersensitive response promoter protein or polypeptide is applied to the plants as a composition further comprising a carrier.

22. A method according to claim 21, characterized in that the carrier is selected from the group consisting of water and aqueous solutions.

23. A method according to claim 21, characterized in that the composition contains more than 500 nM day protein or hypersensitive response promoter polypeptide.

24. A method according to claim 21, characterized in that the composition also contains additives selected from the group consisting of fertilizers, insecticides, fungicides and mixtures thereof.

25. A method according to claim 1, characterized in that the hypersensitive response promoter protein or polypeptide is in isolated form.

26. A method according to claim 1, characterized in that the hypersensitive response promoter protein or polypeptide is applied as bacteria that do not cause disease, and are transformed with a gene encoding the hypersensitive response promoter protein or polypeptide.

27. A method according to claim 1 characterized in that the protein or hypersensitive response promoter polypeptide is applied as bacteria which cause disease in some plant species, but not in those subject to said application, and contain a gene coding for the protein or hypersensitive response promoter polypeptide.

28. A method according to claim 1, characterized in that the application causes day protein or polypeptide infiltration in the plant.

29. A plant resistant to pathogens, characterized in that it has cells in contact with the protein or polypeptide promoter of hypersensitive, non-infectious response.

30. A pathogen resistant plant according to claim 29, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derived from a pathogen selected from the group consisting of Erwinia amylovora, Erwinia chrysanthemi, Pseudomonas syringae, Pse? Domonas solancearum, Xanthomonas. campestris, and mixtures thereof.

31. A plant resistant to pathogens according to claim 30, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derived from Erwinia chrysan themi.

32. A plant resistant to pathogens according to claim 31, characterized in that the protein or hypersensitive response promoter polypeptide has an amino acid sequence corresponding to SEQ ID No. 1.

33. A pathogen resistant plant according to claim 30, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derived from Erwinia amyl ovora.

34. A plant resistant to pathogens according to claim 33, characterized in that the protein or hypersensitive response promoter polypeptide has an amino acid sequence corresponding to SEQ ID No. 3.

35. A plant resistant to pathogens according to claim 30, characterized in that the protein or hypersensitive response promoter polypeptide corresponds to that derived from Pseudomonas syringae.

36. A plant resistant to pathogens according to claim 35, characterized in that the protein or hypersensitive response promoter polypeptide has an amino acid sequence corresponding to SEQ ID No. 5.

37. A plant resistant to pathogens according to claim 30, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derived from Pseudomonas sol anacearum.

38. A plant resistant to pathogens according to claim 37, characterized in that the protein or hypersensitive response promoter polypeptide has an amino acid sequence corresponding to SEQ ID No. 7.

39. A plant resistant to pathogens according to claim 30, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that Xantho / ponas campestris derivative.

40. A plant resistant to pathogens according to claim 29, characterized in that the protein or hypersensitive response promoter polypeptide has an amino acid sequence corresponding to SEQ ID No. 9.

41. A plant resistant to pathogens according to claim 29, characterized in that the plant is selected from the group consisting of dicotyledons and monocotyledons.

42. A plant resistant to pathogens according to claim 41, characterized in that the plant is selected from the group consisting of rice, wheat, barley, rye, cotton, sunflower, peanut, corn, potato, sweet potato, peas, chicory, lettuce , endives, cabbage, cauliflower, broccoli, turnip, radish, spinach, onion, garlic, eggplant, pepper, celery, carrot, squash, pumpkin, zucchini, cucumber, apple, pear, melon, strawberry, grape, raspberry, pineapple, bean of soy, tobacco, tomato, sorghum, and sugarcane.

43. A plant resistant to pathogens according to claim 41, characterized in that the plant is selected from the group consisting of Arabidopsi s thaliana, Sain tpaulia, petunia, pelargonium, fire flower, chrysanthemum, carnation, and zinia.

44. A plant resistant to pathogens according to claim 30, characterized in that the pathogen which is resistant to the plant is selected from the group consisting of a virus, bacteria, fungus and combinations thereof.

45. A pathogen resistant plant according to claim 29, characterized in that the protein or hypersensitive response promoter polypeptide is in isolated form.

46. A plant resistant to pathogens according to claim 29, characterized in that the plant cells are in contact with bacteria which do not cause disease, and are transformed with a gene that codes for the protein or polypeptide promoter of hypersensitive response.

47. A plant resistant to pathogens according to claim 29, characterized in that the plant cells are in contact with bacteria which do not cause disease in the plant, but if they cause disease in other plant species.

48. A plant resistant to pathogens according to claim 29, characterized in that the plant is infiltrated with the polypeptide or protein.

49. A composition for imparting resistance against pathogens to plants, characterized in that it comprises: a non-infectious hypersensitive response promoter protein or polypeptide and a carrier.

50. A composition according to claim 49, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derived from a pathogen selected from the group consisting of Erwini a amylovora, Erwinia chrysanthemi, Pseudomonas syringae, Pseudomonas sol ancearum, Xan thomonas campestri s , and mixtures thereof.

51. A composition according to claim 50, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derived from Erwinia chrysanthemi.

52. A composition according to claim 50, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derived from Erwinia amylovora.

53. A composition according to claim 50, characterized in that the protein or hypersensitive response promoter polypeptide corresponds to that derived from Pseudomonas syringae.

54. A composition according to claim 50, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derived from Pseudomonas solanacearum.

55. A composition according to claim 50, characterized in that the hypersensitive response promoter protein or polypeptide corresponds to that derived from Xanthomonas campestris.

56. A composition according to claim 49, characterized in that the carrier is selected from the group consisting of water and aqueous solutions.

57. A composition according to claim 49, characterized in that the composition contains more than 500 nM day protein or hypersensitive response promoter polypeptide.

58. A composition according to claim 49, characterized in that the composition also contains additives selected from the group consisting of fertilizers, insecticides, fungicides and mixtures thereof.

59. A composition according to claim 49, characterized in that the hypersensitive response promoting protein or polypeptide is in isolated form.

60. A composition according to claim 49, characterized in that the hypersensitive response promoter protein or polypeptide is produced or capable of being produced by bacteria in the composition, the bacteria do not cause disease and are transformed with a gene encoding the protein or polypeptide hypersensitive response promoter.

61. A composition according to claim 49, characterized in that the hypersensitive response promoter protein or polypeptide is produced or capable of being produced by bacteria capable of causing disease in plants, and that it contains a gene that codes for the response promoter protein or polypeptide. hypersensitive.