EP0769058A1 - Nukleinsäurefragmenten und entsprechende peptide aus den ziegen arthritis und enkephalitis virus (caev) genom und verwendungen davon - Google Patents

Nukleinsäurefragmenten und entsprechende peptide aus den ziegen arthritis und enkephalitis virus (caev) genom und verwendungen davon

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Publication number
EP0769058A1
EP0769058A1 EP95924366A EP95924366A EP0769058A1 EP 0769058 A1 EP0769058 A1 EP 0769058A1 EP 95924366 A EP95924366 A EP 95924366A EP 95924366 A EP95924366 A EP 95924366A EP 0769058 A1 EP0769058 A1 EP 0769058A1
Authority
EP
European Patent Office
Prior art keywords
vaec
positions
env protein
corresponds
called
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Withdrawn
Application number
EP95924366A
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English (en)
French (fr)
Inventor
Giuseppe Bertoni
Gianfranco Pancino
Ernst Peterhans
Pierre Sonigo
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Centre National de la Recherche Scientifique CNRS
Original Assignee
Centre National de la Recherche Scientifique CNRS
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Publication of EP0769058A1 publication Critical patent/EP0769058A1/de
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Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N2740/00—Reverse transcribing RNA viruses
    • C12N2740/00011—Details
    • C12N2740/10011—Retroviridae
    • C12N2740/15011—Lentivirus, not HIV, e.g. FIV, SIV
    • C12N2740/15022—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes

Definitions

  • the present invention relates to nucleotide fragments derived from the env gene of the arthritis virus and caprine encephalitis (VAEC or CAEV: caprine arthri tis-encephali tis virus) and to the corresponding peptide fragments and to their applications to screening for encephalitis and caprine viral arthritis; the present invention also relates to antibodies against peptide fragments and to their applications to the diagnosis of encephalitis and viral arthritis.
  • VAEC caprine encephalitis
  • CAEV caprine arthri tis-encephali tis virus
  • the caprine arthritis and encephalitis virus is a lentivirus, causing leukoencephalitis in young goats and chronic clinical arthritis in 20-30% of naturally infected adult goats. Arthritis is usually progressive and is particularly severe in the synovial spaces of the carpal joints.
  • the nucleotide sequence of the VAEC-CO strain has been sequenced and described (M. SALTARELLI et al., Virol., 1990, 179, 347-364), from infectious clones, obtained from transfected HindIII fragments in goat synovial membrane cells.
  • the genome comprises 9189 nucleotides and successively includes the sequence coding for LTR, the sequences coding for the various viral proteins: Gag protein, Pol protein, Q regulatory protein, Tat protein, envelope proteins and protein Rev.
  • the organization of the env gene, coding for the envelope glycoprotein of VAEC is similar to that of sheep viruses (VISNA virus) and comprises a sequence coding for a surface protein (SU) and a sequence coding for a transmembrane protein (TM), which form the envelope glycoprotein.
  • the envelope proteins of VAEC are considered to be at the center of the host-virus relationship; their study is therefore essential to understand the interaction of the virus with the immune system (neutralizing epitopes, epitopes B and T) and with the target cells of the infection and to develop efficient diagnostic reagents.
  • Env anti-viral envelope protein
  • TM anti-transmembrane protein
  • SU anti-surface protein
  • the immune response to the viral antigen plays an important role in the inflammation of the joints (in particular, the inflammation of the synovial spaces of the carpal joints), in particular due to a massive infiltration of said joints. by lymphocytes, plasma cells and macrophages and by an accumulation of antibodies directed against the protein Env.
  • the serum ⁇ having an important titer with respect to the monomeric (38 kDa) and oligomeric TM glycoproteins, are found in goats with progressive arthritis (DP KNO IES et al., J. Virol. , 1990, 64, 2396-2398).
  • VAEC arthritis is primarily diagnosed using serological tests, based on a whole virus preparation; such tests have the disadvantage of being difficult to prepare and of being expensive; they also require a particularly delicate development (problem of standardization) and can, moreover, cause false negative reactions and / or false positive reactions. There are also other tests (tests).
  • the present invention is therefore intended to provide reagents capable of detecting arthritis at VAEC, which better meet the needs of practice, in particular by allowing the development of highly specific diagnostic tests (absence of false positives and false negatives) also comprising no risk for the user and allowing rapid screening of all herds.
  • the present invention relates to nucleic acid fragments, characterized in that they code for a peptide fragment including at least one segment of VAEC Env protein comprising at least one immunodominant epitope and selected from the transmembrane region of said protein, which nucleic acid fragments comprise between 15 and 255 nucleotides.
  • nucleic acid fragments there may be mentioned: a fragment corresponding to positions 8003-8163 of the gene encoding the Env protein CAEV, sequence TAAGGCAGCTGTCCAGACCCTTGCTAATGCAACTGCTGCACAGCAGGA TGTGTTAGAGGCAACCTATGCCATGGTACAGCATGTGGCTAAAGGCGTACGAATCTT GGAAGCTCGAGTGGCTCGAGTGGAAGCTATCACAGATAGAATAATGCTATACCAAG (SEQ ID NO: l), and coding for a peptide fragment called Gl;
  • TAATTGCA SEQ ID No. 3
  • G5 a fragment, corresponding to the positions
  • TM3 A fragment, corresponding to positions 8130-8165 of the gene coding for the VAEC Env protein, of sequence GAAGCTATCACAGATAGAATAATGCTATACCAAGAA (SEQ ID No. 5) and coding for a peptide fragment called TM2; - A fragment, corresponding to positions 8160-8204 of the gene coding for the Env protein of VAEC, of sequence CAAGAATTGGATTGTTGGCACTATCATCAATACTGTATAACCTCT (SEQ ID No. 6) and coding for a peptide fragment called TM3; and
  • TM4 a fragment, corresponding to positions 8256-8297 of the gene coding for the VAEC Env protein, of sequence TGCACATGGCAGCAGTGGGAGAGAGGATTACAGGGGTATGAT (SEQ ID No. 7) and coding for a peptide fragment called TM4.
  • Another subject of the present invention is a peptide fragment, characterized in that it includes at least one segment of VAEC Env protein, selected from the transmembrane region of said protein, comprising between 5 and 85 amino acids and at least one epitope. immunodominant, and in that it is recognized by at least 60% of antibodies produced during an infection and / or during an inoculation with a strain of VAEC.
  • epitope means group-specific epitopes, that is to say common to all the strains of VAEC (conserved areas), recognized by the antibodies directed against all strains of VAEC (group recognition).
  • the invention includes inter alia: a fragment including a segment of 53 amino acids, called Gl, and which corresponds to positions 665-717 of the Env protein of VAEC; a fragment including a segment of 82 amino acids, called G2, and which corresponds to positions 670-751 of said Env protein;
  • TM3 a fragment including a segment of 15 amino acids, called TM3, and which corresponds to positions 717-731 of said Env protein, which segment has the sequence: Xaa-Glu-Leu-Asp-Cys-Trp-His-Tyr-Xaa-Xaa -Tyr-Cys-Xaa-Thr-Ser (SEQ ID No.
  • the amino acid Xaa in position 13 represents Ile or Val; preferably, when the amino acid Xaa at position 9 represents His, the amino acid Xaa at position 10 and the amino acid Xaa at position 1 represent Gln and the amino acid Xaa at position 13 represents Ile and when the amino acid Xaa at position 9 represents Gln, the amino acid Xaa in position 10 and the amino acid Xaa in position 1 represent His and the amino acid Xaa in position 13 represents Val; a fragment including a segment of 14 amino acids, called TM4, and which corresponds to positions 749-762 of said Env protein, which segment has the sequence:
  • the peptide fragments G5 or TM3 and G4 or TM4 exhibit a significantly high correlation with the development of the disease and therefore serve as particularly specific markers for the diagnosis of VAEC infection; the G5 or TM3 peptide fragments also serve as markers for the diagnosis of VISNA infection.
  • peptide fragment includes all the fragments including a segment of peptides as defined above, as well as the homologous peptides; generally speaking, by homologous peptides, the peptide fragments whose position and function are equivalent, within the VAEC (same location as that defined above, on the VAEC genome). All of said peptides can advantageously be obtained either by cloning or by synthesis, in particular by synthesis of Merrifield.
  • the present invention also relates to anti-VAEC antibodies, characterized in that they consist of antibodies specific for at least one peptide fragment originating from the transmembrane region of the Env protein of VAEC, in accordance with the invention.
  • the present invention also relates to a method for screening for a VAEC and / or VISNA infection, characterized in that it consists in detecting the antibodies, possibly present in a biological sample, using at least a peptide or fragment of peptides according to the invention, optionally attached to an appropriate solid support, by bringing said biological sample into contact with said peptide (s) or peptide fragment (s), to which the antibodies bind, if such antibodies are present in the sample to analyze, the reading of the result being revealed by an appropriate means, in particular EIA, RIA, fluorescence.
  • an appropriate means in particular EIA, RIA, fluorescence.
  • the peptide is chosen from TM3 and TM4 or a mixture of these.
  • the present invention also relates to a method for screening for a VAEC infection, characterized in that a biological sample suitably treated to extract the DNA and / or the transcription products of the VAEC:
  • step (2) after which, the hybrid formed is detected.
  • said DNA can be amplified.
  • the present invention also relates to a method for screening for a VAEC infection, characterized in that it consists in detecting the envelope glycoproteins of the VAEC, by bringing together a biological sample to be tested with minus an anti-peptide antibody according to the invention, the reading of the result being revealed by an appropriate means.
  • the invention also comprises other provisions, which will emerge from the description which follows, which refers to examples of implementation of the method which is the subject of the present invention.
  • nucleotide and amino acid positions which define the various abovementioned env regions, correspond to the positions of the sequences as published in this reference.
  • the VAEC-CO clone consists of two plasmids, one containing a large part of the VAEC-CO genome from 5 '-LTR and the second containing a short insert of 321 bp, comprising the sequences coding for the C-terminal part of Env and the 3 'part of the viral LTR.
  • the Smal-HindIII fragment of VAEC-CO is subcloned into the plasmid pUC18, as well as the HindIII-HindIII fragment of 321 bp; we obtain a construction called pUC18 env 3.1.
  • the plasmid pUC18 env 3.1 is subjected to a partial digestion with DNAase I at 15 ° C. (15 ⁇ g / ml of DNAase I in Tris-HCl, pH 7.4 in the presence of MgCl2, 1.5 mM, for 20 min), so as to obtain different DNA fragments, of approximately 200 bp.
  • the ligation products are then digested with the restriction enzyme EcoRI and separated by electrophoresis in 2% LMP NUSieve® agarose gels, so as to select a set of fragments comprising between 100 and 200 bp and eliminating free linkage sequences.
  • the selected fragments are extracted with phenol from agarose; the various fragments obtained are then inserted into the EcoRI site of the phage ⁇ gtll.
  • the ligation products are then packaged in vi tro.
  • a bank of 3.10 ⁇ phages is thus constituted.
  • a sample from the ⁇ gtll bank is inoculated on the strain of E. coli Y1090 at a dilution representing 10 ⁇ phages per dish 90 cm in diameter.
  • the induction of the expression of the protein under control of the Lac promoter is triggered at 42 ° C., in the presence of isopropyl-thio- ⁇ -galactosidase (IPTG).
  • IPTG isopropyl-thio- ⁇ -galactosidase
  • the recombinant phages are selected by the absence of blue coloration of the lysis plates.
  • the PCR includes 32 cycles (cycle 1: 94 ° C,
  • the E. coli Y1090 probe is infected with 3 ⁇ 10 4 PFUs from the original unamplified library, spread on plates and incubated at 42 ° C. for 4 hours.
  • the plates are then covered with nitrocellulose filters, saturated with 10 mM IPTG and incubated for 3 hours at 37 ° C., so as to induce the expression of the fusion protein, ⁇ -galactosidase- Env peptide.
  • Filters are treated for immunological screening with sera from 3 goats by separate incubation (2 filters per serum), using standard methods, such as the defatted milk procedure
  • This screening makes it possible to isolate 5 highly immunoreactive clones, which are sequenced according to the following protocol: the PCR products are separated on 1.8% agarose gel and purified using QIAEX® beads (Qiagen®) , according to the manufacturer's instructions. A total of 1 ⁇ l of dimethyl sulfoxide (DMSO) and 20 ⁇ M either of the sense primer or of the antisense primer are added to a final volume of 10 ⁇ l.
  • DMSO dimethyl sulfoxide
  • This mixture is denatured at 100 ° C for 12 min, and immediately transferred to an ice-cold methanol bath.
  • G5 8090-8259 694-749 are included in the extracellular region of TM.
  • Overlapping decapeptides covering the sequences between positions 8022 and 8327 of the Env protein of the VAEC were synthesized.
  • An enzyme immunoassay was performed according to the manufacturer's instructions (Cambridge Research Biochemicals), using sera from 7 goats (1: 100 dilution).
  • the region containing the two conserved cysteines known to form an immunodominant structure and conserved in different lentiviruses, does not react with the sera tested, but the TM3 peptide, comprising this region, has nevertheless been synthesized.
  • TM3c Another peptide, with the same sequence, but chemically cyclized by a covalent link between the two cysteines was also prepared (TM3c), so as to reproduce a loop structure, considered to exist before in the native TM protein.
  • the TM3 epitope is located in the most conserved env region, while the sequences corresponding to TM1, TM2 and TM4 show variations (FIG. 3A).
  • TM4 also corresponds to a conserved region. Conversely, the Gl domain, which contains the TM1 and TM2 epitopes, seems more variable.
  • EXAMPLE 2 Screening test for a VAEC infection.
  • the domains binding to the antibodies namely: Gl: 8003-8163, G4: 8204-8360 and G5: 8090-8259 were expressed in the form of fusion proteins with ⁇ -galactosidase in E. coli lyso bacteria - Y1089 genes, as specified above.
  • the bacteria lysates containing the fusion proteins were prepared from lysogenic culture-HPTG.
  • the lysates (40 ⁇ g / well) are separated in SDS-PAGE gels (sodium dodecylsulfate-polyacrylamide) at 10% and transferred to nitrocellulose filters.
  • SDS-PAGE gels sodium dodecylsulfate-polyacrylamide
  • the non-specific sites are blocked by in ⁇ cubation with defatted milk at 3% in a Tris-HCl (10 mM), NaCl (150 mM) and Tween 20 (0.1%) buffer.
  • nitrocellulose strips are incubated with a goat serum diluted 1: 100/1: 800 overnight at 4 ° C.
  • the binding with the antibody is revealed by incubation with protein G conjugated to per ⁇ oxidase, diluted to 1: 5,000, followed by a revelation with 4-chlorine-1-naphthol (Sigma).
  • a lysate of bacteria infected with a non-recombinant phage ⁇ gtll is used as a negative control.
  • the sera collected before the experimental infection and a pool of sera from uninfected goats are used as an antibody control.
  • the peptides Gl, G4 and G5 as defined in Example 1 covering the immunoreactive region of the transmembrane protein TM, are used in a western blot to screen 60 sera of naturally infected goats from different herds, in the above conditions.
  • Protocol The peptides (TM1-TM4) were synthesized and purified.
  • the peptides TM3 and TM4 were. adsorbs on microtiter plate as follows:
  • TM1 peptide shows a weak bond and the TM2 peptide does not bind at all to these plates or to other ELISA plates tested.
  • TM1 1 mg / ml
  • TM2 0.5 mg / ml
  • the activated pep ⁇ tides are diluted in an ice-cold 0.1 M carbonate buffer (pH 8.9) at 10 ⁇ g / ml and 100 ⁇ l / well are adsorbed by Covalink® plates overnight at 4 ° C.
  • the ELISA test is carried out as follows: after coating the microtitra ⁇ tion plates, the latter are washed three times with PBS, the residual adsorption sites on the plates are saturated by incubation with 100 ⁇ l of PBS containing milk (1 %) and Tween 20 (0.1%) (ELISA EB buffer) for 2 hours at room temperature.
  • optical density is measured at 405 nm on tests carried out in duplicate.
  • the results are normalized using, as standard, a set of goat sera, calibrated in a Gag-GST ELISA, produced as described in R.G. ZANONI et al., J. Clin. Microbiol., 1991, 29, 1290-1294.
  • TM4, TM2 and TM1 peptides react with the majority of sera, although with lower percentages than for TM3.
  • optical density values obtained by ELISA were normalized and expressed as a percentage of reactivity, compared to a reference serum consisting, as specified above, in a set of serums seropositive with respect to VAEC.
  • the ELISA reactivities of sera from healthy animals and arthritic animals were compared.
  • IR reactivity index
  • TM fragments or anti-TM antibodies
  • results obtained made it possible to identify the determinants involved in the correlation between serological reactivity and evolution of viral arthritis, and therefore allow better monitoring of this disease.
  • the TM3 epitope of the VAEC TM protein has the same location as the immunodominant epitope of other lentiviruses such as the lentiviruses causing immunodeficiency: HIV, SIV and FIV.
  • This epitope is located in a region containing a structure defined by two cysteines which is conserved by all of the lentiviruses despite the absence of a homology of the primary sequence.
  • cysteines which is conserved by all of the lentiviruses despite the absence of a homology of the primary sequence.
  • SIV and FIV the sequence between the cysteines is highly conserved between the different viral isolates of the same species.
  • the ELISA TM3 according to the invention is significantly more specific. The only case of reactive serum with TM3 and
  • TM4 and negative with the Chekit® test requires additional tools to determine whether it is a true or a false positive.
  • SEQ ID NO: 1 TAAGGCAGCT GTCCAGACCC TTGCTAATGC AACTGCTGCA CAGCAGGATG TGTTAGAGGC 60 AACCTATGCC ATGGTACAGC ATGTGGCTAA AGGCGTACGA ATCTTGGAAG CTCGAGTGGC 120 TCGAGATGGAA GCTGATA
  • SEQ ID NO: 2 TACAAAAACA GAAGTAGCAA AATATATCAA TTGGACGAGG TTTAAGGATA ATTGCACATG 60 GCAGCAGTGG GAGAGAGGAT TACAGGGTA TGATACAAAC TTAACAATAC TGTTAAAGGA TACAGAAGA 120 (2) INFORMATION FOR SEQ ID NO: 3:

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  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
EP95924366A 1994-06-28 1995-06-26 Nukleinsäurefragmenten und entsprechende peptide aus den ziegen arthritis und enkephalitis virus (caev) genom und verwendungen davon Withdrawn EP0769058A1 (de)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
FR9407933A FR2721618B1 (fr) 1994-06-28 1994-06-28 Fragments d'acide nucléique et fragments peptidiques correspondants issus du génome du virus de l'arthrite et de l'encéphalite caprine (VAEC) et leurs applications.
FR9407933 1994-06-28
PCT/FR1995/000848 WO1996000784A1 (fr) 1994-06-28 1995-06-26 Fragments d'acide nucleique et fragments peptidiques correspondants issus du genome du virus de l'arthrite et de l'encephalite caprine (vaec) et leurs applications

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EP0769058A1 true EP0769058A1 (de) 1997-04-23

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ID=9464728

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EP95924366A Withdrawn EP0769058A1 (de) 1994-06-28 1995-06-26 Nukleinsäurefragmenten und entsprechende peptide aus den ziegen arthritis und enkephalitis virus (caev) genom und verwendungen davon

Country Status (7)

Country Link
US (1) US5858672A (de)
EP (1) EP0769058A1 (de)
AU (1) AU693575B2 (de)
CA (1) CA2193997A1 (de)
FR (1) FR2721618B1 (de)
NZ (1) NZ289147A (de)
WO (1) WO1996000784A1 (de)

Families Citing this family (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
AU732865B2 (en) * 1996-03-15 2001-05-03 University Of Southern California Caprine arthritis-encephalitis virus provides immunoprotection against HIV-1 infection
FR2765688B1 (fr) 1997-07-04 1999-09-10 Pasteur Institut Reactif de detection et de suivi des infections provoquees par le virus d'epstein-barr et ses applications
EP0953574A1 (de) * 1998-04-30 1999-11-03 Innogenetics N.V. Immundiagnostischer Wirkstoff zum Nachweiss von Maedi-Visna Virus und CAEV Infektionen
US6602505B2 (en) 1998-04-30 2003-08-05 University Of Southern California Viral chimeras comprised of CAEV and HIV-1 genetic elements
KR20020033983A (ko) * 2000-10-31 2002-05-08 김규조 신용카드를 이용한 자동판매기 및 그 서비스 방법

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO9600784A1 *

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Publication number Publication date
AU2890495A (en) 1996-01-25
US5858672A (en) 1999-01-12
NZ289147A (en) 1998-07-28
AU693575B2 (en) 1998-07-02
CA2193997A1 (fr) 1996-01-11
FR2721618A1 (fr) 1995-12-29
FR2721618B1 (fr) 1996-09-13
WO1996000784A1 (fr) 1996-01-11

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