Delineation of a neutralizing subregion within the immunodominant epitope (GH loop) of foot-and-mouth disease virus VP1 which does not contain the RGD motif
Identifieur interne : 003091 ( Main/Corpus ); précédent : 003090; suivant : 003092Delineation of a neutralizing subregion within the immunodominant epitope (GH loop) of foot-and-mouth disease virus VP1 which does not contain the RGD motif
Auteurs : Fred Brown ; Nadia Benkirane ; David Limal ; Hubert Halimi ; John F. E Newman ; Marc H. V Van Regenmortel ; Jean-Paul Briand ; Sylviane MullerSource :
- Vaccine [ 0264-410X ] ; 1999.
English descriptors
Abstract
The major immunogenic site of foot-and-mouth disease virus (FMDV) is contained in a disordered loop comprising residues 134–158 of capsid protein VP1, located on the surface of the viral particle. Peptides corresponding to this sequence generally elicit protective levels of neutralizing antibodies in guinea pigs. In some instances, however, the level of neutralizing antibodies is low although the level of antibodies against the peptide, determined by ELISA, is as high as that in the sera with high neutralizing antibody titres. In an attempt to ascertain the reason for this difference, we have synthesized on a cellulose membrane 10 overlapping decapeptides, offset by one residue, covering the segment 141–159 of VP1 of two viruses belonging to serotypes A12 and O1, and tested them with guinea pig antisera raised against peptide 141–159, VP1 and FMDV particles (SPOTscan method). With type A, some peptides which were strongly positive with highly neutralizing antisera did not include the RGD triplet located at residues 145–147. In contrast, antisera with low neutralization titres reacted only with decapeptides which included the RGD motif. Moreover, peptide 147–156 coupled to keyhole limpet haemocyanin, but not peptide 141–149 coupled to the same carrier, elicited high levels of neutralizing antibodies in guinea pigs. In the case of serotype O, highly neutralizing antisera to virus reacted in ELISA with peptides 141–150 (containing the RGD motif) and 135–144 (located upstream from the RGD motif). The results suggest that the RGD triplet is not an indispensable constituent of peptides able to elicit a neutralizing antibody response against the virus.
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DOI: 10.1016/S0264-410X(99)00169-3
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Delineation of a neutralizing subregion within the immunodominant epitope (GH loop) of foot-and-mouth disease virus VP1 which does not contain the RGD motif</title><author><name sortKey="Brown, Fred" sort="Brown, Fred" uniqKey="Brown F" first="Fred" last="Brown">Fred Brown</name><affiliation><mods:affiliation>Plum Island Animal Disease Center, USDA/ARS, P.O. Box 848, Greenport, NY 11944-0848, USA</mods:affiliation></affiliation></author><author><name sortKey="Benkirane, Nadia" sort="Benkirane, Nadia" uniqKey="Benkirane N" first="Nadia" last="Benkirane">Nadia Benkirane</name><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author><author><name sortKey="Limal, David" sort="Limal, David" uniqKey="Limal D" first="David" last="Limal">David Limal</name><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author><author><name sortKey="Halimi, Hubert" sort="Halimi, Hubert" uniqKey="Halimi H" first="Hubert" last="Halimi">Hubert Halimi</name><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author><author><name sortKey="Newman, John F E" sort="Newman, John F E" uniqKey="Newman J" first="John F. 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V Van Regenmortel</name><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author><author><name sortKey="Briand, Jean Paul" sort="Briand, Jean Paul" uniqKey="Briand J" first="Jean-Paul" last="Briand">Jean-Paul Briand</name><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author><author><name sortKey="Muller, Sylviane" sort="Muller, Sylviane" uniqKey="Muller S" first="Sylviane" last="Muller">Sylviane Muller</name><affiliation><mods:affiliation>E-mail: smuller@ibmc.u-strasbg.fr</mods:affiliation></affiliation><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:2AD6B7EAD87108170867942AE3822C4EC7E5951E</idno><date when="1999" year="1999">1999</date><idno type="doi">10.1016/S0264-410X(99)00169-3</idno><idno type="url">https://api.istex.fr/document/2AD6B7EAD87108170867942AE3822C4EC7E5951E/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">003091</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Delineation of a neutralizing subregion within the immunodominant epitope (GH loop) of foot-and-mouth disease virus VP1 which does not contain the RGD motif</title><author><name sortKey="Brown, Fred" sort="Brown, Fred" uniqKey="Brown F" first="Fred" last="Brown">Fred Brown</name><affiliation><mods:affiliation>Plum Island Animal Disease Center, USDA/ARS, P.O. Box 848, Greenport, NY 11944-0848, USA</mods:affiliation></affiliation></author><author><name sortKey="Benkirane, Nadia" sort="Benkirane, Nadia" uniqKey="Benkirane N" first="Nadia" last="Benkirane">Nadia Benkirane</name><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author><author><name sortKey="Limal, David" sort="Limal, David" uniqKey="Limal D" first="David" last="Limal">David Limal</name><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author><author><name sortKey="Halimi, Hubert" sort="Halimi, Hubert" uniqKey="Halimi H" first="Hubert" last="Halimi">Hubert Halimi</name><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author><author><name sortKey="Newman, John F E" sort="Newman, John F E" uniqKey="Newman J" first="John F. E" last="Newman">John F. E Newman</name><affiliation><mods:affiliation>Plum Island Animal Disease Center, USDA/ARS, P.O. Box 848, Greenport, NY 11944-0848, USA</mods:affiliation></affiliation></author><author><name sortKey="Van Regenmortel, Marc H V" sort="Van Regenmortel, Marc H V" uniqKey="Van Regenmortel M" first="Marc H. V" last="Van Regenmortel">Marc H. V Van Regenmortel</name><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author><author><name sortKey="Briand, Jean Paul" sort="Briand, Jean Paul" uniqKey="Briand J" first="Jean-Paul" last="Briand">Jean-Paul Briand</name><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author><author><name sortKey="Muller, Sylviane" sort="Muller, Sylviane" uniqKey="Muller S" first="Sylviane" last="Muller">Sylviane Muller</name><affiliation><mods:affiliation>E-mail: smuller@ibmc.u-strasbg.fr</mods:affiliation></affiliation><affiliation><mods:affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Vaccine</title><title level="j" type="abbrev">JVAC</title><idno type="ISSN">0264-410X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1999">1999</date><biblScope unit="volume">18</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="50">50</biblScope><biblScope unit="page" to="56">56</biblScope></imprint><idno type="ISSN">0264-410X</idno></series><idno type="istex">2AD6B7EAD87108170867942AE3822C4EC7E5951E</idno><idno type="DOI">10.1016/S0264-410X(99)00169-3</idno><idno type="PII">S0264-410X(99)00169-3</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0264-410X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Foot-and-mouth disease virus</term><term>Neutralization</term><term>Synthetic peptide</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The major immunogenic site of foot-and-mouth disease virus (FMDV) is contained in a disordered loop comprising residues 134–158 of capsid protein VP1, located on the surface of the viral particle. Peptides corresponding to this sequence generally elicit protective levels of neutralizing antibodies in guinea pigs. In some instances, however, the level of neutralizing antibodies is low although the level of antibodies against the peptide, determined by ELISA, is as high as that in the sera with high neutralizing antibody titres. In an attempt to ascertain the reason for this difference, we have synthesized on a cellulose membrane 10 overlapping decapeptides, offset by one residue, covering the segment 141–159 of VP1 of two viruses belonging to serotypes A12 and O1, and tested them with guinea pig antisera raised against peptide 141–159, VP1 and FMDV particles (SPOTscan method). With type A, some peptides which were strongly positive with highly neutralizing antisera did not include the RGD triplet located at residues 145–147. In contrast, antisera with low neutralization titres reacted only with decapeptides which included the RGD motif. Moreover, peptide 147–156 coupled to keyhole limpet haemocyanin, but not peptide 141–149 coupled to the same carrier, elicited high levels of neutralizing antibodies in guinea pigs. In the case of serotype O, highly neutralizing antisera to virus reacted in ELISA with peptides 141–150 (containing the RGD motif) and 135–144 (located upstream from the RGD motif). The results suggest that the RGD triplet is not an indispensable constituent of peptides able to elicit a neutralizing antibody response against the virus.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Fred Brown</name><affiliations><json:string>Plum Island Animal Disease Center, USDA/ARS, P.O. Box 848, Greenport, NY 11944-0848, USA</json:string></affiliations></json:item><json:item><name>Nadia Benkirane</name><affiliations><json:string>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</json:string></affiliations></json:item><json:item><name>David Limal</name><affiliations><json:string>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</json:string></affiliations></json:item><json:item><name>Hubert Halimi</name><affiliations><json:string>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</json:string></affiliations></json:item><json:item><name>John F.E Newman</name><affiliations><json:string>Plum Island Animal Disease Center, USDA/ARS, P.O. Box 848, Greenport, NY 11944-0848, USA</json:string></affiliations></json:item><json:item><name>Marc H.V Van Regenmortel</name><affiliations><json:string>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</json:string></affiliations></json:item><json:item><name>Jean-Paul Briand</name><affiliations><json:string>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</json:string></affiliations></json:item><json:item><name>Sylviane Muller</name><affiliations><json:string>E-mail: smuller@ibmc.u-strasbg.fr</json:string><json:string>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Foot-and-mouth disease virus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Neutralization</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Synthetic peptide</value></json:item></subject><language><json:string>eng</json:string></language><abstract>The major immunogenic site of foot-and-mouth disease virus (FMDV) is contained in a disordered loop comprising residues 134–158 of capsid protein VP1, located on the surface of the viral particle. Peptides corresponding to this sequence generally elicit protective levels of neutralizing antibodies in guinea pigs. In some instances, however, the level of neutralizing antibodies is low although the level of antibodies against the peptide, determined by ELISA, is as high as that in the sera with high neutralizing antibody titres. In an attempt to ascertain the reason for this difference, we have synthesized on a cellulose membrane 10 overlapping decapeptides, offset by one residue, covering the segment 141–159 of VP1 of two viruses belonging to serotypes A12 and O1, and tested them with guinea pig antisera raised against peptide 141–159, VP1 and FMDV particles (SPOTscan method). With type A, some peptides which were strongly positive with highly neutralizing antisera did not include the RGD triplet located at residues 145–147. In contrast, antisera with low neutralization titres reacted only with decapeptides which included the RGD motif. Moreover, peptide 147–156 coupled to keyhole limpet haemocyanin, but not peptide 141–149 coupled to the same carrier, elicited high levels of neutralizing antibodies in guinea pigs. In the case of serotype O, highly neutralizing antisera to virus reacted in ELISA with peptides 141–150 (containing the RGD motif) and 135–144 (located upstream from the RGD motif). The results suggest that the RGD triplet is not an indispensable constituent of peptides able to elicit a neutralizing antibody response against the virus.</abstract><qualityIndicators><score>7.262</score><pdfVersion>1.2</pdfVersion><pdfPageSize>595 x 792 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>3</keywordCount><abstractCharCount>1673</abstractCharCount><pdfWordCount>4262</pdfWordCount><pdfCharCount>26203</pdfCharCount><pdfPageCount>7</pdfPageCount><abstractWordCount>254</abstractWordCount></qualityIndicators><title>Delineation of a neutralizing subregion within the immunodominant epitope (GH loop) of foot-and-mouth disease virus VP1 which does not contain the RGD motif</title><pii><json:string>S0264-410X(99)00169-3</json:string></pii><genre><json:string>research-article</json:string></genre><host><volume>18</volume><pii><json:string>S0264-410X(00)X0086-2</json:string></pii><pages><last>56</last><first>50</first></pages><issn><json:string>0264-410X</json:string></issn><issue>1–2</issue><genre><json:string>Journal</json:string></genre><language><json:string>unknown</json:string></language><title>Vaccine</title><publicationDate>1999</publicationDate></host><categories><wos><json:string>IMMUNOLOGY</json:string><json:string>MEDICINE, RESEARCH & EXPERIMENTAL</json:string><json:string>VETERINARY SCIENCES</json:string></wos></categories><publicationDate>1999</publicationDate><copyrightDate>1999</copyrightDate><doi><json:string>10.1016/S0264-410X(99)00169-3</json:string></doi><id>2AD6B7EAD87108170867942AE3822C4EC7E5951E</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/2AD6B7EAD87108170867942AE3822C4EC7E5951E/fulltext/pdf</uri></json:item><json:item><original>true</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/2AD6B7EAD87108170867942AE3822C4EC7E5951E/fulltext/txt</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/2AD6B7EAD87108170867942AE3822C4EC7E5951E/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/2AD6B7EAD87108170867942AE3822C4EC7E5951E/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Delineation of a neutralizing subregion within the immunodominant epitope (GH loop) of foot-and-mouth disease virus VP1 which does not contain the RGD motif</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1999</date></publicationStmt><notesStmt><note type="content">Fig. 1: SPOTscan of overlapping decapeptides covering the VP1 segments 141–159 of serotypes A (variant USA) and O1 (strain Kaufbeuren) with guinea pig antibodies induced against peptides 141–159, 141–149 and 147–156 (serotype A) and 141–159 (serotype O1), VP1 of serotype A, and A and O1 virus particles. The presence of residues of the RGD motif in each peptide is mentioned on the top. The principal characteristics of antisera (specificity, respective neutralization indices at 1/100 serum dilution and working dilutions used in the SPOTscan) are indicated on the right. Positive reactions were revealed using rabbit anti-guinea pig Ig conjugated with alkaline phosphatase and BCIP/NT color development substrate (a and c) or the ECL immunoblotting reagents (b and d–h). Reaction with normal guinea pig serum was insignificant (not shown).</note><note type="content">Fig. 2: Capacity of serotype A peptides 141–149 and 147–156 to inhibit the ELISA reaction between peptide 141–159 and guinea pig antisera induced against virion, VP1 and peptide 141–159 of serotype A. Antipeptide sera were raised against peptide 141–159 conjugated to KLH via its additional N-terminal cysteine residue. Antisera were diluted 1/20,000 and successively incubated for 1 h at 37°C and 1 h at 4°C with increasing amounts of peptide analogues. The mixtures were then added to microtitre plates precoated with 0.2 μM peptide 141–159. Peptides used as inhibitors: serotype A peptides 141–159 (⋅), 141–149 (■) and 147–156 (▴).</note><note type="content">Fig. 3: Capacity of serotype O peptides 135–144, 141–150 and 147–156 to inhibit the ELISA reaction between peptide 135–159 and guinea pig antisera to serotype O virus. The anti-O virus antiserum was diluted 1/10,000 and incubated with peptide analogues as indicated in Fig. 2. The mixtures were added to microtitre plates precoated with 0.5 μM peptide 135–159. Inhibitor peptides were serotype O peptides 135–144 (○), 141–150 (▵) and 147–156 (□).</note><note type="content">Table 1: Amino acid sequences of VP1 peptides of FMDV</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Delineation of a neutralizing subregion within the immunodominant epitope (GH loop) of foot-and-mouth disease virus VP1 which does not contain the RGD motif</title><author><persName><forename type="first">Fred</forename><surname>Brown</surname></persName><affiliation>Plum Island Animal Disease Center, USDA/ARS, P.O. Box 848, Greenport, NY 11944-0848, USA</affiliation></author><author><persName><forename type="first">Nadia</forename><surname>Benkirane</surname></persName><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation></author><author><persName><forename type="first">David</forename><surname>Limal</surname></persName><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation></author><author><persName><forename type="first">Hubert</forename><surname>Halimi</surname></persName><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation></author><author><persName><forename type="first">John F.E</forename><surname>Newman</surname></persName><affiliation>Plum Island Animal Disease Center, USDA/ARS, P.O. Box 848, Greenport, NY 11944-0848, USA</affiliation></author><author><persName><forename type="first">Marc H.V</forename><surname>Van Regenmortel</surname></persName><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation></author><author><persName><forename type="first">Jean-Paul</forename><surname>Briand</surname></persName><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation></author><author><persName><forename type="first">Sylviane</forename><surname>Muller</surname></persName><email>smuller@ibmc.u-strasbg.fr</email><note type="correspondence"><p>Corresponding author. Tel.: +33-3-8841-7027; fax +33-3-8861-0680</p></note><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation></author></analytic><monogr><title level="j">Vaccine</title><title level="j" type="abbrev">JVAC</title><idno type="pISSN">0264-410X</idno><idno type="PII">S0264-410X(00)X0086-2</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1999"></date><biblScope unit="volume">18</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="50">50</biblScope><biblScope unit="page" to="56">56</biblScope></imprint></monogr><idno type="istex">2AD6B7EAD87108170867942AE3822C4EC7E5951E</idno><idno type="DOI">10.1016/S0264-410X(99)00169-3</idno><idno type="PII">S0264-410X(99)00169-3</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1999</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>The major immunogenic site of foot-and-mouth disease virus (FMDV) is contained in a disordered loop comprising residues 134–158 of capsid protein VP1, located on the surface of the viral particle. Peptides corresponding to this sequence generally elicit protective levels of neutralizing antibodies in guinea pigs. In some instances, however, the level of neutralizing antibodies is low although the level of antibodies against the peptide, determined by ELISA, is as high as that in the sera with high neutralizing antibody titres. In an attempt to ascertain the reason for this difference, we have synthesized on a cellulose membrane 10 overlapping decapeptides, offset by one residue, covering the segment 141–159 of VP1 of two viruses belonging to serotypes A12 and O1, and tested them with guinea pig antisera raised against peptide 141–159, VP1 and FMDV particles (SPOTscan method). With type A, some peptides which were strongly positive with highly neutralizing antisera did not include the RGD triplet located at residues 145–147. In contrast, antisera with low neutralization titres reacted only with decapeptides which included the RGD motif. Moreover, peptide 147–156 coupled to keyhole limpet haemocyanin, but not peptide 141–149 coupled to the same carrier, elicited high levels of neutralizing antibodies in guinea pigs. In the case of serotype O, highly neutralizing antisera to virus reacted in ELISA with peptides 141–150 (containing the RGD motif) and 135–144 (located upstream from the RGD motif). The results suggest that the RGD triplet is not an indispensable constituent of peptides able to elicit a neutralizing antibody response against the virus.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>Foot-and-mouth disease virus</term></item><item><term>Neutralization</term></item><item><term>Synthetic peptide</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1999-04-08">Registration</change><change when="1999">Published</change></revisionDesc></teiHeader></istex:fulltextTEI></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: ce:floats; body; tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"><istex:entity SYSTEM="fx1" NDATA="IMAGE" name="fx1"></istex:entity><istex:entity SYSTEM="gr1" NDATA="IMAGE" name="gr1"></istex:entity><istex:entity SYSTEM="gr2" NDATA="IMAGE" name="gr2"></istex:entity><istex:entity SYSTEM="gr3" NDATA="IMAGE" name="gr3"></istex:entity></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>JVAC</jid><aid>1612</aid><ce:pii>S0264-410X(99)00169-3</ce:pii><ce:doi>10.1016/S0264-410X(99)00169-3</ce:doi><ce:copyright type="full-transfer" year="1999">Elsevier Science Ltd</ce:copyright></item-info><head><ce:title>Delineation of a neutralizing subregion within the immunodominant epitope (GH loop) of foot-and-mouth disease virus VP1 which does not contain the RGD motif</ce:title><ce:author-group><ce:author><ce:given-name>Fred</ce:given-name><ce:surname>Brown</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Nadia</ce:given-name><ce:surname>Benkirane</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>David</ce:given-name><ce:surname>Limal</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Hubert</ce:given-name><ce:surname>Halimi</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>John F.E</ce:given-name><ce:surname>Newman</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Marc H.V</ce:given-name><ce:surname>Van Regenmortel</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jean-Paul</ce:given-name><ce:surname>Briand</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Sylviane</ce:given-name><ce:surname>Muller</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref><ce:cross-ref refid="CORR1">*</ce:cross-ref><ce:e-address>smuller@ibmc.u-strasbg.fr</ce:e-address></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Plum Island Animal Disease Center, USDA/ARS, P.O. Box 848, Greenport, NY 11944-0848, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</ce:textfn></ce:affiliation><ce:correspondence id="CORR1"><ce:label>*</ce:label><ce:text>Corresponding author. Tel.: +33-3-8841-7027; fax +33-3-8861-0680</ce:text></ce:correspondence></ce:author-group><ce:date-received day="16" month="12" year="1998"></ce:date-received><ce:date-accepted day="8" month="4" year="1999"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The major immunogenic site of foot-and-mouth disease virus (FMDV) is contained in a disordered loop comprising residues 134–158 of capsid protein VP1, located on the surface of the viral particle. Peptides corresponding to this sequence generally elicit protective levels of neutralizing antibodies in guinea pigs. In some instances, however, the level of neutralizing antibodies is low although the level of antibodies against the peptide, determined by ELISA, is as high as that in the sera with high neutralizing antibody titres. In an attempt to ascertain the reason for this difference, we have synthesized on a cellulose membrane 10 overlapping decapeptides, offset by one residue, covering the segment 141–159 of VP1 of two viruses belonging to serotypes A12 and O1, and tested them with guinea pig antisera raised against peptide 141–159, VP1 and FMDV particles (SPOTscan method). With type A, some peptides which were strongly positive with highly neutralizing antisera did not include the RGD triplet located at residues 145–147. In contrast, antisera with low neutralization titres reacted only with decapeptides which included the RGD motif. Moreover, peptide 147–156 coupled to keyhole limpet haemocyanin, but not peptide 141–149 coupled to the same carrier, elicited high levels of neutralizing antibodies in guinea pigs. In the case of serotype O, highly neutralizing antisera to virus reacted in ELISA with peptides 141–150 (containing the RGD motif) and 135–144 (located upstream from the RGD motif). The results suggest that the RGD triplet is not an indispensable constituent of peptides able to elicit a neutralizing antibody response against the virus.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword" xml:lang="en"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Foot-and-mouth disease virus</ce:text></ce:keyword><ce:keyword><ce:text>Neutralization</ce:text></ce:keyword><ce:keyword><ce:text>Synthetic peptide</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Delineation of a neutralizing subregion within the immunodominant epitope (GH loop) of foot-and-mouth disease virus VP1 which does not contain the RGD motif</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Delineation of a neutralizing subregion within the immunodominant epitope (GH loop) of foot-and-mouth disease virus VP1 which does not contain the RGD motif</title></titleInfo><name type="personal"><namePart type="given">Fred</namePart><namePart type="family">Brown</namePart><affiliation>Plum Island Animal Disease Center, USDA/ARS, P.O. Box 848, Greenport, NY 11944-0848, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Nadia</namePart><namePart type="family">Benkirane</namePart><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">David</namePart><namePart type="family">Limal</namePart><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hubert</namePart><namePart type="family">Halimi</namePart><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">John F.E</namePart><namePart type="family">Newman</namePart><affiliation>Plum Island Animal Disease Center, USDA/ARS, P.O. Box 848, Greenport, NY 11944-0848, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Marc H.V</namePart><namePart type="family">Van Regenmortel</namePart><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean-Paul</namePart><namePart type="family">Briand</namePart><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Sylviane</namePart><namePart type="family">Muller</namePart><affiliation>E-mail: smuller@ibmc.u-strasbg.fr</affiliation><affiliation>Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue René Descartes, F67084 Strasbourg, France</affiliation><description>Corresponding author. Tel.: +33-3-8841-7027; fax +33-3-8861-0680</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1999</dateIssued><dateValid encoding="w3cdtf">1999-04-08</dateValid><copyrightDate encoding="w3cdtf">1999</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">The major immunogenic site of foot-and-mouth disease virus (FMDV) is contained in a disordered loop comprising residues 134–158 of capsid protein VP1, located on the surface of the viral particle. Peptides corresponding to this sequence generally elicit protective levels of neutralizing antibodies in guinea pigs. In some instances, however, the level of neutralizing antibodies is low although the level of antibodies against the peptide, determined by ELISA, is as high as that in the sera with high neutralizing antibody titres. In an attempt to ascertain the reason for this difference, we have synthesized on a cellulose membrane 10 overlapping decapeptides, offset by one residue, covering the segment 141–159 of VP1 of two viruses belonging to serotypes A12 and O1, and tested them with guinea pig antisera raised against peptide 141–159, VP1 and FMDV particles (SPOTscan method). With type A, some peptides which were strongly positive with highly neutralizing antisera did not include the RGD triplet located at residues 145–147. In contrast, antisera with low neutralization titres reacted only with decapeptides which included the RGD motif. Moreover, peptide 147–156 coupled to keyhole limpet haemocyanin, but not peptide 141–149 coupled to the same carrier, elicited high levels of neutralizing antibodies in guinea pigs. In the case of serotype O, highly neutralizing antisera to virus reacted in ELISA with peptides 141–150 (containing the RGD motif) and 135–144 (located upstream from the RGD motif). The results suggest that the RGD triplet is not an indispensable constituent of peptides able to elicit a neutralizing antibody response against the virus.</abstract><note type="content">Fig. 1: SPOTscan of overlapping decapeptides covering the VP1 segments 141–159 of serotypes A (variant USA) and O1 (strain Kaufbeuren) with guinea pig antibodies induced against peptides 141–159, 141–149 and 147–156 (serotype A) and 141–159 (serotype O1), VP1 of serotype A, and A and O1 virus particles. The presence of residues of the RGD motif in each peptide is mentioned on the top. The principal characteristics of antisera (specificity, respective neutralization indices at 1/100 serum dilution and working dilutions used in the SPOTscan) are indicated on the right. Positive reactions were revealed using rabbit anti-guinea pig Ig conjugated with alkaline phosphatase and BCIP/NT color development substrate (a and c) or the ECL immunoblotting reagents (b and d–h). Reaction with normal guinea pig serum was insignificant (not shown).</note><note type="content">Fig. 2: Capacity of serotype A peptides 141–149 and 147–156 to inhibit the ELISA reaction between peptide 141–159 and guinea pig antisera induced against virion, VP1 and peptide 141–159 of serotype A. Antipeptide sera were raised against peptide 141–159 conjugated to KLH via its additional N-terminal cysteine residue. Antisera were diluted 1/20,000 and successively incubated for 1 h at 37°C and 1 h at 4°C with increasing amounts of peptide analogues. The mixtures were then added to microtitre plates precoated with 0.2 μM peptide 141–159. Peptides used as inhibitors: serotype A peptides 141–159 (⋅), 141–149 (■) and 147–156 (▴).</note><note type="content">Fig. 3: Capacity of serotype O peptides 135–144, 141–150 and 147–156 to inhibit the ELISA reaction between peptide 135–159 and guinea pig antisera to serotype O virus. The anti-O virus antiserum was diluted 1/10,000 and incubated with peptide analogues as indicated in Fig. 2. The mixtures were added to microtitre plates precoated with 0.5 μM peptide 135–159. Inhibitor peptides were serotype O peptides 135–144 (○), 141–150 (▵) and 147–156 (□).</note><note type="content">Table 1: Amino acid sequences of VP1 peptides of FMDV</note><subject lang="en"><genre>Keywords</genre><topic>Foot-and-mouth disease virus</topic><topic>Neutralization</topic><topic>Synthetic peptide</topic></subject><relatedItem type="host"><titleInfo><title>Vaccine</title></titleInfo><titleInfo type="abbreviated"><title>JVAC</title></titleInfo><genre type="Journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19990820</dateIssued></originInfo><identifier type="ISSN">0264-410X</identifier><identifier type="PII">S0264-410X(00)X0086-2</identifier><part><date>19990820</date><detail type="volume"><number>18</number><caption>vol.</caption></detail><detail type="issue"><number>1–2</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>202</end></extent><extent unit="pages"><start>50</start><end>56</end></extent></part></relatedItem><identifier type="istex">2AD6B7EAD87108170867942AE3822C4EC7E5951E</identifier><identifier type="DOI">10.1016/S0264-410X(99)00169-3</identifier><identifier type="PII">S0264-410X(99)00169-3</identifier><accessCondition type="use and reproduction" contentType="">© 1999Elsevier Science Ltd</accessCondition><recordInfo><recordContentSource>ELSEVIER</recordContentSource><recordOrigin>Elsevier Science Ltd, ©1999</recordOrigin></recordInfo></mods></metadata><enrichments><istex:catWosTEI uri="https://api.istex.fr/document/2AD6B7EAD87108170867942AE3822C4EC7E5951E/enrichments/catWos"><teiHeader><profileDesc><textClass><classCode scheme="WOS">IMMUNOLOGY</classCode><classCode scheme="WOS">MEDICINE, RESEARCH & EXPERIMENTAL</classCode><classCode scheme="WOS">VETERINARY SCIENCES</classCode></textClass></profileDesc></teiHeader></istex:catWosTEI></enrichments><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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