Fine Mapping of a Continuous Epitope on VP7 of Bluetongue Virus Using Overlapping Synthetic Peptides and a Random Epitope Library
Identifieur interne : 004445 ( Main/Exploration ); précédent : 004444; suivant : 004446Fine Mapping of a Continuous Epitope on VP7 of Bluetongue Virus Using Overlapping Synthetic Peptides and a Random Epitope Library
Auteurs : Dion H. Du Plessis [Australie] ; Lin-Fa Wang [Australie] ; Frances A. Jordaan [Australie] ; Bryan T. Eaton [Australie]Source :
- Virology [ 0042-6822 ] ; 1994.
Abstract
Abstract: Two complementary techniques have been used to delineate an epitope on VP7 of bluetongue virus. Two MAbs (F10 and D11), both of which bound within a region spanning amino acids 255 to 274 in the 349 amino acid protein, were used to probe overlapping synthetic peptides covering this region. A pentapeptide, QYPAL, and a hexapeptide, QYPALT (amino acids 259-264), preferentially bound both MAbs. MAb F10 also reacted with a heptapeptide (TAEIFNV) immediately adjacent to QYPALT. The MAbs were also used to affinity-purify fusion phages from a random hexapeptide library. All phage peptides selected were similar to QYPALT. Comparison of the peptides suggested that residues Q and P at positions 1 and 3 were critical for recognition. Some affinity-purified phages displayed the hexapeptide QYPSLL, which is similar to a sequence in VP7 of another orbivirus, epizootic hemorrhagic disease virus. This finding allowed a potentially cross-reactive site to be identified.
Url:
DOI: 10.1006/viro.1994.1039
Affiliations:
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Bag 24, Geelong, Victoria 3220</wicri:regionArea><wicri:noRegion>Victoria 3220</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994">1994</date><biblScope unit="volume">198</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="346">346</biblScope><biblScope unit="page" to="349">349</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Two complementary techniques have been used to delineate an epitope on VP7 of bluetongue virus. Two MAbs (F10 and D11), both of which bound within a region spanning amino acids 255 to 274 in the 349 amino acid protein, were used to probe overlapping synthetic peptides covering this region. A pentapeptide, QYPAL, and a hexapeptide, QYPALT (amino acids 259-264), preferentially bound both MAbs. MAb F10 also reacted with a heptapeptide (TAEIFNV) immediately adjacent to QYPALT. The MAbs were also used to affinity-purify fusion phages from a random hexapeptide library. All phage peptides selected were similar to QYPALT. Comparison of the peptides suggested that residues Q and P at positions 1 and 3 were critical for recognition. Some affinity-purified phages displayed the hexapeptide QYPSLL, which is similar to a sequence in VP7 of another orbivirus, epizootic hemorrhagic disease virus. This finding allowed a potentially cross-reactive site to be identified.</div></front></TEI><affiliations><list><country><li>Australie</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Du Plessis, Dion H" sort="Du Plessis, Dion H" uniqKey="Du Plessis D" first="Dion H." last="Du Plessis">Dion H. Du Plessis</name></noRegion><name sortKey="Eaton, Bryan T" sort="Eaton, Bryan T" uniqKey="Eaton B" first="Bryan T." last="Eaton">Bryan T. Eaton</name><name sortKey="Jordaan, Frances A" sort="Jordaan, Frances A" uniqKey="Jordaan F" first="Frances A." last="Jordaan">Frances A. Jordaan</name><name sortKey="Wang, Lin Fa" sort="Wang, Lin Fa" uniqKey="Wang L" first="Lin-Fa" last="Wang">Lin-Fa Wang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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