Extension of a minimal T cell Determinant allows relaxation of the requirement for particular residues within the determinant
Identifieur interne : 004937 ( Main/Exploration ); précédent : 004936; suivant : 004938Extension of a minimal T cell Determinant allows relaxation of the requirement for particular residues within the determinant
Auteurs : Lorena E. Brown [Australie] ; David C. Jackson [Australie] ; Gordon Tribbick [Australie] ; David O. White [Australie] ; H. Mario Geysen [Australie]Source :
- International Immunology [ 0953-8178 ] ; 1991.
Abstract
The determinant recognized by a class II restricted helper T cell clone raised against a peptide corresponding to the C-terminal 24 residues of the heavy chain of influenza virus hemagglutinin (HA) was examined in detail. The sequence 309VKQNTLKL316 was identified as the minimal determinant for T cell activation but its stimulatory capacity was augmented by extension at either end. Sets of peptide analogs, in which each residue within the minimal determinant was replaced in turn by every one of the other naturally occurring amino acids, revealed either an absolute requirement for the native residue or a very limited degree of replaceability, at seven of the eight positions. Only the N-terminal residue 309V could be replaced with almost any other amino acid without loss of reactivity; in fact, substitution at this position with residues containing bulky side groups enhanced the response. The reactivity of the clone with analogs of the longer peptide 307KYVKQNTLKL316, which induces maximal levels of stimulation, revealed a very different pattern of replaceability for certain residues; in particular, the requirement for a lysine at position 310 was no longer apparent. This study presents a complete analysis of the importance of each individual residue to the integrity of a T cell determinant and provides evidence that the critical requirement for a particular amino acid at a given location may be overridden by N-terminal extension of the minimal determinant. These findings indicate that, within different homologs of the native sequence, particular residues may assume quite different roles.
Url:
DOI: 10.1093/intimm/3.12.1307
Affiliations:
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Brown</name><affiliation wicri:level="4"><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052, Australia, Victoria 3168</wicri:regionArea><orgName type="university">Université de Melbourne</orgName><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></affiliation><affiliation></affiliation></author><author><name sortKey="Jackson, David C" sort="Jackson, David C" uniqKey="Jackson D" first="David C." last="Jackson">David C. Jackson</name><affiliation wicri:level="4"><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052, Australia, Victoria 3168</wicri:regionArea><orgName type="university">Université de Melbourne</orgName><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></affiliation></author><author><name sortKey="Tribbick, Gordon" sort="Tribbick, Gordon" uniqKey="Tribbick G" first="Gordon" last="Tribbick">Gordon Tribbick</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Coselco Mimotopes Pty Ltd, Clayton Victoria 3168</wicri:regionArea><wicri:noRegion>Clayton Victoria 3168</wicri:noRegion></affiliation></author><author><name sortKey="White, David O" sort="White, David O" uniqKey="White D" first="David O." last="White">David O. 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Mario Geysen</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Coselco Mimotopes Pty Ltd, Clayton Victoria 3168</wicri:regionArea><wicri:noRegion>Clayton Victoria 3168</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">International Immunology</title><idno type="eISSN">1460-2377</idno><idno type="ISSN">0953-8178</idno><imprint><publisher>Oxford University Press</publisher><date type="published">1991</date><biblScope unit="vol">3</biblScope><biblScope unit="issue">12</biblScope><biblScope unit="page" from="1307">1307</biblScope><biblScope unit="page" to="1313">1313</biblScope></imprint><idno type="ISSN">0953-8178</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0953-8178</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">The determinant recognized by a class II restricted helper T cell clone raised against a peptide corresponding to the C-terminal 24 residues of the heavy chain of influenza virus hemagglutinin (HA) was examined in detail. The sequence 309VKQNTLKL316 was identified as the minimal determinant for T cell activation but its stimulatory capacity was augmented by extension at either end. Sets of peptide analogs, in which each residue within the minimal determinant was replaced in turn by every one of the other naturally occurring amino acids, revealed either an absolute requirement for the native residue or a very limited degree of replaceability, at seven of the eight positions. Only the N-terminal residue 309V could be replaced with almost any other amino acid without loss of reactivity; in fact, substitution at this position with residues containing bulky side groups enhanced the response. The reactivity of the clone with analogs of the longer peptide 307KYVKQNTLKL316, which induces maximal levels of stimulation, revealed a very different pattern of replaceability for certain residues; in particular, the requirement for a lysine at position 310 was no longer apparent. This study presents a complete analysis of the importance of each individual residue to the integrity of a T cell determinant and provides evidence that the critical requirement for a particular amino acid at a given location may be overridden by N-terminal extension of the minimal determinant. These findings indicate that, within different homologs of the native sequence, particular residues may assume quite different roles.</div></front></TEI><affiliations><list><country><li>Australie</li></country><region><li>Victoria (État)</li></region><settlement><li>Melbourne</li></settlement><orgName><li>Université de Melbourne</li></orgName></list><tree><country name="Australie"><region name="Victoria (État)"><name sortKey="Brown, Lorena E" sort="Brown, Lorena E" uniqKey="Brown L" first="Lorena E." last="Brown">Lorena E. Brown</name></region><name sortKey="Geysen, H Mario" sort="Geysen, H Mario" uniqKey="Geysen H" first="H. Mario" last="Geysen">H. Mario Geysen</name><name sortKey="Jackson, David C" sort="Jackson, David C" uniqKey="Jackson D" first="David C." last="Jackson">David C. Jackson</name><name sortKey="Tribbick, Gordon" sort="Tribbick, Gordon" uniqKey="Tribbick G" first="Gordon" last="Tribbick">Gordon Tribbick</name><name sortKey="White, David O" sort="White, David O" uniqKey="White D" first="David O." last="White">David O. White</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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