Complexity among constituents of the HLA-B*1501 peptide motif
Identifieur interne : 001392 ( Istex/Checkpoint ); précédent : 001391; suivant : 001393Complexity among constituents of the HLA-B*1501 peptide motif
Auteurs : Kiley R. Prilliman [États-Unis] ; Mark Lindsey [États-Unis] ; Kenneth W. Jackson [États-Unis] ; Jeffrey Cole [États-Unis] ; Ron Bonner [États-Unis] ; W. H. Hildebrand [États-Unis]Source :
- Immunogenetics [ 0093-7711 ] ; 1998-06-01.
English descriptors
Abstract
Abstract: Analysis of peptides derived from HLA class I molecules indicates that thousands of unique peptides are bound by a single molecular type, and sequence examination of the pooled constituents yields a motif which collectively defines the peptides bound by a given class I molecule. Motifs resulting from pooled sequencing are then used to infer whether particular viral and tumor protein fragments might serve as class I-presented peptide therapeutics. Still undetermined from a pooled motif is the breadth or range of peptides in the population which are brought together to form the pooled motif, and it is therefore not yet known how representative of the population a pooled motif is. By employing hollow fiber bioreactors for large-scale production of HLA class I molecules, sufficient peptides are produced to investigate individual subsets of peptides comprising a motif. Edman sequencing and mass spectrometric analysis of peptides eluted from HLA-B*1501 reveal that many peptide sequences fail to align with either the N- or C-terminal anchors predicted for the B*1501 peptide motif through whole pool sequencing. These analyses further reveal auxiliary anchors not previously detected and peptides significantly larger and smaller than the predicted nonamer, ranging from 6 to 12 amino acids in length. These results demonstrate that constituents of the B*1501 peptide pool vary markedly in comparison with one another and therefore in comparison with previously established B*1501 motifs, and such complexity indicates that many of the peptide ligands presented to CTL cannot be predicted using class I consensus motifs as search criteria.
Url:
DOI: 10.1007/s002510050408
Affiliations:
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Hildebrand</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73190, USA</wicri:regionArea><wicri:noRegion>USA</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Immunogenetics</title><title level="j" type="abbrev">Immunogenetics</title><idno type="ISSN">0093-7711</idno><idno type="eISSN">1432-1211</idno><imprint><publisher>Springer-Verlag</publisher><pubPlace>Berlin/Heidelberg</pubPlace><date type="published" when="1998-06-01">1998-06-01</date><biblScope unit="volume">48</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="89">89</biblScope><biblScope unit="page" to="97">97</biblScope></imprint><idno type="ISSN">0093-7711</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0093-7711</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antigen presentation</term><term>Key words HLA-Bantigens</term><term>Ligands</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Analysis of peptides derived from HLA class I molecules indicates that thousands of unique peptides are bound by a single molecular type, and sequence examination of the pooled constituents yields a motif which collectively defines the peptides bound by a given class I molecule. Motifs resulting from pooled sequencing are then used to infer whether particular viral and tumor protein fragments might serve as class I-presented peptide therapeutics. Still undetermined from a pooled motif is the breadth or range of peptides in the population which are brought together to form the pooled motif, and it is therefore not yet known how representative of the population a pooled motif is. By employing hollow fiber bioreactors for large-scale production of HLA class I molecules, sufficient peptides are produced to investigate individual subsets of peptides comprising a motif. Edman sequencing and mass spectrometric analysis of peptides eluted from HLA-B*1501 reveal that many peptide sequences fail to align with either the N- or C-terminal anchors predicted for the B*1501 peptide motif through whole pool sequencing. These analyses further reveal auxiliary anchors not previously detected and peptides significantly larger and smaller than the predicted nonamer, ranging from 6 to 12 amino acids in length. These results demonstrate that constituents of the B*1501 peptide pool vary markedly in comparison with one another and therefore in comparison with previously established B*1501 motifs, and such complexity indicates that many of the peptide ligands presented to CTL cannot be predicted using class I consensus motifs as search criteria.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><country name="États-Unis"><noRegion><name sortKey="Prilliman, Kiley R" sort="Prilliman, Kiley R" uniqKey="Prilliman K" first="Kiley R." last="Prilliman">Kiley R. Prilliman</name></noRegion><name sortKey="Bonner, Ron" sort="Bonner, Ron" uniqKey="Bonner R" first="Ron" last="Bonner">Ron Bonner</name><name sortKey="Cole, Jeffrey" sort="Cole, Jeffrey" uniqKey="Cole J" first="Jeffrey" last="Cole">Jeffrey Cole</name><name sortKey="Hildebrand, W H" sort="Hildebrand, W H" uniqKey="Hildebrand W" first="W. H." last="Hildebrand">W. H. Hildebrand</name><name sortKey="Jackson, Kenneth W" sort="Jackson, Kenneth W" uniqKey="Jackson K" first="Kenneth W." last="Jackson">Kenneth W. Jackson</name><name sortKey="Lindsey, Mark" sort="Lindsey, Mark" uniqKey="Lindsey M" first="Mark" last="Lindsey">Mark Lindsey</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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