HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes
Identifieur interne : 004348 ( Main/Exploration ); précédent : 004347; suivant : 004349HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes
Auteurs : Xin-Ting Fu [États-Unis] ; Robert W. Karr [États-Unis]Source :
- Human Immunology [ 0198-8859 ] ; 1994.
English descriptors
- Teeft :
- Andrea sant, Cdna, Cell line, Chain residues, Cham, Channel fluorescence, Clone, Crystal structure, Direct contact, Drot, Drot chain, Drot cham, Drot residues, Epitope, Epltopes, Expressmn vector, Groove, Heddy zola, Human class, Hybrid molecules, Immunol, Karr, Lechler, Less hkely, Mabs, Molecule, Molecules implications, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Mutant, Outer loops, Outer surface, Polymorphic, Polymorphic chain residues, Polymorphlc, Residue, Robert lechler, Sanna goyert, Several residues, Side chain, Soldano ferrone, Stefan carrel, Superantlgen binding, Toxin, Transfectants.
Abstract
Abstract: The structure-function relationships of the HLA-DRα chain have been analyzed by identifying DRα residues involved in several nonpolymorphic and polymorphic antibody epitopes. Antibody binding to transfectants expressing a WT or mutant DRα chain with the WT DR (β1∗0701) chain was analyzed. Our results indicate that residues 18, 36, and 39 located on the outer loops of the DRα chain are critical for one of more of the epitopes recognized by the SG157, Q2/70, L243, LB3. 1, D1-12, and CL413 mAbs. Similar results were obtained when the DRα position 18 and 39 mutants were expressed with other DRβ1 allesles. Furthermore, residues 15 and 18 of the DRα chain were shown to be involved in the epitopes of two polymorphic mAbs, HU-26 and I-2, whose epitopes also include residue 4 of the corresponding DRβ chains. In addition to their involvement in antibody-binding epitopes, residues in this region on the outer surface of the DRα chain have also been shown to be involved in superantigen binding and presentation and T-cell recognition of foreign antigen, emphasizing the functional importance of DRα-chain residues located outside of the peptide-binding groove.
Url:
DOI: 10.1016/0198-8859(94)90268-2
Affiliations:
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes</title><author><name sortKey="Fu, Xin Ting" sort="Fu, Xin Ting" uniqKey="Fu X" first="Xin-Ting" last="Fu">Xin-Ting Fu</name></author><author><name sortKey="Karr, Robert W" sort="Karr, Robert W" uniqKey="Karr R" first="Robert W." last="Karr">Robert W. 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Karr</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri</wicri:regionArea><placeName><region type="state">Missouri (État)</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Human Immunology</title><title level="j" type="abbrev">HIM</title><idno type="ISSN">0198-8859</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994">1994</date><biblScope unit="volume">39</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="253">253</biblScope><biblScope unit="page" to="260">260</biblScope></imprint><idno type="ISSN">0198-8859</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0198-8859</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Andrea sant</term><term>Cdna</term><term>Cell line</term><term>Chain residues</term><term>Cham</term><term>Channel fluorescence</term><term>Clone</term><term>Crystal structure</term><term>Direct contact</term><term>Drot</term><term>Drot chain</term><term>Drot cham</term><term>Drot residues</term><term>Epitope</term><term>Epltopes</term><term>Expressmn vector</term><term>Groove</term><term>Heddy zola</term><term>Human class</term><term>Hybrid molecules</term><term>Immunol</term><term>Karr</term><term>Lechler</term><term>Less hkely</term><term>Mabs</term><term>Molecule</term><term>Molecules implications</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal antibody</term><term>Mutant</term><term>Outer loops</term><term>Outer surface</term><term>Polymorphic</term><term>Polymorphic chain residues</term><term>Polymorphlc</term><term>Residue</term><term>Robert lechler</term><term>Sanna goyert</term><term>Several residues</term><term>Side chain</term><term>Soldano ferrone</term><term>Stefan carrel</term><term>Superantlgen binding</term><term>Toxin</term><term>Transfectants</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The structure-function relationships of the HLA-DRα chain have been analyzed by identifying DRα residues involved in several nonpolymorphic and polymorphic antibody epitopes. Antibody binding to transfectants expressing a WT or mutant DRα chain with the WT DR (β1∗0701) chain was analyzed. Our results indicate that residues 18, 36, and 39 located on the outer loops of the DRα chain are critical for one of more of the epitopes recognized by the SG157, Q2/70, L243, LB3. 1, D1-12, and CL413 mAbs. Similar results were obtained when the DRα position 18 and 39 mutants were expressed with other DRβ1 allesles. Furthermore, residues 15 and 18 of the DRα chain were shown to be involved in the epitopes of two polymorphic mAbs, HU-26 and I-2, whose epitopes also include residue 4 of the corresponding DRβ chains. In addition to their involvement in antibody-binding epitopes, residues in this region on the outer surface of the DRα chain have also been shown to be involved in superantigen binding and presentation and T-cell recognition of foreign antigen, emphasizing the functional importance of DRα-chain residues located outside of the peptide-binding groove.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Missouri (État)</li></region></list><tree><country name="États-Unis"><region name="Missouri (État)"><name sortKey="Fu, Xin Ting" sort="Fu, Xin Ting" uniqKey="Fu X" first="Xin-Ting" last="Fu">Xin-Ting Fu</name></region><name sortKey="Karr, Robert W" sort="Karr, Robert W" uniqKey="Karr R" first="Robert W." last="Karr">Robert W. Karr</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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