Abstract
Antigen-specific and major histocompatibility complex (MHC)-restricted recognition by the T cell receptor involves multiple structural contacts over a large molecular surface area. Using a human T cell clone specific for a rubella viral peptide restricted by subsets of HLA DR4 molecules, we identified structurally diverse combinations of peptide-MHC complexes which were functionally equivalent to T cell recognition. Presentation of the rubella-derived peptide on DR4 molecules with an E-74 polymorphism triggered T cell recognition, as did presentation of a single amino acid-substituted peptide in the context of DR4 molecule which lacked the E-74 site. Peptide binding and molecular modeling analysis indicates the structural and functional complementarity of T cell recognition for a specific amino acid side chain, whether contributed by the peptide or by the MHC molecule.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Alleles
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Antigen Presentation*
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Antigens, Viral / immunology*
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Autoantigens / immunology*
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CD4-Positive T-Lymphocytes / immunology*
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CD4-Positive T-Lymphocytes / metabolism
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HLA-DR Antigens / genetics
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HLA-DR4 Antigen / chemistry
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HLA-DR4 Antigen / genetics
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HLA-DR4 Antigen / immunology*
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HLA-DR4 Antigen / metabolism
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HLA-DRB1 Chains
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Humans
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Lymphocyte Activation
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Models, Molecular
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Mutagenesis, Site-Directed
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Peptide Fragments / immunology*
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Peptide Fragments / metabolism
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Protein Binding
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Protein Conformation
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Receptors, Antigen, T-Cell, alpha-beta / immunology*
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Receptors, Antigen, T-Cell, alpha-beta / metabolism
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Rubella / immunology*
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Structure-Activity Relationship
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T-Lymphocytes, Cytotoxic / immunology*
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T-Lymphocytes, Cytotoxic / metabolism
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Viral Envelope Proteins / chemistry
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Viral Envelope Proteins / immunology*
Substances
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Antigens, Viral
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Autoantigens
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HLA-DR Antigens
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HLA-DR4 Antigen
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HLA-DRB1 Chains
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Peptide Fragments
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Receptors, Antigen, T-Cell, alpha-beta
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Viral Envelope Proteins
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E1 envelope protein, Rubella virus