Abstract
Peptides which bind to human HLA-DRB1 class II molecules in an allele-specific fashion were derived from the immunodominant E1 envelope protein of rubella virus. Two nonoverlapping E1 peptide epitopes were recognized by rubella virus-specific T cells in the context of independent HLA alleles when presented either separately or as a contiguous polypeptide containing both epitopes. Direct binding analysis of potential peptide epitopes to distinct HLA molecules provides a direct approach for selecting antigenic peptides useful for epitope-based vaccine targeted to multiple HLA types.
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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CD4-Positive T-Lymphocytes / immunology*
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Cell Line, Transformed
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Epitope Mapping
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Epitopes, T-Lymphocyte / genetics
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Epitopes, T-Lymphocyte / immunology
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HLA-DR Antigens / immunology*
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HLA-DRB1 Chains
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Humans
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Immunodominant Epitopes / genetics
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Immunodominant Epitopes / immunology
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Peptides / chemical synthesis
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Rubella virus / genetics
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Rubella virus / immunology*
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Viral Envelope Proteins / genetics
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Viral Envelope Proteins / immunology*
Substances
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Epitopes, T-Lymphocyte
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HLA-DR Antigens
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HLA-DRB1 Chains
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Immunodominant Epitopes
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Peptides
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Viral Envelope Proteins
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E1 envelope protein, Rubella virus