Recognition of contiguous allele-specific peptide elements in the Rubella virus E1 envelope protein

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 non-overlapping E1 peptide epitopes were recognized by rubella virus-specific T cells in the context of independent HLA alleles when p...

Full description

Saved in:
Bibliographic Details
Published in:Vaccine 1997-04, Vol.15 (6), p.648-652
Main Authors: Nepom, Gerald T., Domeier, Mary Ellen, Ou, Dawei, Kovats, Susan, Mitchell, Leslie Ann, Tingle, Aubrey J.
Format: Article
Language:English
Subjects:
Alleles
Biological and medical sciences
CD4-Positive T-Lymphocytes - immunology
Cell Line, Transformed
class II histocompatibility molecules
Epitope Mapping
Epitopes, T-Lymphocyte - genetics
Epitopes, T-Lymphocyte - immunology
Fundamental and applied biological sciences. Psychology
HLA genes
HLA-DR Antigens - immunology
HLA-DRB1 Chains
Humans
Immunodominant Epitopes - genetics
Immunodominant Epitopes - immunology
Microbiology
peptide vaccines
Peptides - chemical synthesis
rubella virus
Rubella virus - genetics
Rubella virus - immunology
Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies
Viral Envelope Proteins - genetics
Viral Envelope Proteins - immunology
Virology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 non-overlapping 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.
ISSN:0264-410X
1873-2518
DOI:10.1016/S0264-410X(96)00194-6