| Literature DB >> 7680390 |
R S van Binnendijk1, J P Versteeg-van Oosten, M C Poelen, H F Brugghe, P Hoogerhout, A D Osterhaus, F G Uytdehaag.
Abstract
The transmembrane fusion (F) glycoprotein of measles virus is an important target antigen of human HLA class I- and class II-restricted cytotoxic T lymphocytes (CTL). Genetically engineered F proteins and nested sets of synthetic peptides spanning the F protein were used to determine sequences of F recognized by a number of F-specific CTL clones. Combined N- and C-terminal deletions of the respective peptides revealed that human HLA class I and HLA class II-restricted CTL efficiently recognize nonapeptides or decapeptides representing epitopes of F. Three distinct sequences recognized by three different HLA class II (DQw1, DR2, and DR4/w53)-restricted CTL clones appear to cluster between amino acids 379 and 466 of F, thus defining an important T-cell epitope area of F. Within this same region, a nonamer peptide of F was found to be recognized by an HLA-B27-restricted CTL clone, as expected on the basis of the structural homology between this peptide and other known HLA-B27 binding peptides.Entities:
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Year: 1993 PMID: 7680390 PMCID: PMC240367
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103