Apparent lack of MHC restriction in binding of class I HLA molecules to solid-phase peptides.
J Exp Med
; 172(3): 931-6, 1990 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-1696957
ABSTRACT
The specificity of binding of solubilized, purified HLA-A,B molecules to solid-phase peptides has been examined using the assay described by Bouillet et al. [1989. Nature (Lond.). 339473.] 64 peptides derived from the sequences of viral antigens, HLA-A,B,C heavy chains, and clathrin light chains were tested for binding to HLA-A2.1, Aw68.1, Aw69, B44, and B5, molecules that differ by 5-17 residues of the peptide binding groove. 15 of the peptides, including those known to be T cell epitopes, gave significant binding. The pattern of peptide binding for each of the five HLA-A,B molecules was not significantly different. Binding was demonstrated to be a property of native beta 2m-associated HLA-A,B molecules that preserved conformational antigenic determinants after binding to peptide. In comparison to our previous results from solution-based assays the proportion of HLA-A,B molecules that can bind solid-phase peptides is very high. This accessibility of solid-phase peptides to the binding site of MHC molecules may be directly related to the observed absence of MHC specificity in the binding.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Antígenos HLA-A
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Antígenos HLA-B
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Antígenos HLA-C
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Complexo Principal de Histocompatibilidade
Limite:
Humans
Idioma:
En
Revista:
J Exp Med
Ano de publicação:
1990
Tipo de documento:
Article