Peptide binding to empty HLA-B27 molecules of viable human cells View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-05

AUTHORS

R J Benjamin, J A Madrigal, P Parham

ABSTRACT

Intracellular binding of antigenic peptides by polymorphic class I major histocompatibility complex molecules creates the ligands recognized by receptors of CD8+ T cells. Previously described in vitro assays of peptide binding to class I molecules have been limited by either the low proportion of accessible binding sites or the lack of allelic specificity. Here we describe a system in which the human class I molecule HLA-B27 binds considerable amounts of an influenza peptide with precise allelic discrimination. Binding requires viable cells, is stimulated by gamma-interferon and is inhibited by brefeldin A. Our results are consistent with the presence of fairly stable 'empty' HLA-B27 molecules at the cell surface. By contrast, analysis of the binding of a second influenza peptide indicates that empty HLA-Aw68 molecules are relatively short-lived. We speculate that HLA-B27 might bind extracellular peptides in vivo and that this property could underlie its association with autoimmune disease. More... »

PAGES

74-77

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/351074a0

DOI

http://dx.doi.org/10.1038/351074a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1002566833

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2027387


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