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Science 7 December 1990:
Vol. 250. no. 4986, pp. 1423 - 1426
DOI: 10.1126/science.2124002
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Articles

Science, Vol 250, Issue 4986, 1423-1426
Copyright © 1990 by American Association for the Advancement of Science

articles

The role of beta 2-microglobulin in peptide binding by class I molecules

A Vitiello, TA Potter, and LA Sherman

Cytel Corporation, La Jolla, CA 92037.

Efficient transport of class I major histocompatibility complex molecules to the cell surface requires association of the class I heavy chain with endogenous peptide and the class I light chain, beta 2-microglobulin (beta 2M). A mutant cell line deficient in beta 2M transports low amounts of nonpeptide-associated heavy chains to the cell surface that can associate with exogenously provided beta 2M and synthetic peptide antigens. Normal beta 2M-sufficient cells grown in serum-free media devoid of beta 2M also require an exogenous source of beta 2M to efficiently bind synthetic peptide. Thus, class I molecules on normal cells do not spontaneously bind or exchange peptides.


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