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Science 11 December 1992:
Vol. 258. no. 5089, pp. 1801 - 1804
DOI: 10.1126/science.1465617
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Articles
Science, Vol 258, Issue 5089, 1801-1804
Copyright © 1992 by American Association for the Advancement of Science
Invariant chain peptides in most HLA-DR molecules of an antigen-processing mutant
A Sette,
S Ceman,
RT Kubo,
K Sakaguchi,
E Appella,
DF Hunt,
TA Davis,
H Michel,
J Shabanowitz,
R Rudersdorf,
and
al. et
Laboratory of Genetics, University of Wisconsin, Madison 53706.
Class II major histocompatibility complexes bind peptides in an endosome-like compartment. When the class II null cell line 721.174 was transfected with class II DR3 genes, DR molecules were produced in normal amounts. However, the DR molecules were abnormally conformed and unstable because deletion of an antigen-processing gene had impaired intracellular formation of most class II-peptide complexes. Yet, 70 percent of the DR molecules still bore peptides, 80 percent of which were 21- to 24-amino acid fragments of the class II-associated invariant chain. These peptides were rare on DR3 from control cells. Thus, a defect in the main antigen-processing pathway revealed a process in which DR molecules bind long peptides derived from proteins present in the same compartment.
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