Invariant chain peptides in most HLA-DR molecules of an antigen-processing mutant

Alessandro Sette, Stephanie Ceman, Ralph T. Kubo, Kazuyasu Sakaguchi, Ettore Appella, Donald F. Hunt, Theresa A. Davis, Hanspeter Michel, Jeffrey Shabanowitz, Richard Rudersdorf, Howard M. Grey, Robert DeMars

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Abstract

Class II major histocompatibility complexes bind peptides in an endosome-like compartment. When the class II null cell line 721.174 was transferred 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.

Original languageEnglish (US)
Pages (from-to)1801-1804
Number of pages4
JournalScience
Volume258
Issue number5089
DOIs
StatePublished - 1992

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    Sette, A., Ceman, S., Kubo, R. T., Sakaguchi, K., Appella, E., Hunt, D. F., Davis, T. A., Michel, H., Shabanowitz, J., Rudersdorf, R., Grey, H. M., & DeMars, R. (1992). Invariant chain peptides in most HLA-DR molecules of an antigen-processing mutant. Science, 258(5089), 1801-1804. https://doi.org/10.1126/science.1465617