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Science 6 March 1992:
Vol. 255. no. 5049, pp. 1261 - 1263
DOI: 10.1126/science.1546328

Articles

Science, Vol 255, Issue 5049, 1261-1263
Copyright © 1992 by American Association for the Advancement of Science


articles

Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry

DF Hunt, RA Henderson, J Shabanowitz, K Sakaguchi, H Michel, N Sevilir, AL Cox, E Appella, and VH Engelhard

Department of Chemistry, University of Virginia, Charlottesville 22903.

Antigens recognized by T cells are expressed as peptides bound to major histocompatibility complex (MHC) molecules. Microcapillary high-performance liquid chromatography-electrospray ionization-tandem mass spectrometry was used to fractionate and sequence subpicomolar amounts of peptides isolated from the MHC molecule HLA-A2.1. Of 200 different species quantitated, eight were sequenced and four were found in cellular proteins. All were nine residues long and shared a distinct structural motif. The sensitivity and speed of this approach should enhance the analysis of peptides from small quantities of virally infected and transformed cells as well as those associated with autoimmune disease states.





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Science. ISSN 0036-8075 (print), 1095-9203 (online)