Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry (Reprinted from Science, vol 255, March 6, 1992)

被引:1124
作者
Hunt, Donald F.
Henderson, Robert A.
Shabanowitz, Jeffrey
Sakaguchi, Kazuyasu
Michel, Hanspeter
Sevilir, Noelle
Cox, Andrea L.
Appella, Ettore
Engelhard, Victor H.
机构
[1] Univ Virginia, Dept Chem, Charlottesville, VA 22903 USA
[2] Univ Virginia, Sch Med, Dept Microbiol, Charlottesville, VA 22908 USA
[3] Univ Virginia, Sch Med, Beirne Carter Ctr Immunol Res, Charlottesville, VA 22908 USA
[4] NCI, Cell Biol Lab, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1126/science.1546328
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
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 peptidcs from small quantities of vitally infected and transformed cells as well as those associated with autoinumme disease states.
引用
收藏
页码:2669 / 2671
页数:3
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