A peptide from heat shock protein 60 is the dominant peptide bound to Qa-1 in the absence of the MHC class Ia leader sequence peptide QDM

被引:51
作者
Davies, A
Kalb, S
Liang, BT
Aldrich, CJ
Lemonnier, FA
Jiang, H
Cotter, R
Soloski, MJ
机构
[1] Johns Hopkins Univ, Sch Med, Dept Med, Baltimore, MD 21205 USA
[2] Johns Hopkins Univ, Sch Med, Dept Pharmacol & Mol Sci, Baltimore, MD 21205 USA
[3] Columbia Univ, Coll Phys & Surg, Dept Med, New York, NY 10032 USA
[4] Indiana Univ Sch Med, Evansville Ctr, Dept Microbiol & Immunol, Evansville, IN 47712 USA
[5] Inst Pasteur, Unite Immun Cellulaire Antivirale, Dept SIDA Retrovirus, Paris, France
关键词
D O I
10.4049/jimmunol.170.10.5027
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
The MHC class Ib molecule Qa-1 binds specifically and predominantly to a single 9-aa peptide (AMAPRTLLL) derived from the leader sequence of many MHC class la proteins. This peptide is referred to as Qdm. In this study, we report the isolation and sequencing of a heat shock protein 60-derived peptide (GMKFDRGYI) from Qa-1. This peptide is the dominant peptide bound to Qa-1 in the absence of Qdm. A Qa-1-restricted CTL clone recognizes this heat shock protein 60 peptide, further verifying that it binds to Qa-1 and a peptide from the homologous Salmonella typhimurium protein GroEL (GMQFDRGYL). These observations have implications for how Qa-1 can influence NK cell and T cell effector function via the TCR and CD94/NKG2 family members, and how this effect can change under conditions that cause the peptides bound to Qa-1 to change.
引用
收藏
页码:5027 / 5033
页数:7
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