Heat shock protein 60: Identification of specific epitopes for binding to primary macrophages

被引：38
作者：
Habich, C [1 ]
Kempe, K
Gomez, FJ
Lillicrap, M
Gaston, H
van der Zee, R
Kolb, H
Burkart, V
机构：
[1] Univ Dusseldorf, Leibniz Inst, German Diabet Ctr, German Diabet Clin, D-40225 Dusseldorf, Germany
[2] Univ Cincinnati, Coll Med, Dept Internal Med, Div Infect Dis, Cincinnati, OH 45267 USA
[3] Univ Cambridge, Dept Med, Cambridge CB2 2QQ, England
[4] Univ Utrecht, Fac Vet Med, Dept Infect Dis & Immunol, NL-3508 TD Utrecht, Netherlands
来源：
FEBS LETTERS | 2006年 / 580卷 / 01期
关键词：
heat shock protein 60; binding epitope; receptor; macrophages;
D O I：
10.1016/j.febslet.2005.11.060
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
In the present study, we characterized regions of human heat shock protein (HSP) 60 responsible for binding to primary macrophages. Studies using 20-mer peptides of the HSP60 sequence to compete with HSP60-binding to macrophages from C57BL/6J mice showed that regions aa241-260, aa391-410 and aa461-480 are involved in surface-binding. HSP60 mutants, lacking the N-terminal 137, 243 or 359 amino acids, inhibited HSP60-binding to primary macrophages to different degrees, demonstrating that all three regions are required for optimal binding. Analysis of different pro- and eukaryotic HSP60 species indicated that phylogenetically separate HSP60 species use different binding sites on primary macrophages. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码：115 / 120
页数：6
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