Identification of the heat shock protein 60 epitope involved in receptor binding on macrophages

被引:22
作者
Habich, C [1 ]
Kempe, K
Burkart, V
van der Zee, R
Lillicrap, M
Gaston, H
Kolb, H
机构
[1] Univ Dusseldorf, Leibniz Inst, Geman Diabet Res Inst, D-40225 Dusseldorf, Germany
[2] Univ Utrecht, Fac Med, Dept Infect Dis & Immunol, NL-3508 TD Utrecht, Netherlands
[3] Univ Cambridge, Dept Med, Cambridge CB2 2QQ, England
关键词
heat shock protein 60; binding epitope; receptor; macrophage;
D O I
10.1016/j.febslet.2004.05.010
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 identified the human beat shock protein 60 (FISP60) epitope responsible for binding to macrophages. Studies using overlapping 15- and 20-mer peptides of the human HSP60 sequence to compete with binding of HSP60 to macrophages indicated that surface binding was accounted for by the region aa481-500. Deletion mutants of FISP60, lacking the N-terminal 137, 243 or 359 amino acids, strongly inhibited HSP60 binding to macrophages. Monoclonal antibodies addressing regions aa1-200, aa335-366 or aa383-447 did not block HSP60 binding. We conclude that a single C-terminal region, aa481-500, accounts for the binding of HSP60 to macrophages. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:65 / 69
页数:5
相关论文
共 23 条
[1]   T cell proliferative responses of type 1 diabetes patients and healthy individuals to human hsp60 and its peptides [J].
Abulafia-Lapid, R ;
Elias, D ;
Raz, I ;
Keren-Zur, Y ;
Atlan, H ;
Cohen, IR .
JOURNAL OF AUTOIMMUNITY, 1999, 12 (02) :121-129
[2]   HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine [J].
Asea, A ;
Kraeft, SK ;
Kurt-Jones, EA ;
Stevenson, MA ;
Chen, LB ;
Finberg, RW ;
Koo, GC ;
Calderwood, SK .
NATURE MEDICINE, 2000, 6 (04) :435-442
[3]  
Ausubel FM, 1995, CURRENT PROTOCOLS MO
[4]   CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin [J].
Basu, S ;
Binder, RJ ;
Ramalingam, T ;
Srivastava, PK .
IMMUNITY, 2001, 14 (03) :303-313
[5]   CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes [J].
Becker, T ;
Hartl, FU ;
Wieland, F .
JOURNAL OF CELL BIOLOGY, 2002, 158 (07) :1277-1285
[6]   CD91: a receptor for heat shock protein gp96 [J].
Binder, RJ ;
Han, DK ;
Srivastava, PK .
NATURE IMMUNOLOGY, 2000, 1 (02) :151-155
[7]   Saturation, competition, and specificity in interaction of heat shock proteins (hsp) gp96, hsp90, and hsp70 with CD11b+ cells [J].
Binder, RJ ;
Harris, ML ;
Ménoret, A ;
Srivastava, PK .
JOURNAL OF IMMUNOLOGY, 2000, 165 (05) :2582-2587
[8]  
Chen W, 1999, J IMMUNOL, V162, P3212
[9]   Chaperone-mediated protein folding [J].
Fink, AL .
PHYSIOLOGICAL REVIEWS, 1999, 79 (02) :425-449
[10]   Human heat shock protein 60 induces maturation of dendritic cells versus a Th1-promoting phenotype [J].
Flohé, SB ;
Brüggemann, J ;
Lendemans, S ;
Nikulina, M ;
Meierhoff, G ;
Flohé, S ;
Kolb, H .
JOURNAL OF IMMUNOLOGY, 2003, 170 (05) :2340-2348