Heat shock protein 60: identification of specific epitopes for binding to primary macrophages.
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.
Habich
Christiane
C
German Diabetes Clinic, German Diabetes Center, Leibniz Institute, Heinrich-Heine-University of Düsseldorf, D-40225 Düsseldorf, Germany. christiane.habich@ddz.uni-duesseldorf.de
Kempe
Karina
K
Gomez
Francisco J
FJ
Lillicrap
Mark
M
Gaston
Hill
H
van der Zee
Ruurd
R
Kolb
Hubert
H
Burkart
Volker
V
D000818:Animals; D001426:Bacterial Proteins / Q000276:immunology* / Q000378:metabolism; D001854:Bone Marrow Cells / Q000166:cytology / Q000276:immunology* / Q000378:metabolism; D002460:Cell Line; D018834:Chaperonin 60 / Q000276:immunology*; D000939:Epitopes / Q000276:immunology* / Q000378:metabolism; D006658:Histoplasma / Q000276:immunology* / Q000378:metabolism; D006801:Humans; D008264:Macrophages / Q000166:cytology / Q000276:immunology* / Q000378:metabolism; D051379:Mice; D011485:Protein Binding / Q000276:immunology; D013045:Species Specificity
D001426:Bacterial Proteins; D018834:Chaperonin 60; D000939:Epitopes