Identification of the heat shock protein 60 epitope involved in receptor binding on macrophages.
In the present study, we identified the human heat shock protein 60 (HSP60) 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 HSP60, 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.
Habich
Christiane
C
German Diabetes Research Institute, Leibniz Institute at the Heinrich-Heine-University of Düsseldorf, D-40225 Düsseldorf, Germany. christiane.habich@ddfi.uni-duesseldorf.de
Kempe
Karina
K
Burkart
Volker
V
Van Der Zee
Ruurd
R
Lillicrap
Mark
M
Gaston
Hill
H
Kolb
Hubert
H
D000818:Animals; D002460:Cell Line; D018834:Chaperonin 60 / Q000276:immunology* / Q000378:metabolism; D000939:Epitopes / Q000276:immunology*; D008264:Macrophages / Q000276:immunology*; D051379:Mice; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000378:metabolism*
D018834:Chaperonin 60; D000939:Epitopes; D011956:Receptors, Cell Surface