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

Christiane Habich; Karina Kempe; Volker Burkart; Ruurd Van Der Zee; Mark Lillicrap; Hill Gaston; Hubert Kolb

doi:10.1016/j.febslet.2004.05.010

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

FEBS Lett. 2004 Jun 18;568(1-3):65-9. doi: 10.1016/j.febslet.2004.05.010.

Authors

Christiane Habich¹, Karina Kempe, Volker Burkart, Ruurd Van Der Zee, Mark Lillicrap, Hill Gaston, Hubert Kolb

Affiliation

¹ German Diabetes Research Institute, Leibniz Institute at the Heinrich-Heine-University of Düsseldorf, D-40225 Düsseldorf, Germany. christiane.habich@ddfi.uni-duesseldorf.de

PMID: 15196922
DOI: 10.1016/j.febslet.2004.05.010

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Cell Line
Chaperonin 60 / immunology*
Chaperonin 60 / metabolism
Epitopes / immunology*
Macrophages / immunology*
Mice
Protein Binding
Receptors, Cell Surface / metabolism*

Substances

Chaperonin 60
Epitopes
Receptors, Cell Surface