Identification of conformational epitopes for human IgG on Chemotaxis inhibitory protein of Staphylococcus aureus.

ABSTRACT:

Background

The Chemotaxis inhibitory protein of Staphylococcus aureus (CHIPS) blocks the Complement fragment C5a receptor (C5aR) and formylated peptide receptor (FPR) and is thereby a potent inhibitor of neutrophil chemotaxis and activation of inflammatory responses. The majority of the healthy human population has antibodies against CHIPS that have been shown to interfere with its function in vitro. The aim of this study was to define potential epitopes for human antibodies on the CHIPS surface. We also initiate the process to identify a mutated CHIPS molecule that is not efficiently recognized by preformed anti-CHIPS antibodies and retains anti-inflammatory activity.

Results

In this paper, we panned peptide displaying phage libraries against a pool of CHIPS specific affini

SUBMITTER: Gustafsson E 

PROVIDER: S-EPMC2662796 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature