期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1784, 期 9, 页码 1271-1276出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2008.04.029
关键词
C1q; Salmonella lipopolysaccharide; IgG; Ca2+; recognition
资金
- EMBO
- FEBS
- Brunel University's BRIEF
- Human Immunology and Infection Biology
Gram-negative bacteria can bind complement protein C1q in an antibody-independent manner and activate classical pathway via their lipopolysaccharides (LPS). Earlier studies have implicated the collagen-like region of human C1q in binding LPS. In recent years, a number of C1q target molecules, previously considered to interact with collagen-like region of C1q, have been shown to bind via the globular domain (gC1q). Here we report, using recombinant forms of the globular head regions of C1q A, B and C chains, that LPS derived from Salmonella typhimurium interact specifically with the B-chain of the gC1q domain in a calcium-dependent manner. LIPS and IgG-binding sites on the gC1q domain appear to be overlapping and this interaction can be inhibited by a synthetic C1q inhibitor, suggesting common interacting mechanisms. (c) 2008 Elsevier B.V. All rights reserved.
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