Interaction of the globular domain of human C1q with Salmonella typhimurium lipopolysaccharide.
Biochim Biophys Acta
; 1784(9): 1271-6, 2008 Sep.
Article
em En
| MEDLINE
| ID: mdl-18513495
ABSTRACT
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. LPS 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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Complemento C1q
/
Lipopolissacarídeos
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article
País de afiliação:
Bulgária