Interaction of the globular domain of human C1q with Salmonella typhimurium lipopolysaccharide

Lubka T. Roumenina, Krustyo T. Popov, Svetlana V. Bureeva, Mihaela Kojouharova, Mihaela Gadjeva, Shweta Rabheru, Roshni Thakrar, Alexander Kaplun, Uday Kishore

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1271-1276
Number of pages6
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1784
Issue number9
DOIs
Publication statusPublished - Sept 2008
Externally publishedYes

Keywords

  • C1q
  • Ca
  • IgG
  • Recognition
  • Salmonella lipopolysaccharide

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology

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