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Please use this identifier to cite or link to this item: http://bura.brunel.ac.uk/handle/2438/3272

Title: Interaction of the globular domain of human C1q with Salmonella typhimurium lipopolysaccharide
Authors: Roumenina, LT
Popov, KT
Bureeva, SV
Kojouharova, MS
Gadjeva, M
Rabheru, S
Thakrar, R
Kaplun, A
Kishore, U
Keywords: Salmonella lipopolysaccharide
IgG
Ca2+
Recognition
Publication Date: 2008
Publisher: American Chemical Society
Citation: Biochemistry 47: 13093–13102, 2008
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.
URI: http://bura.brunel.ac.uk/handle/2438/3272
ISSN: 0006-2960
Appears in Collections:Health
School of Health Sciences and Social Care Research Papers
Biosciences

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