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 |
Issue 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: | Biological Sciences Community Health and Public Health Dept of Life Sciences Research Papers |
Files in This Item:
File | Description | Size | Format | |
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Closed+Access+Paper.txt | 297 B | Text | View/Open |
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