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DC Field | Value | Language |
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dc.contributor.author | Roumenina, LT | - |
dc.contributor.author | Popov, KT | - |
dc.contributor.author | Bureeva, SV | - |
dc.contributor.author | Kojouharova, MS | - |
dc.contributor.author | Gadjeva, M | - |
dc.contributor.author | Rabheru, S | - |
dc.contributor.author | Thakrar, R | - |
dc.contributor.author | Kaplun, A | - |
dc.contributor.author | Kishore, U | - |
dc.date.accessioned | 2009-05-01T20:29:42Z | - |
dc.date.available | 2009-05-01T20:29:42Z | - |
dc.date.issued | 2008 | - |
dc.identifier.citation | Biochemistry 47: 13093–13102, 2008 | en |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/3272 | - |
dc.description.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. | en |
dc.format.extent | 297 bytes | - |
dc.format.mimetype | text/plain | - |
dc.language.iso | en | - |
dc.publisher | American Chemical Society | - |
dc.subject | Salmonella lipopolysaccharide | - |
dc.subject | IgG | - |
dc.subject | Ca2+ | - |
dc.subject | Recognition | - |
dc.title | Interaction of the globular domain of human C1q with Salmonella typhimurium lipopolysaccharide | en |
dc.type | Research Paper | en |
Appears in Collections: | Biological Sciences Community Health and Public Health Dept of Life Sciences Research Papers |
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File | Description | Size | Format | |
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Closed+Access+Paper.txt | 297 B | Text | View/Open |
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