Renshaw, Philip S., Lightbody, Kirsty L., Veverka, Vaclav, Muskett, Frederick W., Kelly, Geoff, Frenkiel, Tom A., Gordon, Stephen V., Hewinson, R. Glyn, Burke, Bernard, Norman, Jim, and others. (2005) Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6. EMBO Journal, 24 . pp. 2491-2498. ISSN 0261-4189. E-ISSN 1460-2075. (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:78)
PDF
Language: English Restricted to Repository staff only |
|
|
|
Official URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... |
Abstract
The secreted Mycobacterium tuberculosis complex proteins CFP-10 and ESAT-6 have recently been shown to play an essential role in tuberculosis pathogenesis. We have determined the solution structure of the tight, 1:1 complex formed by CFP-10 and ESAT-6, and employed fluorescence microscopy to demonstrate specific binding of the complex to the surface of macrophage and monocyte cells. A striking feature of the complex is the long flexible arm formed by the C-terminus of CFP-10, which was found to be essential for binding to the surface of cells. The surface features of the CFP-10.ESAT-6 complex, together with observed binding to specific host cells, strongly suggest a key signalling role for the complex, in which binding to cell surface receptors leads to modulation of host cell behaviour to the advantage of the pathogen.
Item Type: | Article |
---|---|
Subjects: | Q Science |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Susan Davies |
Date Deposited: | 19 Dec 2007 17:54 UTC |
Last Modified: | 16 Nov 2021 09:39 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/78 (The current URI for this page, for reference purposes) |
- Export to:
- RefWorks
- EPrints3 XML
- BibTeX
- CSV
- Depositors only (login required):