We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6.
- Authors
Renshaw, Philip S.; Lightbody, Kirsty L.; Veverka, Vaclav; Muskett, Fred W.; Kelly, Geoff; Frenkiel, Thomas A.; Gordon, Stephen V.; Hewinson, R Glyn; Burke, Bernard; Norman, Jim; Williamson, Richard A.; Carr, Mark D.
- 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.
- Subjects
MYCOBACTERIUM tuberculosis; TUBERCULIN; MICROBIAL virulence; PATHOGENIC microorganisms; TUBERCULOSIS; MICROBIOLOGY
- Publication
EMBO Journal, 2005, Vol 24, Issue 14, p2491
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1038/sj.emboj.7600732