Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6.

Renshaw, P.S. and Lightbody, K.L. and Veverka, V. and Muskett, F.W. and Kelly, G. and Frenkiel, T.A. and Gordon, S.V. and Hewinson, R.G. and Burke, B. and Norman, J. and Williamson, R.A. and Carr, M.D. (2005) Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6. EMBO Journal, 24 . pp. 2491-2498. (Access to this publication is restricted)

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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: Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Sue Davies
Date Deposited: 19 Dec 2007 17:54
Last Modified: 18 Nov 2011 11:45
Resource URI: http://kar.kent.ac.uk/id/eprint/78 (The current URI for this page, for reference purposes)
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