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EMBO Press, The EMBO Journal, 14(24), p. 2491-2498

DOI: 10.1038/sj.emboj.7600732

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

Journal article published in 2005 by Ps S. Renshaw, Kl L. Lightbody, Vaclav Veverka, Fw W. Muskett, Geoff Kelly, Ta A. Frenkiel, Sv Gordon, R. Glyn Hewinson, Rg Glyn Hewinson, Bernard Burke, Jim Norman ORCID, Ra A. Williamson, Mark D. Carr
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.