Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6 |
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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 |
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Institution: | Department of Biochemistry, University of Leicester, Leicester, UK. |
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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. |
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