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

Philip S. Renshaw; Kirsty L. Lightbody; Vaclav Veverka; Fred W. Muskett; Geoff Kelly; Thomas A. Frenkiel; Stephen V. Gordon; R. Glyn Hewinson; Bernard Burke; Jim Norman; Richard A. Williamson; Mark D. Carr

doi:10.1038/sj.emboj.7600732

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

Philip S. Renshaw, Kirsty L. Lightbody, Vaclav Veverka, Fred W. Muskett, Geoff Kelly, Thomas A. Frenkiel, Stephen V. Gordon, R. Glyn Hewinson, Bernard Burke, Jim Norman, Richard A. Williamson, Mark D. Carr^*

^*Awdur cyfatebol y gwaith hwn

TB buchol, clefydau a rheolaeth

Allbwn ymchwil: Cyfraniad at gyfnodolyn › Erthygl › adolygiad gan gymheiriaid

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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.

Iaith wreiddiol	Saesneg
Tudalennau (o-i)	2491-2498
Nifer y tudalennau	8
Cyfnodolyn	EMBO Journal
Cyfrol	24
Rhif cyhoeddi	14
Dyddiad ar-lein cynnar	23 Mai 2005
Dynodwyr Gwrthrych Digidol (DOIs)	https://doi.org/10.1038/sj.emboj.7600732
Statws	Cyhoeddwyd - 20 Gorff 2005

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10.1038/sj.emboj.7600732

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@article{4e92aaa0ad764379b7549a37bce52d99,

title = "Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6",

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.",

keywords = "CFP-10, ESAT-6, Pathogenesis, Tuberculosis, Virulence",

author = "Renshaw, {Philip S.} and Lightbody, {Kirsty L.} and Vaclav Veverka and Muskett, {Fred W.} and Geoff Kelly and Frenkiel, {Thomas A.} and Gordon, {Stephen V.} and Hewinson, {R. Glyn} and Bernard Burke and Jim Norman and Williamson, {Richard A.} and Carr, {Mark D.}",

year = "2005",

month = jul,

day = "20",

doi = "10.1038/sj.emboj.7600732",

language = "English",

volume = "24",

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TY - JOUR

T1 - Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6

AU - Renshaw, Philip S.

AU - Lightbody, Kirsty L.

AU - Veverka, Vaclav

AU - Muskett, Fred W.

AU - Kelly, Geoff

AU - Frenkiel, Thomas A.

AU - Gordon, Stephen V.

AU - Hewinson, R. Glyn

AU - Burke, Bernard

AU - Norman, Jim

AU - Williamson, Richard A.

AU - Carr, Mark D.

PY - 2005/7/20

Y1 - 2005/7/20

N2 - 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.

AB - 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.

KW - CFP-10

KW - ESAT-6

KW - Pathogenesis

KW - Tuberculosis

KW - Virulence

UR - http://www.scopus.com/inward/record.url?scp=23044505589&partnerID=8YFLogxK

U2 - 10.1038/sj.emboj.7600732

DO - 10.1038/sj.emboj.7600732

M3 - Article

C2 - 15973432

AN - SCOPUS:23044505589

SN - 0261-4189

VL - 24

SP - 2491

EP - 2498

JO - EMBO Journal

JF - EMBO Journal

IS - 14

ER -

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

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