Universität zu Köln

Lou, Ye, Rybniker, Jan, Sala, Claudia ORCID: 0000-0003-4031-4648 and Cole, Stewart T. (2017). EspC forms a filamentous structure in the cell envelope of Mycobacterium tuberculosis and impacts ESX-1 secretion. Mol. Microbiol., 103 (1). S. 26 - 39. HOBOKEN: WILEY-BLACKWELL. ISSN 1365-2958

Full text not available from this repository.

Abstract

Pathogenicity of Mycobacterium tuberculosis (M. tb) is mediated by the ESX-1 secretion system, which exports EsxA and EsxB, the major virulence factors that are co-secreted with EspA and EspC. Functional information about ESX-1 components is scarce. Here, it was shown that EspC associates with EspA in the cytoplasm and membrane, then polymerizes during secretion from M. tb. EspC was localized by immuno-gold electron microscopy in whole cells or cryosections as a surface-exposed filamentous structure that seems to span the cell envelope. Consistent with these findings, purified EspC homodimerizes via disulphide bond formation, multimerizes and self-assembles into long filaments in vitro. The C-terminal domain is required for multimerization as truncation and selected point mutations therein impact EspC filament formation, thus reducing secretion of EsxA and causing attenuation of M. tb. The data are consistent with EspC serving either as a modulator of ESX-1 function or as a component of the secretion apparatus.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Lou, Ye UNSPECIFIED UNSPECIFIED UNSPECIFIED Rybniker, Jan UNSPECIFIED UNSPECIFIED UNSPECIFIED Sala, Claudia UNSPECIFIED orcid.org/0000-0003-4031-4648 UNSPECIFIED Cole, Stewart T. UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-243788
DOI:	10.1111/mmi.13575
Journal or Publication Title:	Mol. Microbiol.
Volume:	103
Number:	1
Page Range:	S. 26 - 39
Date:	2017
Publisher:	WILEY-BLACKWELL
Place of Publication:	HOBOKEN
ISSN:	1365-2958
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language VII SECRETION; SYSTEM; VIRULENCE; PROTEIN; ESAT-6; MECHANISM; SMEGMATIS; BACILLUS; NEEDLE; ATTENUATION Multiple languages Biochemistry & Molecular Biology; Microbiology Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/24378