Open AccessThe Erp protein is anchored at the surface by a carboxy‐terminal hydrophobic domain and is important for cell‐wall structure in Mycobacterium smegmatis
Author(s) -
Kocı́ncová Dana,
Sondén Berit,
MendonçaLima Leila,
Gicquel Brigitte,
Reyrat JeanMarc
Publication year - 2004
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00964-9
Subject(s) - mycobacterium smegmatis , complementation , mutant , virulence , extracellular , biology , mycobacterium , gene , domain (mathematical analysis) , protein domain , microbiology and biotechnology , biochemistry , mycobacterium tuberculosis , bacteria , genetics , medicine , tuberculosis , mathematical analysis , mathematics , pathology
Erp ( e xported r epetitive p rotein), also known as P36, Pirg and Rv3810, is a member of a mycobacteria‐specific family of extracellular proteins. In pathogenic species, the erp gene has been described as a virulence factor. The Erp proteins comprise three domains. The N‐ and C‐terminal domains are similar in all mycobacterial species, while the central domain consists of a repeated module that differs considerably between species. Here we show that the Erp protein is loosely attached to the surface and that the carboxy‐terminal domain, which displays hydrophobic features, anchors Erp at the surface of the bacillus. The hydrophobic region is not necessary for the complementation of the altered colony morphology of a Mycobacterium smegmatis erp − mutant but proved to be necessary to achieve resistance to detergent at wild‐type levels.