The Erp protein is anchored at the surface by a carboxy-terminal hydrophobic domain and is important for cell-wall structure in Mycobacterium smegmatis

Erp (exported repetitive protein), 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 sim...

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Bibliographic Details
Published in:FEMS microbiology letters 2004-02, Vol.231 (2), p.191-196
Main Authors: Kocíncová, Dana, Sondén, Berit, Leila de Mendonça-Lima, Gicquel, Brigitte, Jean-Marc Reyrat
Format: Article
Language:English
Subjects:
Complementation
Erp protein
Hydrophobicity
Microbiology
Morphology
Mycobacterium smegmatis
Proteins
Species
Virulence
Virulence factors
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Summary:Erp (exported repetitive protein), 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.
ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-10970300964-9