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

• Published in: FEMS microbiology letters Vol. 231; no. 2; pp. 191 - 196
• Main Authors: Kocíncová, Dana, Sondén, Berit, Leila de Mendonça-Lima, Gicquel, Brigitte, Jean-Marc Reyrat
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 01.02.2004
• Subjects: Complementation; Erp protein; Hydrophobicity; Microbiology; Morphology; Mycobacterium smegmatis; Proteins; Species; Virulence; Virulence factors
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1016/S0378-10970300964-9

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.