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© Research
Publication : FEMS microbiology letters

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEMS microbiology letters - 16 Feb 2004

Kocíncová D, Sondén B, de Mendonça-Lima L, Gicquel B, Reyrat JM

Link to Pubmed [PMID] – 14987764

FEMS Microbiol. Lett. 2004 Feb;231(2):191-6

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.

http://www.ncbi.nlm.nih.gov/pubmed/14987764