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: Kocı́ncová, Dana, Sondén, Berit, de Mendonça-Lima, Leila, Gicquel, Brigitte, Reyrat, Jean-Marc
• Format: Journal Article
• Language: English
• Published: Oxford, UK Elsevier B.V 16.02.2004; Blackwell Publishing Ltd; Blackwell
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Biological and medical sciences; Cell wall; Cell Wall - chemistry; Cell Wall - drug effects; Cell Wall - metabolism; Detergent; Detergents; Fundamental and applied biological sciences. Psychology; Hydrophobic and Hydrophilic Interactions; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Microbiology; Mycobacterium smegmatis; Mycobacterium smegmatis - chemistry; Mycobacterium smegmatis - drug effects; Mycobacterium smegmatis - metabolism; Protein Structure, Tertiary; Sodium Dodecyl Sulfate; Mycobacterium smegmatis; Cell wall; Detergent; Mycobacteriales; Mycobacteriaceae; Bacteria; Actinomycetes; Protein
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1016/S0378-1097(03)00964-9

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.