Kocíncová Dana, Sondén Berit, de Mendonça-Lima Leila, Gicquel Brigitte, Reyrat Jean-Marc
Unité de Génétique Mycobactérienne, Institut Pasteur, F-75724 Paris Cedex 15, France.
FEMS Microbiol Lett. 2004 Feb 16;231(2):191-6. doi: 10.1016/S0378-1097(03)00964-9.
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.
ERP(分泌型重复蛋白),也被称为P36、Pirg和Rv3810,是分枝杆菌属特异性细胞外蛋白家族的成员。在致病菌种中,erp基因被描述为一种毒力因子。ERP蛋白包含三个结构域。所有分枝杆菌物种的N端和C端结构域相似,而中央结构域由一个重复模块组成,不同物种之间差异很大。在这里,我们表明ERP蛋白松散地附着在表面,具有疏水特性的羧基末端结构域将ERP锚定在杆菌表面。疏水区域对于耻垢分枝杆菌erp突变体改变的菌落形态的互补不是必需的,但事实证明对于达到野生型水平的去污剂抗性是必需的。