Lipoprotein synthesis in mycobacteria
Author(s) -
Mandana Rezwan,
Thomas Grau,
Andreas Tschumi,
Peter Sander
Publication year - 2007
Publication title -
microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 179
eISSN - 1465-2080
pISSN - 1350-0872
DOI - 10.1099/mic.0.2006/000216-0
Subject(s) - mycobacterium tuberculosis , bacteria , virulence , biology , microbiology and biotechnology , signal peptide , lipoprotein , mutant , lipid a , biochemistry , moiety , bacterial cell structure , gene , peptide sequence , chemistry , tuberculosis , cholesterol , genetics , medicine , pathology , stereochemistry
Lipoproteins are a functionally diverse class of secreted bacterial proteins characterized by an N-terminal lipid moiety. The lipid moiety serves to anchor these proteins to the cell surface. Lipoproteins are synthesized as pre-prolipoproteins and mature by post-translational modifications. The post-translational modifications are directed by the lipobox motif located within the signal peptide. Enzymes involved in lipoprotein synthesis are essential in Gram-negative bacteria but not in Gram-positive bacteria. Inactivation of genes involved in lipoprotein synthesis attenuates a variety of Gram-positive pathogens, including Mycobacterium tuberculosis. The attenuated phenotype of these mutants indicates an important role of lipoproteins and lipoprotein synthesis in bacterial virulence. M. tuberculosis, the causative agent of tuberculosis, is one of the most devastating pathogens in the world. This article reviews recent findings on the synthesis, localization and function of lipoproteins in mycobacteria.
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