Lipoprotein synthesis in mycobacteria
Authors:
- 1 March 2007
- journal article
- review article
- Published by Microbiology Society in Microbiology
- Vol. 153 (3) , 652-658
Abstract
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-positve 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.Keywords
This publication has 41 references indexed in Scilit:
- Signature proteins that are distinctive characteristics of Actinobacteria and their subgroupsAntonie van Leeuwenhoek, 2006
- A Database of Bacterial Lipoproteins (DOLOP) with Functional Assignments to Predicted LipoproteinsJournal of Bacteriology, 2006
- Potent Inhibition of Macrophage Responses to IFN-γ by Live Virulent Mycobacterium tuberculosis Is Independent of Mature Mycobacterial Lipoproteins but Dependent on TLR2The Journal of Immunology, 2006
- The 19-kDa antigen of Mycobacterium tuberculosis is a major adhesin that binds the mannose receptor of THP-1 monocytic cells and promotes phagocytosis of mycobacteriaMicrobial Pathogenesis, 2005
- The Transcriptional Responses of Mycobacterium tuberculosis to Inhibitors of MetabolismJournal of Biological Chemistry, 2004
- The knockout of the lprG-Rv1410 operon produces strong attenuation of Mycobacterium tuberculosisMicrobes and Infection, 2004
- In Vivo Interaction between the Polyprenol Phosphate Mannose Synthase Ppm1 and the Integral Membrane Protein Ppm2 from Mycobacterium smegmatis Revealed by a Bacterial Two-hybrid SystemJournal of Biological Chemistry, 2003
- Ppm1, a novel polyprenol monophosphomannose synthase from Mycobacterium tuberculosisBiochemical Journal, 2002
- Identification of Lipoprotein Homologues of Pneumococcal PsaA in the Equine Pathogens Streptococcus equi and Streptococcus zooepidemicusInfection and Immunity, 2000
- THE ENVELOPE OF MYCOBACTERIAAnnual Review of Biochemistry, 1995