Cloning, expression and characterization of Mycobacterium tuberculosis lipoprotein LprF

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• 作者：Juliane K. Brü ; lle ; Thomas Grau ; Andreas Tschumi ; Yol ; a Auchli ; Reto Burri ; Silke Polsfuss ; Peter M. Keller ; Peter Hunziker ; Peter S ; er
• 关键词：Tuberculosis ; Lipoprotein ; N-Acyltransferase ; Post-translational modification ; Mycobacterium ; Lipidation
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2010
• 出版时间：1 January 2010
• 年：2010
• 卷：391
• 期：1
• 页码：679-684
• 全文大小：491 K

文摘

Lipoproteins are well known virulence factors of bacterial pathogens in general and of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, in particular. Lipoprotein lipidation between Gram-positive and Gram-negative bacteria differs significantly as these are di- and triacylated, respectively. Little is known about the lipid anchor of mycobacterial lipoproteins. We reported recently that mycobacterial LppX, a lipoprotein involved in synthesis of cell wall components is triacylated, although mycobacteria are classified as GC-rich Gram-positive bacteria. We here exploited the model organism Mycobacterium smegmatis for the expression of Mtb LprF and characterized N-terminal modifications at the molecular level. LprF is a putative lipoprotein of Mtb involved in signaling of potassium-dependent osmotic stress. LprF is extensively modified in a mycobacterium-specific manner by a thioether-linked diacylglyceryl residue with one ester-bound tuberculostearic- and one C16:0 fatty acid and additionally by a third N-linked C16:0 fatty acid, and a hexose.