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Cloning, expression and characterization of Mycobacterium tuberculosis lipoprotein LprF


Brülle, J K; Grau, T; Tschumi, A; Auchli, Y; Burri, R; Polsfuss, S; Keller, P M; Hunziker, P; Sander, P (2010). Cloning, expression and characterization of Mycobacterium tuberculosis lipoprotein LprF. Biochemical and Biophysical Research Communications (BBRC), 391(1):679-684.

Abstract

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.

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.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Medical Microbiology
04 Faculty of Medicine > Functional Genomics Center Zurich
08 University Research Priority Programs > Systems Biology / Functional Genomics
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Date:January 2010
Deposited On:20 Jan 2010 07:48
Last Modified:05 Apr 2016 13:46
Publisher:Elsevier
ISSN:0006-291X
Publisher DOI:10.1016/j.bbrc.2009.11.120
PubMed ID:19944079
Permanent URL: http://doi.org/10.5167/uzh-27797

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