Cloning, expression and characterization of Mycobacterium tuberculosis lipoprotein LprF

Biochemical and Biophysical Research Communications
Juliane K BrüllePeter Sander

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.

References

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Feb 27, 2007·Microbiology·Mandana RezwanPeter Sander
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Feb 17, 2009·The Journal of Biological Chemistry·Kazuki TawaratsumidaMasahito Hashimoto
Aug 8, 2009·The Journal of Biological Chemistry·Andreas TschumiPeter Sander

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Citations

Apr 12, 2011·Molecular Microbiology·David A WiddickMatthew I Hutchings
Oct 26, 2012·The FEBS Journal·Hiroshi NakayamaBok Luel Lee
Feb 12, 2015·FEMS Microbiology Reviews·Nienke Buddelmeijer
May 24, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Laure ToniniMichel Rivière

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