The MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Tindall, Brian J
MetadataShow full item record
AbstractPathogenic bacteria have to cope with defence mechanisms mediated by adaptive and innate immunity of the host cells. Cationic antimicrobial peptides (CAMPs) represent one of the most effective components of the host innate immune response. Here we establish the function of Lmo1695, a member of the VirR-dependent virulence regulon, recently identified in Listeria monocytogenes. Lmo1695 encodes a membrane protein of 98 kDa with strong homology to the multiple peptide resistance factor (MprF) of Staphylococcus aureus. Like staphylococcal MprF, we found that Lmo1695 is involved in the synthesis of the membrane phospholipid lysylphosphatidylglycerol (L-PG). In addition, Lmo1695 is also essential for lysinylation of diphosphatidylglycerol (DPG), another phospholipid widely distributed in bacterial membranes. A Deltalmo1695 mutant lacking the lysinylated phospholipids was particularly susceptible to CAMPs of human and bacterial origin. The mutant strain infected both epithelial cells and macrophages only poorly and was attenuated for virulence when tested in a mouse model of infection. Lmo1695 is a member of a growing list of survival factors which enable growth of L. monocytogenes in different environments.
CitationThe MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes. 2006, 62 (5):1325-39 Mol. Microbiol.
AffiliationHelmholtz Centre for Infection Research, Division of Cell and Immune Biology, Cellular Proteomics Group, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.
- Broad-spectrum antimicrobial peptide resistance by MprF-mediated aminoacylation and flipping of phospholipids.
- Authors: Ernst CM, Peschel A
- Issue date: 2011 Apr
- LysPGS formation in Listeria monocytogenes has broad roles in maintaining membrane integrity beyond antimicrobial peptide resistance.
- Authors: Dare K, Shepherd J, Roy H, Seveau S, Ibba M
- Issue date: 2014 May 15
- The VirAB ABC Transporter Is Required for VirR Regulation of Listeria monocytogenes Virulence and Resistance to Nisin.
- Authors: Grubaugh D, Regeimbal JM, Ghosh P, Zhou Y, Lauer P, Dubensky TW Jr.,, Higgins DE
- Issue date: 2018 Mar
- Intracellular gene expression profile of Listeria monocytogenes.
- Authors: Chatterjee SS, Hossain H, Otten S, Kuenne C, Kuchmina K, Machata S, Domann E, Chakraborty T, Hain T
- Issue date: 2006 Feb
- Inactivation of the gene encoding the cationic antimicrobial peptide resistance factor MprF increases biofilm formation but reduces invasiveness of Listeria monocytogenes.
- Authors: Nowak J, Visnovsky SB, Cruz CD, Fletcher GC, van Vliet AHM, Hedderley D, Butler R, Flint S, Palmer J, Pitman AR
- Issue date: 2021 Feb