The MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes.

2.50
Hdl Handle:
http://hdl.handle.net/10033/15318
Title:
The MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes.
Authors:
Thedieck, Kathrin; Hain, Torsten; Mohamed, Walid; Tindall, Brian J; Nimtz, Manfred; Chakraborty, Trinad; Wehland, Jürgen; Jänsch, Lothar
Abstract:
Pathogenic 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.
Affiliation:
Helmholtz Centre for Infection Research, Division of Cell and Immune Biology, Cellular Proteomics Group, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.
Citation:
The 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.
Journal:
Molecular microbiology
Issue Date:
Dec-2006
URI:
http://hdl.handle.net/10033/15318
DOI:
10.1111/j.1365-2958.2006.05452.x
PubMed ID:
17042784
Type:
Article
Language:
en
ISSN:
0950-382X
Appears in Collections:
publications of the research group cellular proteom research (CPRO)

Full metadata record

DC FieldValue Language
dc.contributor.authorThedieck, Kathrinen
dc.contributor.authorHain, Torstenen
dc.contributor.authorMohamed, Waliden
dc.contributor.authorTindall, Brian Jen
dc.contributor.authorNimtz, Manfreden
dc.contributor.authorChakraborty, Trinaden
dc.contributor.authorWehland, Jürgenen
dc.contributor.authorJänsch, Lotharen
dc.date.accessioned2007-12-17T10:27:38Zen
dc.date.available2007-12-17T10:27:38Zen
dc.date.issued2006-12en
dc.identifier.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.en
dc.identifier.issn0950-382Xen
dc.identifier.pmid17042784en
dc.identifier.doi10.1111/j.1365-2958.2006.05452.xen
dc.identifier.urihttp://hdl.handle.net/10033/15318en
dc.description.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.en
dc.language.isoenen
dc.subject.meshAnimalsen
dc.subject.meshAntimicrobial Cationic Peptidesen
dc.subject.meshBacterial Proteinsen
dc.subject.meshCell Membraneen
dc.subject.meshDrug Resistance, Bacterialen
dc.subject.meshListeria monocytogenesen
dc.subject.meshLysineen
dc.subject.meshMiceen
dc.subject.meshMice, Inbred BALB Cen
dc.subject.meshMicrobial Sensitivity Testsen
dc.subject.meshPhospholipidsen
dc.subject.meshVirulenceen
dc.titleThe MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for Infection Research, Division of Cell and Immune Biology, Cellular Proteomics Group, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.en
dc.identifier.journalMolecular microbiologyen

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