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

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    Authors
    Thedieck, Kathrin
    Hain, Torsten
    Mohamed, Walid
    Tindall, Brian J
    Nimtz, Manfred
    Chakraborty, Trinad
    Wehland, Jürgen
    Jänsch, Lothar cc
    Issue Date
    2006-12
    
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    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.
    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.
    Affiliation
    Helmholtz Centre for Infection Research, Division of Cell and Immune Biology, Cellular Proteomics Group, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.
    Journal
    Molecular microbiology
    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
    ae974a485f413a2113503eed53cd6c53
    10.1111/j.1365-2958.2006.05452.x
    Scopus Count
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    publications of the research group cellular proteom research (CPRO)

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