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Lif, the lysostaphin immunity factor, complements FemB in staphylococcal peptidoglycan interpeptide bridge formation

Tschierske, M. ; Ehlert, K. ; Strandén, A.M. ; Berger-Bächi, B.

In: FEMS Microbiology Letters, 1997, vol. 153, no. 2, p. 261-264

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    Titre
    • Lif, the lysostaphin immunity factor, complements FemB in staphylococcal peptidoglycan interpeptide bridge formation
    Auteur
    • Tschierske, M.. Institute of Medical Microbiology, University of Zürich, Gloriastr. 32, CH-8028 Zürich, Switzerland
    • Ehlert, K.. Bayer AG, PH-Research Antiinfectives I, D-42096 Wuppertal, Germany
    • Strandén, A.M.. Institute of Medical Microbiology, University of Zürich, Gloriastr. 32, CH-8028 Zürich, Switzerland
    • Berger-Bächi, B.. Institute of Medical Microbiology, University of Zürich, Gloriastr. 32, CH-8028 Zürich, Switzerland
    Type de document
    • Postprint
    Identifiant OAI-PMH
    • oai:doc.rero.ch:294950
    Summary
    The formation of the Staphylococcus aureus peptidoglycan pentaglycine interpeptide chain needs FemA and FemB for the incorporation of glycines Gly2-Gly3, and Gly4-Gly5, respectively. The lysostaphin immunity factor Lif was able to complement FemB, as could be shown by serine incorporation and by an increase in lysostaphin resistance in the wild-type as well as in a femB mutant. However, Lif could not substitute for FemA in femA or in femAB-null mutants. Methicillin resistance, which is dependent on functional FemA and FemB, was not complemented by Lif, suggesting that serine-substituted side chains are a lesser substrate for penicillin-binding protein PBP2′ in methicillin resistance