Lif, the lysostaphin immunity factor, complements FemB in staphylococcal peptidoglycan interpeptide bridge formation |
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| Authors: | M Tschierske K Ehlert AM Strandén B Berger-Bächi |
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| Institution: | Department of Cellular Physiology, The Babraham Institute, Babraham Hall, Babraham, Cambridge CB2 4AT, UK;Department of Biochemistry, Institute of Food Research, Norwich Research Park, Colney, Norwich NR4 7UA, UK;Department of Biological and Nutritional Sciences, Faculty of Agriculture and Biological Sciences, The University, Newcastle upon Tyne NE1 7RU, UK |
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| Abstract: | 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. |
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| Keywords: | Cellulomonas fimi Xylanase structure NodB domain Deacetylase |
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