title: Lif, the lysostaphin immunity factor, complements FemB in staphylococcal peptidoglycan interpeptide bridge formation.
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.
authors.affiliation: Institute of Medical Microbiology, University of Zürich, Switzerland.
authors.forename: M
authors.initials: M
authors.lastname: Tschierske
authors.forename: K
authors.initials: K
authors.lastname: Ehlert
authors.forename: A M
authors.initials: AM
authors.lastname: Strandén
authors.forename: B
authors.initials: B
authors.lastname: Berger-Bächi
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology*; D002352:Carrier Proteins; D002473:Cell Wall / Q000737:chemistry; D005816:Genetic Complementation Test; D005998:Glycine / Q000032:analysis / Q000378:metabolism; D006602:Hexosyltransferases / Q000378:metabolism; D008248:Lysostaphin; D016106:Methicillin Resistance; D009097:Multienzyme Complexes / Q000378:metabolism; D002267:Muramoylpentapeptide Carboxypeptidase; D009154:Mutation; D046915:Penicillin-Binding Proteins; D010457:Peptidoglycan / Q000096:biosynthesis / Q000737:chemistry*; D010458:Peptidyl Transferases / Q000378:metabolism; D012694:Serine / Q000032:analysis; D013211:Staphylococcus aureus / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D001426:Bacterial Proteins; D002352:Carrier Proteins; C096686:FemA protein, Bacteria; C102928:FemB protein, Staphylococcus epidermidis; D009097:Multienzyme Complexes; D046915:Penicillin-Binding Proteins; D010457:Peptidoglycan; D012694:Serine; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D008248:Lysostaphin; D005998:Glycine