Open AccessLif, the lysostaphin immunity factor, complements FemB in staphylococcal peptidoglycan interpeptide bridge formation
Author(s) -
Tschierske M,
Ehlert K,
Strandén A.M,
BergerBächi B
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb12583.x
Subject(s) - lysostaphin , peptidoglycan , microbiology and biotechnology , mutant , serine , chemistry , staphylococcus aureus , biology , biochemistry , bacteria , genetics , cell wall , enzyme , gene
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.