Open AccessSelective inhibition of penicillin‐binding proteins and its effects on growth and architecture of Staphylococcus aureus *
Author(s) -
Beise F.,
Labischinski H.,
Giesbrecht P.
Publication year - 1988
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.1574-6968.1988.tb13933.x
Subject(s) - penicillin binding proteins , staphylococcus aureus , cefotaxime , mecillinam , penicillin , antibiotics , microbiology and biotechnology , imipenem , chemistry , biology , bacteria , biochemistry , escherichia coli , enterobacteriaceae , antibiotic resistance , genetics , gene
We found that the three high molecular weight penicillin‐binding proteins (PBP) 1, 2, and 3 of Staphylococcus aureus could be blocked by the β‐lactam antibiotics imipenem, cefotaxime, and mecillinam, respectively. The inhibition of any of these PBPs was not sufficient for an antibacterial effect. Even the simultaneous blocking of PBPs 2 and 3, previously supposed to be the lethal targets of β‐lactam antibiotics, did not induce bacteriolysis, nor did the combined saturation of PBPs 2, 3, and 4. Instead, PBP 1 seems to play a key role, because on one hand the combined inhibition of PBP 1 with any of the other high molecular weight PBPs led to bacteriolysis, on the other hand, only inhibition of PBP 1 led to a loss of the ‘splitting system’ of the staphylococcal cross wall, similar to that observed in penicillin G‐treated cells earlier.