Open AccessPenicillin‐binding proteins and β‐lactam resistance
Author(s) -
Zapun André,
ContrerasMartel Carlos,
Vernet Thierry
Publication year - 2008
Publication title -
fems microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.91
H-Index - 212
eISSN - 1574-6976
pISSN - 0168-6445
DOI - 10.1111/j.1574-6976.2007.00095.x
Subject(s) - penicillin binding proteins , biology , penicillin , antibiotics , homologous recombination , point mutation , endogeny , microbiology and biotechnology , antibiotic resistance , dna binding protein , binding site , biochemistry , lipid ii , bacteria , genetics , mutation , gene , peptidoglycan , transcription factor
A number of ways and means have evolved to provide resistance to eubacteria challenged by β‐lactams. This review is focused on pathogens that resist by expressing low‐affinity targets for these antibiotics, the penicillin‐binding proteins (PBPs). Even within this narrow focus, a great variety of strategies have been uncovered such as the acquisition of an additional low‐affinity PBP, the overexpression of an endogenous low‐affinity PBP, the alteration of endogenous PBPs by point mutations or homologous recombination or a combination of the above.