title: Penicillin-binding proteins and beta-lactam resistance.
abstract: A number of ways and means have evolved to provide resistance to eubacteria challenged by beta-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.
authors.affiliation: Laboratoire d'Ingénierie des Macromolécules, Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075-CNRS, CEA, Université Joseph Fourier, Grenoble, France.
authors.forename: André
authors.initials: A
authors.lastname: Zapun
authors.forename: Carlos
authors.initials: C
authors.lastname: Contreras-Martel
authors.forename: Thierry
authors.initials: T
authors.lastname: Vernet
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016983:Enterococcus / Q000187:drug effects; D008969:Molecular Sequence Data; D009154:Mutation; D009343:Neisseria / Q000187:drug effects; D046915:Penicillin-Binding Proteins / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D013211:Staphylococcus aureus / Q000187:drug effects; D013296:Streptococcus pneumoniae / Q000187:drug effects; D018440:beta-Lactam Resistance; D047090:beta-Lactams / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D046915:Penicillin-Binding Proteins; D047090:beta-Lactams