Class B HMW-PBPs can be further divided into subclasses and Escherichia coli PBP3 is paradigmatic of subclass B3 that groups class B PBPs from Gram negative bacteria involved in cell division. The HMW-PBPs group can be subdivided into classes A and B, the LMW group into classes A, B and C. The former enzymes act as transpeptidases in vivo and are involved in peptidoglycan synthesis while the latter are carboxypeptidases and endopeptidases thought to remodel peptidoglycan during the bacterial life cycle but details of their in vivo activities are not well established. Penicillin-binding proteins belong to the family of acyl-serine transferases and are traditionally separated into high-molecular-weight (HMW) PBPs and low-molecular-weight (LMW) PBPs based on molecular weight and sequence homology –. They are found in all bacteria and represent major targets in anti-biotherapy, especially for the widely used β-lactam antibiotics. The penicillin-binding proteins (PBPs) synthesize and remodel the cell wall peptidoglycan, a major component of the bacterial cell wall that gives the cell its shape and rigidity –. This does not alter the authors’ adherence to PLOS ONE policies on sharing data and materials. All other funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Ĭompeting interests: Jacques Dumas is employed by Sanofi-Aventis.
The specific role of this author is articulated in the ‘author contributions’ section. Sanofi-Aventis provided support in the form of salary for author JD, but did not have any additional role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. Jacques Dumas is employed by Sanofi-Aventis. FK is research associates of the FRS-FNRS, Belgium. is recipient of a FRIA (Fonds de la Recherche pour l’Industrie et l’Agriculture) fellowship (F.R.S.-FNRS, Brussels, Belgium). P6/19), the Fonds de la Recherche Scientifique, (IISN 4.4505.09, IISN 4.4509.11, FRFC 2.4511.06F), the University of Liège (Fonds spéciaux, Crédit classique, C-06/19 and C-09/75), and a return grant to AD. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.įunding: This work was supported in part by the Belgian Program on Interuniversity Poles of Attraction initiated by the Belgian State, Prime Minister’s Office, Science Policy programming (IAP no. Received: JanuAccepted: ApPublished: May 29, 2014Ĭopyright: © 2014 Sauvage et al. PLoS ONE 9(5):Įditor: Eric Cascales, Centre National de la Recherche Scientifique, Aix-Marseille Université, France (2014) Crystal Structure of Penicillin-Binding Protein 3 (PBP3) from Escherichia coli.
Citation: Sauvage E, Derouaux A, Fraipont C, Joris M, Herman R, Rocaboy M, et al.
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