The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
TLDR
An overview of the content in PBPs of some bacteria is provided with an emphasis on comparing the biochemical properties of homologous PBPs (orthologues) belonging to different bacteria.Abstract:
Penicillin-binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural information on PBPs together with the ongoing long-term biochemical experimental investigations, and results from more recent techniques such as protein localization by green fluorescent protein-fusion immunofluorescence or double-hybrid assay, have brought our understanding of the last stages of the peptidoglycan biosynthesis to an outstanding level that allows a broad outlook on the properties of these enzymes. Details are emerging regarding the interaction between the peptidoglycan-synthesizing PBPs and the peptidoglycan, their mesh net-like product that surrounds and protects bacteria. This review focuses on the detailed structure of PBPs and their implication in peptidoglycan synthesis, maturation and recycling. An overview of the content in PBPs of some bacteria is provided with an emphasis on comparing the biochemical properties of homologous PBPs (orthologues) belonging to different bacteria.read more
Citations
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Journal ArticleDOI
Peptidoglycan O-acetylation is functionally related to cell wall biosynthesis and cell division in Streptococcus pneumoniae.
J. Bonnet,Claire Durmort,Maxime Jacq,Isabelle Mortier-Barrière,Nathalie Campo,Michael S. VanNieuwenhze,Yves V. Brun,Christopher Arthaud,Benoit Gallet,Christine Moriscot,Cécile Morlot,Thierry Vernet,Anne Marie Di Guilmi +12 more
TL;DR: It is shown that O‐acetylation driven by Adr protects the peptidoglycan of dividing cells from cleavage by the major autolysin LytA and occurs at the septal site.
Book ChapterDOI
Overview of Clostridium difficile Infection: Life Cycle, Epidemiology, Antimicrobial Resistance and Treatment
TL;DR: The pathway of peptidoglycan synthesis in this organism and associated resistances, as well as resistance to other classes of antibiotics are examined, including against first-line antibiotics.
Journal ArticleDOI
Investigating β-Lactam Drug Targets in Mycobacterium tuberculosis Using Chemical Probes.
TL;DR: In this article, the authors synthesized fluorescent analogues of β-lactam antibiotics to study two classes of enzymes that maintain Mtb's peptidoglycan: penicillin-binding proteins (PBPs) and l,d-transpeptidases (LDTs).
Book ChapterDOI
Cell Wall Biogenesis During Elongation and Division in the Plant Pathogen Agrobacterium tumefaciens.
TL;DR: How the field has evolved over the years is addressed by providing a historical overview of cell elongation and division in rod-shaped bacteria and the need for further research to answer key questions related to the regulation of cell wall biogenesis in A. tumefaciens is highlighted.
Journal ArticleDOI
Discovery and characterization of New Delhi metallo-β-lactamase-1 inhibitor peptides that potentiate meropenem-dependent killing of carbapenemase-producing Enterobacteriaceae.
Misha I. Kazi,Blair W. Perry,Daren C. Card,Richard D. Schargel,Hana B Ali,Victor C Obuekwe,Victor C Obuekwe,Madhab Sapkota,Katie N. Kang,Mark W. Pellegrino,David E. Greenberg,Todd A. Castoe,Joseph M. Boll +12 more
TL;DR: This work identified and characterized novel synthetic peptide inhibitors that bound to and inhibited NDM-1, which is an emerging β-lactam resistance mechanism in CPE, and discovered lead N DM-1 inhibitors, which serve as a starting point for further chemical optimization.
References
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Journal ArticleDOI
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Journal ArticleDOI
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