The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
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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
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Journal ArticleDOI
A switch in surface polymer biogenesis triggers growth-phase-dependent and antibiotic-induced bacteriolysis.
Josué Flores-Kim,Genevieve S Dobihal,Andy Fenton,Andy Fenton,David Z. Rudner,Thomas G. Bernhardt,Thomas G. Bernhardt +6 more
TL;DR: It is shown that alterations in surface polymers called teichoic acids (TAs) play a key role in penicillin-induced lysis of the Gram-positive pathogen Streptococcus pneumoniae (Sp), and changes in surface polymer assembly may underlie the mechanism of antibiotic- and/or growth phase- induced lysis for other important Gram- positive pathogens.
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pFiD188, the linear virulence plasmid of Rhodococcus fascians D188
Isolde M. Francis,Annick De Keyser,Philippe De Backer,Carmen Simón-Mateo,Jutta Kalkus,Ine Pertry,Wilson Ardiles-Diaz,Riet De Rycke,Olivier M. Vandeputte,Mondher El Jaziri,Marcelle Holsters,Danny Vereecke +11 more
TL;DR: In this paper, a linear plasmid of rhodococcus fascians, pFiD188, was determined, which is the only phytopathogen of which the virulence genes occur on a linearplasmid.
Journal ArticleDOI
Penicillin-Binding Protein 3 Is Essential for Growth of Pseudomonas aeruginosa.
TL;DR: Overall, these findings reveal that PBP3 represents the most promising target for drug discovery against P. aeruginosa, whereas other HMM PBPs have less potential.
Journal ArticleDOI
Fluorosugar Chain Termination Agents as Probes of the Sequence Specificity of a Carbohydrate Polymerase
TL;DR: A method for testing the fidelity of carbohydrate polymerase pattern deposition is reported: synthesized fluorosugar donors and used them as chain termination agents, and the data indicate that this enzyme mediates the cell wall galactan production through a sequence-specific polymerization.
Journal ArticleDOI
Deciphering the Catalytic Domain of Colicin M, a Peptidoglycan Lipid II-degrading Enzyme
Hélène Barreteau,Hélène Barreteau,Ahmed Bouhss,Ahmed Bouhss,Fabien Gérard,Denis Duché,Boubekeur Boussaid,Boubekeur Boussaid,Didier Blanot,Didier Blanot,Roland Lloubès,Dominique Mengin-Lecreulx,Dominique Mengin-Lecreulx,Thierry Touzé,Thierry Touzé +14 more
TL;DR: Mutational analysis identified five residues that are essential for cytotoxicity as well as in vitro lipid II-degrading activity: Asp-229, His-235, AsP-226, Tyr-228, and Arg-236, hence suggesting they belong to the colicin M active site.
References
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