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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d‐amino carboxamide‐based recruitment of dinitrophenol antibodies to bacterial surfaces via peptidoglycan remodeling
Jonathan M. Fura,Marcos M. Pires +1 more
TL;DR: It is shown that the amidation of the C‐terminus to generate DNP‐displaying d‐amino carboxamide drastically improves antibody recruitment, which could potentially facilitate translation of these results to in vivo animal disease models.
Journal ArticleDOI
Synthesis and evaluation of boronic acids as inhibitors of Penicillin Binding Proteins of classes A, B and C
Astrid Zervosen,André Bouillez,Alexandre Herman,Ana Maria Amoroso,Bernard Joris,Eric Sauvage,Paulette Charlier,André Luxen +7 more
TL;DR: This work synthesized and studied the potential of a number of acylaminomethylboronic acids as inhibitors of PBPs from different classes, and identified several derivatives that inhibited PBPs of classes A, B and C from penicillin sensitive strains.
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Re-evaluation of the significance of penicillin binding protein 3 in the susceptibility of Listeria monocytogenes to β-lactam antibiotics.
TL;DR: The present study allows a reevaluation of the importance of PBP3 in the susceptibility of L. monocytogenes to β-lactams and indicates that this protein in cell division during this phase of growth is subject to tight regulation.
Journal ArticleDOI
Tetrahedral Framework Nucleic Acids Loading Ampicillin Improve the Drug Susceptibility against Methicillin-Resistant Staphylococcus aureus.
Yue Sun,Songhang Li,Yuxin Zhang,Qirong Li,Xueping Xie,Dan Zhao,Taoran Tian,Sirong Shi,Lingxian Meng,Yunfeng Lin +9 more
TL;DR: The downregulation of genes related to bacterial cell wall synthesis and upregulation of a gene related to antibiotic sensibility (PBP2) were responsible for the enhanced killing effect of tFNAs-ampicillin against MRSA.
Journal ArticleDOI
Analysis of the Streptococcus agalactiae exoproteome.
Salvatore Papasergi,Roberta Galbo,Veronica Lanza-Cariccio,Maria Domina,Giacomo Signorino,Carmelo Biondo,I Pernice,Claire Poyart,Patrick Trieu-Cuot,Giuseppe Teti,Concetta Beninati +10 more
TL;DR: The identification of several putative virulence factors and vaccine candidates of the group B streptococcus, an important pathogen, is described using a simple proteomics strategy involving LC-MS analysis of culture supernatants obtained from two strains with divergent gene expression patterns.
References
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