Results 21 to 30 of about 399,815 (205)

Penicillin-binding Proteins (PBP) and Lmo0441 (a PBP-like protein) play a role in Beta-lactam sensitivity of Listeria monocytogenes

Gut Pathogens, 2009
While seven penicillin-binding proteins (PBPs) or PBP-like proteins have been identified either by radiolabelled penicillin binding studies or genomic analysis, only PBP3 has been considered of interest for Beta-lactams activity against Listeria ...
Van de Velde Sébastien, Carryn Stéphane, Van Bambeke Françoise, Hill Colin, Tulkens Paul M, Sleator Roy D   +5 more
doaj   +1 more source

A CozE Homolog Contributes to Cell Size Homeostasis of Streptococcus pneumoniae

mBio, 2020
Control of peptidoglycan assembly is critical to maintain bacterial cell size and morphology. Penicillin-binding proteins (PBPs) are crucial enzymes for the polymerization of the glycan strand and/or their cross-linking via peptide branches.
Gro Anita Stamsås, Marine Restelli, Adrien Ducret, Céline Freton, Pierre Simon Garcia, Leiv Sigve Håvarstein, Daniel Straume, Christophe Grangeasse, Morten Kjos   +8 more
doaj   +1 more source

MacP bypass variants of Streptococcus pneumoniae PBP2a suggest a conserved mechanism for the activation of bifunctional cell wall synthases

mBio, 2023
The peptidoglycan (PG) layer protects bacteria from osmotic lysis and defines their shape. The class A penicillin-binding proteins (aPBPs) are PG synthases that possess both glycan polymerization and crosslinking activities needed for PG biogenesis.
Caroline Midonet, Sean Bisset, Irina Shlosman, Felipe Cava, David Z. Rudner, Thomas G. Bernhardt   +5 more
doaj   +1 more source

Impacts of Penicillin Binding Protein 2 Inactivation on β-Lactamase Expression and Muropeptide Profile in Stenotrophomonas maltophilia

mSystems, 2017
Penicillin binding proteins (PBPs) are involved in peptidoglycan synthesis, and their inactivation is linked to β-lactamase expression in ampR–β-lactamase module–harboring Gram-negative bacteria.
Yi-Wei Huang, Yu Wang, Yun Lin, Chin Lin, Yi-Tsung Lin, Cheng-Chih Hsu, Tsuey-Ching Yang   +6 more
doaj   +1 more source

Structural and Regulatory Changes in PBP4 Trigger Decreased β-Lactam Susceptibility in Enterococcus faecalis

mBio, 2018
Enterococcus faecalis strains resistant to penicillin and ampicillin are rare and have been associated with increases in quantities of low-affinity penicillin-binding protein 4 (PBP4) or with amino acid substitutions in PBP4. We report an E.
Louis B. Rice, Charlene Desbonnet, Amelia Tait-Kamradt, Monica Garcia-Solache, John Lonks, Thomas M. Moon, Éverton D. D’Andréa, Rebecca Page, Wolfgang Peti   +8 more
doaj   +1 more source

Penicillin binding proteins as danger signals: meningococcal penicillin binding protein 2 activates dendritic cells through Toll-like receptor 4.

PLoS ONE, 2011
Neisseria meningitidis is a human pathogen responsible for life-threatening inflammatory diseases. Meningococcal penicillin-binding proteins (PBPs) and particularly PBP2 are involved in bacterial resistance to β-lactams. Here we describe a novel function
Marcelo Hill, Ala-Eddine Deghmane, Mercedes Segovia, Maria Leticia Zarantonelli, Gaëlle Tilly, Philippe Blancou, Gaëlle Bériou, Régis Josien, Ignacio Anegon, Eva Hong, Corinne Ruckly, Aude Antignac, Meriem El Ghachi, Ivo Gomperts Boneca, Muhamed-Kheir Taha, Maria Cristina Cuturi   +15 more
doaj   +1 more source

In Silico Design and Molecular Docking Studies of Carbapenem Analogues Targeting Acinetobacter baumannii PBP1A Receptor

Al-Mustansiriyah Journal of Pharmaceutical Sciences, 2020
Carbapenems are considered as the most effective antibiotic against Acinetobacter baumannii infections, as the pathogen has a resistance to the most of the other beta-lactam antibiotics; however, recent studies proved that this pathogen has developed
Twana Salih, Hawzhin A. Salih
doaj   +1 more source

Hfq mutation confers increased cephalosporin resistance in Klebsiella pneumoniae [PDF]

Archives of Biological Sciences, 2017
Klebsiella pneumoniae (K. pneumoniae), is an opportunistic pathogen raising significant public health concerns owing to its multi-drug resistance. Hfq, one of the main RNA-binding proteins, is a key post-transcriptional regulator.
Li Xinran, Yang Mingjuan, Ke Yuehua, Liu Mingyuan, Wang Yufei, Liu Shiwei, Bo Liu, Chen Zeliang   +7 more
doaj   +1 more source

Identification of Mutations in the mrdA Gene Encoding PBP2 That Reduce Carbapenem and Diazabicyclooctane Susceptibility of Escherichia coli Clinical Isolates with Mutations in ftsI (PBP3) and Which Carry bla_NDM-1

mSphere, 2019
Penicillin-binding proteins (PBPs) are essential for bacterial cell wall biosynthesis, and several are clinically validated antibacterial targets of β-lactam antibiotics.
Srijan Ranjitkar, Folkert Reck, Xiaobo Ke, Qingming Zhu, Glenn McEnroe, Sara L. Lopez, Charles R. Dean   +6 more
doaj   +1 more source

Bacterial Resistance to Penicillin G by Decreased Affinity of Penicillin-Binding Proteins: A Mathematical Model

Emerging Infectious Diseases, 2003
Streptococcus pneumoniae and Neisseria meningitidis have very similar mechanisms of resistance to penicillin G. Although penicillin resistance is now common in S. pneumoniae, it is still rare in N. meningitidis.
L. Temime, P.Y. Boëlle, P. Courvalin, D. Guillemot   +3 more
doaj   +1 more source