Results 31 to 40 of about 401,752 (293)

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

Penicillin-binding proteins in Clostridium perfringens [PDF]

Antimicrobial Agents and Chemotherapy, 1981
The penicillin-binding proteins (PBPs) of Clostridium perfringens were studied. Six PBPs ranging in molecular weight from approximately 42,000 to 100,000 were detected in the cytoplasmic membrane. The relative affinities of the PBPs for 16 beta-lactam antibiotics were determined.
T F, Murphy, M, Barza, J T, Park
openaire   +2 more sources

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

The penicillin binding proteins of the genus Haemophilus [PDF]

Journal of Medical Microbiology, 1988
We questioned whether the penicillin binding protein (PBP) profiles of representative strains from the 19 species varied within the genus Haemophilus and whether these profiles would be of taxonomic value. Seventeen of the 19 representative strains studied had distinct PBP profiles; only those of H. avium and H. paragallinarum were identical.
P M, Mendelman, D A, Serfass
openaire   +2 more sources

Penicillin kills chlamydia following the fusion of bacteria with Lysosomes and prevents genital inflammatory lesions in C. muridarum-infected mice [PDF]

, 2013
The obligate intracellular bacterium Chlamydia exists as two distinct forms. Elementary bodies (EBs) are infectious and extra-cellular, whereas reticulate bodies (RBs) replicate within a specialized intracellular compartment termed an ‘inclusion ...
Le Gall, SM, Colette Kanellopoulos-Langevin, Le Gall Sylvain M., Habbeddine, M, Sylvain M. Le Gall (108751), Habbeddine, Mohamed, Delarbre, C., Dumoux, M, Maud Dumoux (501153), Dumoux, Maud, Delarbre, C, Dumoux Maud, Christiane Delarbre, Hayward Richard D., Philippe Verbeke, Delarbre Christiane, Verbeke, Philippe, Kanellopoulos-Langevin Colette, Kanellopoulos-Langevin, C, Le Gall, Sylvain M, Habbeddine Mohamed, Philippe Verbeke (16975), Hayward, RD, Hayward, Richard D, Richard D Hayward, Christiane Delarbre (501155), Delarbre, Christiane, Le Gall, S.M., Habbeddine, M., Kanellopoulos-Langevin, C., Hayward, Richard D., Colette Kanellopoulos-Langevin (146985), Mohamed Habbeddine (501154), Ramsey, K., Richard D. Hayward (272234), Verbeke, P., Verbeke, P, Kanellopoulos-Langevin, Colette, Sylvain M Le Gall, Maud Dumoux, Mohamed Habbeddine, Verbeke Philippe   +41 more
core   +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 in Haemophilus influenzae [PDF]

Antimicrobial Agents and Chemotherapy, 1981
The penicillin-binding proteins (PBPs) of Haemophilus influenzae were studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. Eight major PBPs, ranging in molecular weights from 90,000 to 27,000, were detected. The pattern of molecular weights was different from that determined fro Escherichia coli or Pseudomonas ...
S D, Makover, R, Wright, E, Telep
openaire   +2 more sources

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

The penicillin-binding proteins in Streptococcus faecalis ATCC 9790 [PDF]

, 1980
peer reviewedStreptococcus faecalis ATCC 9790 possesses seven membrane-bound penicillin-binding proteins. They have been characterized with respect to their apparent molecular weights, relative abundance, specificity profiles for 15 different beta-lactam
J. Coyette, J. M. Ghuysen, Ghuysen, Jean-Marie, Coyette, Jean, Fontana, Roberta   +4 more
core   +1 more source