ArticleAntimicrobial agents and chemotherapy2004
Biochemical characterization of Streptococcus pneumoniae penicillin-binding protein 2b and its implication in beta-lactam resistance.
Article in Antimicrobial agents and chemotherapy, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 46 citations in OpenAlex.
- Boronate-Based Inhibitors of Penicillin-Binding Proteins: An Underestimated Avenue for Antibiotic Discovery?Pharmaceuticals (Basel, Switzerland) · 2025Article
- Chemical genetic approaches for the discovery of bacterial cell wall inhibitors.RSC medicinal chemistry · 2023Review
- Relationship between Penicillin-Binding Proteins Alterations and β-Lactams Non-Susceptibility of Diseased Pig-IsolatedAntibiotics (Basel, Switzerland) · 2023Article
- Prevalence and resistance characteristics of multidrug-resistantFrontiers in cellular and infection microbiology · 2023Article
- A new approach to overcoming antibiotic-resistant bacteria: Traditional Chinese medicine therapy based on the gut microbiota.Frontiers in cellular and infection microbiology · 2023Review
- Molecular Characterization of Penicillin-Binding Protein2x, 2b and 1a ofFrontiers in microbiology · 2022Article
- Functional Insights into the High-Molecular-Mass Penicillin-Binding Proteins of Streptococcus agalactiae Revealed by Gene Deletion and Transposon Mutagenesis Analysis.Journal of bacteriology · 2021Article
- Article
- Mutations in penicillin-binding protein 2 from cephalosporin-resistantThe Journal of biological chemistry · 2020Article
- Substitutions in PBP2b from β-Lactam-resistantThe Journal of biological chemistry · 2017Article
- Molecular characteristics of penicillin-binding protein 2b, 2x and 1a sequences in Streptococcus pneumoniae isolates causing invasive diseases among children in Northeast China.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2016Article
- Molecular analysis of pbp2b in Streptococcus pneumonia isolated from clinical and normal flora samples.Current microbiology · 2015Article
- Mechanism of β-lactam action in Streptococcus pneumoniae: the piperacillin paradox.Antimicrobial agents and chemotherapy · 2015Article
- Characterization of mutants deficient in the L,D-carboxypeptidase (DacB) and WalRK (VicRK) regulon, involved in peptidoglycan maturation of Streptococcus pneumoniae serotype 2 strain D39.Journal of bacteriology · 2011Article
- Affinity of ceftobiprole for penicillin-binding protein 2b in Streptococcus pneumoniae strains with various susceptibilities to penicillin.Antimicrobial agents and chemotherapy · 2010Article
- Crystallization and preliminary crystallographic analysis of the transpeptidase domain of penicillin-binding protein 2B from Streptococcus pneumoniae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
- Highly variable penicillin resistance determinants PBP 2x, PBP 2b, and PBP 1a in isolates of two Streptococcus pneumoniae clonal groups, Poland 23F-16 and Poland 6B-20.Antimicrobial agents and chemotherapy · 2008Article
- Mutational analysis of class A and class B penicillin-binding proteins in Streptococcus gordonii.Antimicrobial agents and chemotherapy · 2006Article
- Mutations in penicillin-binding protein (PBP) genes and in non-PBP genes during selection of penicillin-resistant Streptococcus gordonii.Antimicrobial agents and chemotherapy · 2006Article
- Identical penicillin-binding domains in penicillin-binding proteins of Streptococcus pneumoniae clinical isolates with different levels of beta-lactam resistance.Antimicrobial agents and chemotherapy · 2005Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Extensive use of beta-lactam antibiotics has led to the selection of pathogenic streptococci resistant to beta-lactams due to modifications of the penicillin-binding proteins (PBPs). PBP2b from Streptococcus pneumoniae is a monofunctional (class B) high-molecular-weight PBP catalyzing the transpeptidation between adjacent stem peptides of peptidoglycan. The transpeptidase domain of PBP2b isolated from seven clinical resistant (CR) strains contains 7 to 44 amino acid changes over the sequence of PBP2b from the R6 beta-lactam-sensitive strain. We show that the extracellular soluble domains of recombinant PBP2b proteins (PBP2b*) originating from these CR strains have an in vitro affinity for penicillin G that is reduced by up to 99% from that of the R6 strain. The Thr446Ala mutation is always observed in CR strains and is close to the key conserved motif (S(443)SN). The Thr446Ala mutation in R6 PBP2b* displays a 60% reduction in penicillin G affinity in vitro compared to that for the wild-type protein. A recombinant R6 strain expressing the R6 PBP2b Thr446Ala mutation is twofold less sensitive to piperacillin than the parental S. pneumoniae strain. Analysis of the Thr446Ala mutation in the context of the PBP2b CR sequences revealed that its influence depends upon the presence of other unidentified mutations.
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