ArticleAntimicrobial agents and chemotherapy2015
Mechanism of β-lactam action in Streptococcus pneumoniae: the piperacillin paradox.
Article in Antimicrobial agents and chemotherapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Antibacterial Benzimidazole-2-Methanamines as Allosteric Modulators ofJournal of medicinal chemistry · 2026Article
- Combining live fluorescence imaging with in situ cryoelectron tomography sheds light on the septation process inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- A high-resolution screen identifies a preexisting beta-lactam that specifically treats Lyme disease in mice.Science translational medicine · 2025Article
- The evolution of resistance to synergistic multi-drug combinations is more complex than evolving resistance to each individual drug component.Evolutionary applications · 2023Article
- The Pneumococcal Divisome: Dynamic Control ofFrontiers in microbiology · 2021Review
- Article
- Genomic epidemiology of penicillin-non-susceptibleMicrobial genomics · 2019Review
- Drug Resistance and the Prevention Strategies in Food Borne Bacteria: An Update Review.Advanced pharmaceutical bulletin · 2019Review
- Nascent teichoic acids insertion into the cell wall directs the localization and activity of the major pneumococcal autolysin LytA.Cell surface (Amsterdam, Netherlands) · 2018Article
- PBP2b plays a key role in both peripheral growth and septum positioning in Lactococcus lactis.PloS one · 2018Article
- Peptidoglycan O-acetylation is functionally related to cell wall biosynthesis and cell division in Streptococcus pneumoniae.Molecular microbiology · 2017Article
- Substitutions in PBP2b from β-Lactam-resistantThe Journal of biological chemistry · 2017Article
- Suppression of a deletion mutation in the gene encoding essential PBP2b reveals a new lytic transglycosylase involved in peripheral peptidoglycan synthesis in Streptococcus pneumoniae D39.Molecular microbiology · 2016Article
- β-Lactam Resistance Mechanisms: Gram-Positive Bacteria and Mycobacterium tuberculosis.Cold Spring Harbor perspectives in medicine · 2016Review
- Profiling of β-lactam selectivity for penicillin-binding proteins in Streptococcus pneumoniae D39.Antimicrobial agents and chemotherapy · 2015Article
Corrections and comments
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Authors and funding
8 authors at 7 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human pathogen Streptococcus pneumoniae has been treated for decades with β-lactam antibiotics. Its resistance is now widespread, mediated by the expression of mosaic variants of the target enzymes, the penicillin-binding proteins (PBPs). Understanding the mode of action of β-lactams, not only in molecular detail but also in their physiological consequences, will be crucial to improving these drugs and any counterresistances. In this work, we investigate the piperacillin paradox, by which this β-lactam selects primarily variants of PBP2b, whereas its most reactive target is PBP2x. These PBPs are both essential monofunctional transpeptidases involved in peptidoglycan assembly. PBP2x participates in septal synthesis, while PBP2b functions in peripheral elongation. The formation of the "lemon"-shaped cells induced by piperacillin treatment is consistent with the inhibition of PBP2x. Following the examination of treated and untreated cells by electron microscopy, the localization of the PBPs by epifluorescence microscopy, and the determination of the inhibition time course of the different PBPs, we propose a model of peptidoglycan assembly that accounts for the piperacillin paradox.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.