ArticlePloS one2012
Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Acid-dependent beta-lactam resistance inmBio · 2026Article
- Enzymatic activity of PBP1B is required for growth rate-independent ppGpp-mediated resistance to PBP2 inhibitors inJournal of bacteriology · 2026Article
- Cell density-dependent antibiotic tolerance to inhibition of the elongation machinery requires fully functional PBP1B.Communications biology · 2022Article
- A whole-genome assay identifies four principal gene functions that confer tolerance of meropenem stress uponFrontiers in antibiotics · 2022Article
- A multiplexable assay for screening antibiotic lethality against drug-tolerant bacteria.Nature methods · 2019Article
- Coupling of polymerase and carrier lipid phosphatase prevents product inhibition in peptidoglycan synthesis.Cell surface (Amsterdam, Netherlands) · 2018Article
- The Fluorescent D-Amino Acid NADA as a Tool to Study the Conditional Activity of Transpeptidases inFrontiers in microbiology · 2018Article
- Structural Insights into Inhibition of Escherichia coli Penicillin-binding Protein 1B.The Journal of biological chemistry · 2017Article
- PBP1a/LpoA but not PBP1b/LpoB are involved in regulation of the major β-lactamase gene blaA in Shewanella oneidensis.Antimicrobial agents and chemotherapy · 2015Article
- Opposing effects of target overexpression reveal drug mechanisms.Nature communications · 2014Article
- Differential requirement for PBP1a and PBP1b in in vivo and in vitro fitness of Vibrio cholerae.Infection and immunity · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The combination of antibiotics is one of the strategies to combat drug-resistant bacteria, though only a handful of such combinations are in use, such as the β-lactam combinations. In the present study, the efficacy of a specific sub-inhibitory concentration of cefsulodin with other β-lactams was evaluated against a range of Gram-negative clinical isolates. This approach increased the sensitivity of the isolates, regardless of the β-lactamase production. The preferred target and mechanism of action of cefsulodin were identified in laboratory strains of Escherichia coli, by examining the effects of deleting the penicillin-binding protein (PBP) 1a and 1b encoding genes individually. Deletion of PBP1b was involved in sensitizing the bacteria to β-lactam agents, irrespective of its O-antigen status. Moreover, the use of a sub-inhibitory concentration of cefsulodin in combination with a β-lactam exerted an effect similar to that one obtained for PBP1b gene deletion. We conclude that the identified β-lactam/cefsulodin combination works by inhibiting PBP1b (at least partially) despite the involvement of β-lactamases, and therefore could be extended to a broad range of Gram-negative pathogens.
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