ArticleACS chemical biology2019
Slt, MltD, and MltG of Pseudomonas aeruginosa as Targets of Bulgecin A in Potentiation of β-Lactam Antibiotics.
Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 36 citations in OpenAlex.
- A Concise Route to Orthogonally Protected Bulgecinine.The Journal of organic chemistry · 2026Article
- Gene-specific reversal of carbapenem-resistant Pseudomonas aeruginosa via phage-delivered CRISPR-Cas13a.npj antimicrobials and resistance · 2025Article
- Bacterial peptidoglycan as a living polymer.Current opinion in chemical biology · 2025Review
- Article
- Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024Article
- Structural characterization of lytic transglycosylase MltD of Pseudomonas aeruginosa, a target for the natural product bulgecin A.International journal of biological macromolecules · 2024Article
- Cell envelope structural and functional contributions to antibiotic resistance inJournal of bacteriology · 2024Article
- Mutation ofJournal of bacteriology · 2023Article
- Amber-codon suppression for spatial localization and in vivo photoaffinity capture of the interactome of the Pseudomonas aeruginosa rare lipoprotein A lytic transglycosylase.Protein science : a publication of the Protein Society · 2023Article
- Mutation ofbioRxiv : the preprint server for biology · 2023Article
- Exploring the inhibition of the soluble lytic transglycosylase Cj0843c of Campylobacter jejuni via targeting different sites with different scaffolds.Protein science : a publication of the Protein Society · 2023Article
- Escherichia coli has robust regulatory mechanisms against elevated peptidoglycan cleavage by lytic transglycosylases.The Journal of biological chemistry · 2023Article
- Review
- Penetration through Outer Membrane and Efflux Potential inAntibiotics (Basel, Switzerland) · 2023Article
- Metal cofactor stabilization by a partner protein is a widespread strategy employed for amidase activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Peptidoglycan enzymes ofFrontiers in microbiology · 2022Review
- β-lactam Resistance inPathogens (Basel, Switzerland) · 2021Review
- The Lysozyme Inhibitor Thionine Acetate Is Also an Inhibitor of the Soluble Lytic Transglycosylase Slt35 fromMolecules (Basel, Switzerland) · 2021Article
- Natural products that target the cell envelope.Current opinion in microbiology · 2021Review
- Unconventional Antibacterials and Adjuvants.Accounts of chemical research · 2021Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The interplay between the activities of lytic transglycosylases (LTs) and penicillin-binding proteins (PBPs) is critical for the health of the bacterial cell wall. Bulgecin A (a natural-product inhibitor of LTs) potentiates the activity of β-lactam antibiotics (inhibitors of PBPs), underscoring this intimate mechanistic interdependence. Bulgecin A in the presence of an appropriate β-lactam causes bulge deformation due to the formation of aberrant peptidoglycan at the division site of the bacterium. As Pseudomonas aeruginosa, a nefarious human pathogen, has 11 LT paralogs, the answer as to which LT activity correlates with β-lactam potentiation is important and is currently unknown. Growth of P. aeruginosa PAO1 strains harboring individual transposon-insertion mutants at each of the 11 genes for LTs, in the presence of the β-lactam antibiotic ceftazidime or meropenem, implicated the gene products of slt, mltD, and mltG (of the 11), in bulge formation and potentiation. Hence, the respective enzymes would be the targets of inhibition by bulgecin A, which was indeed documented. We further demonstrated by imaging in real time and by SEM that cell lysis occurs by the structural failure of this bulge. Upon removal of the β-lactam antibiotic prior to lysis, P. aeruginosa experiences delayed recovery from the elongation and bulge phenotype in the presence of bulgecin A. These observations argue for a collaborative role for the target LTs in the repair of the aberrant cell wall, the absence of activities of which in the presence of bulgecin A results in potentiation of the β-lactam antibiotic.
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Registered trials
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