ArticleAntimicrobial agents and chemotherapy2015
Membrane-Bound PenA β-Lactamase of Burkholderia pseudomallei.
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 19 papers.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- The lipoprotein biosynthesis pathway: key to OXA-mediated carbapenem resistance inAntimicrobial agents and chemotherapy · 2025Article
- Evolutionary Dynamics and Functional Differences in Clinically Relevant Pen β-Lactamases fromJournal of chemical information and modeling · 2025Article
- OXA β-lactamases frommBio · 2025Article
- OXA β-lactamases frombioRxiv : the preprint server for biology · 2024Article
- The biogenesis of β-lactamase enzymes.Microbiology (Reading, England) · 2022Review
- Mechanisms Involved in the Active Secretion of CTX-M-15 β-Lactamase by Pathogenic Escherichia coli ST131.Antimicrobial agents and chemotherapy · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Silver Nanoparticles Enhance Antimicrobial Efficacy of Antibiotics and Restore That Efficacy against the Melioidosis Pathogen.Antibiotics (Basel, Switzerland) · 2021Article
- Article
- Regulation and Anaerobic Function of theAntimicrobial agents and chemotherapy · 2019Article
- An in situ high-throughput screen identifies inhibitors of intracellularProceedings of the National Academy of Sciences of the United States of America · 2019Article
- β-Lactamases and β-Lactamase Inhibitors in the 21st Century.Journal of molecular biology · 2019Review
- Lipoproteins and Their Trafficking to the Outer Membrane.EcoSal Plus · 2019Review
- Intrinsic Class D β-Lactamases ofmBio · 2018Article
- Transcriptional and post-transcriptional regulation of PenA β-lactamase in acquired Burkholderia pseudomallei β-lactam resistance.Scientific reports · 2018Article
- Melioidosis.Nature reviews. Disease primers · 2018Review
- Transient In Vivo Resistance Mechanisms of Burkholderia pseudomallei to Ceftazidime and Molecular Markers for Monitoring Treatment Response.PLoS neglected tropical diseases · 2017Article
- Antibiotic resistance in Burkholderia species.Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy · 2016Review
- Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase.Nature chemical biology · 2016Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Burkholderia pseudomallei is the etiologic agent of melioidosis, a difficult-to-treat disease with diverse clinical manifestations. β-Lactam antibiotics such as ceftazidime are crucial to the success of melioidosis therapy. Ceftazidime-resistant clinical isolates have been described, and the most common mechanism is point mutations affecting expression or critical amino acid residues of the chromosomally encoded class A PenA β-lactamase. We previously showed that PenA was exported via the twin arginine translocase system and associated with the spheroplast fraction. We now show that PenA is a membrane-bound lipoprotein. The protein and accompanying β-lactamase activity are found in the membrane fraction and can be extracted with Triton X-114. Treatment with globomycin of B. pseudomallei cells expressing PenA results in accumulation of the prolipoprotein. Mass spectrometric analysis of extracted membrane proteins reveals a protein peak whose mass is consistent with a triacylated PenA protein. Mutation of a crucial lipobox cysteine at position 23 to a serine residue results in loss of β-lactamase activity and absence of detectable PenAC23S protein. A concomitant isoleucine-to-alanine change at position 20 in the signal peptide processing site in the PenAC23S mutant results in a nonlipidated protein (PenAI20A C23S) that is processed by signal peptidase I and exhibits β-lactamase activity. The resistance profile of a B. pseudomallei strain expressing this protein is indistinguishable from the profile of the isogenic strain expressing wild-type PenA. The data show that PenA membrane association is not required for resistance and must serve another purpose.
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