ArticleAntimicrobial agents and chemotherapy2016
Clinical Variants of the Native Class D β-Lactamase of Acinetobacter baumannii Pose an Emerging Threat through Increased Hydrolytic Activity against Carbapenems.
Article in Antimicrobial agents and chemotherapy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Structural insights into the activity of carbapenemases: understanding the mechanism of action of current inhibitors and informing the design of new carbapenem adjuvants.RSC medicinal chemistry · 2025Review
- Diversity in the Common Fold: Structural Insights into Class D β-Lactamases from Gram-Negative Pathogens.Pathogens (Basel, Switzerland) · 2025Article
- Structural and Dynamic Features of Acinetobacter baumannii OXA-66 β-Lactamase Explain Its Stability and Evolution of Novel Variants.Journal of molecular biology · 2024Article
- Specific Amino Acid Substitutions in OXA-51-TypeInternational journal of molecular sciences · 2022Article
- Inhibition of theACS infectious diseases · 2021Article
- Whole-Genome Assessment of ClinicalFrontiers in microbiology · 2021Article
- Structural analysis of avibactam-mediated activation of the bla and mec divergons in methicillin-resistantThe Journal of biological chemistry · 2020Article
- Structure-based functional fitness analyses of carbapenemase variants identified among pathogenic carbapenem-resistant Gram-negative bacteria.World journal of microbiology & biotechnology · 2020Article
- Carbapenemases: TransformingBiomolecules · 2020Review
- Intrinsic Class D β-Lactamases ofmBio · 2018Article
- Multiple substitutions lead to increased loop flexibility and expanded specificity inThe Biochemical journal · 2018Article
- Multicenter Study of the Relationship between Carbapenem MIC Values and Clinical Outcome of Patients with Acinetobacter Bacteremia.Antimicrobial agents and chemotherapy · 2017Article
- The structure of a doripenem-bound OXA-51 class D β-lactamase variant with enhanced carbapenemase activity.Protein science : a publication of the Protein Society · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The threat posed by the chromosomally encoded class D β-lactamase of Acinetobacter baumannii (OXA-51/66) has been unclear, in part because of its relatively low affinity and turnover rate for carbapenems. Several hundred clinical variants of OXA-51/66 have been reported, many with substitutions of active-site residues. We determined the kinetic properties of OXA-66 and five clinical variants with respect to a wide variety of β-lactam substrates. The five variants displayed enhanced activity against carbapenems and in some cases against penicillins, late-generation cephalosporins, and the monobactam aztreonam. Molecular dynamics simulations show that in OXA-66, P130 inhibits the side-chain rotation of I129 and thereby prevents doripenem binding because of steric clash. A single amino acid substitution at this position (P130Q) in the variant OXA-109 greatly enhances the mobility of both I129 and a key active-site tryptophan (W222), thereby facilitating carbapenem binding. This expansion of substrate specificity represents a very worrisome development for the efficacy of β-lactams against this troublesome pathogen.
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