ArticleAntimicrobial agents and chemotherapy2015
Comparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition Profiles.
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 28 papers.
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Who cites it
28 citing papers in PubMed.
- Comparative genome analysis of carbapenemase-producing Pseudomonas aeruginosa: gene diversity, clonal distribution, and genome dynamics.Molecular genetics and genomics : MGG · 2026Article
- Biochemical and structural analyses of metallo-β-lactamase VIM-28: impact of substitutions at residues 224 and 228 on substrate profile, stability, and zinc affinity.Microbiology spectrum · 2026Article
- Biofilm and Outer Membrane Vesicle Formation in ESKAPE Gram-Negative Bacteria: A Comprehensive Review.International journal of molecular sciences · 2025Review
- Genetic diversity, biochemical properties, epidemiology, and detection methods of IMP- and VIM-type carbapenemases.Clinical microbiology reviews · 2025Review
- Overcoming beta-lactam resistance inFrontiers in cellular and infection microbiology · 2025Article
- In silico designing and immunoinformatics analysis of a novel peptide vaccine against metallo-beta-lactamase (VIM and IMP) variants.PloS one · 2023Article
- Identification of a Stable Chromosomal Tandem Multicopy ofJournal of bacteriology · 2022Article
- Antimicrobial Evaluation of Various Honey Types against Carbapenemase-Producing Gram-Negative Clinical Isolates.Antibiotics (Basel, Switzerland) · 2022Article
- Studies on the Reactions of Biapenem with VIM Metallo β-Lactamases and the Serine β-Lactamase KPC-2.Antibiotics (Basel, Switzerland) · 2022Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Carbapenem Use Is Driving the Evolution of Imipenemase 1 Variants.Antimicrobial agents and chemotherapy · 2021Article
- Can We Exploit β-Lactamases Intrinsic Dynamics for Designing More Effective Inhibitors?Antibiotics (Basel, Switzerland) · 2020Review
- 4-(Biomolecules · 2020Article
- Article
- MBLinhibitors.com, a Website Resource Offering Information and Expertise for the Continued Development of Metallo--Lactamase Inhibitors.Biomolecules · 2020Article
- Mortality associated with carbapenem-susceptible and Verona Integron-encoded Metallo-β-lactamase-positive Pseudomonas aeruginosa bacteremia.Antimicrobial resistance and infection control · 2020Article
- Article
- Crystal structures of VIM-1 complexes explain active site heterogeneity in VIM-class metallo-β-lactamases.The FEBS journal · 2019Article
- Polymorphisms of Gene Cassette Promoters of the Class 1 Integron in ClinicalFrontiers in microbiology · 2019Article
- Article
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Authors and funding
10 authors.
Funding
Abstract
Metallo-β-lactamases (MBLs) are of increasing clinical significance; the development of clinically useful MBL inhibitors is challenged by the rapid evolution of variant MBLs. The Verona integron-borne metallo-β-lactamase (VIM) enzymes are among the most widely distributed MBLs, with >40 VIM variants having been reported. We report on the crystallographic analysis of VIM-5 and comparison of biochemical and biophysical properties of VIM-1, VIM-2, VIM-4, VIM-5, and VIM-38. Recombinant VIM variants were produced and purified, and their secondary structure and thermal stabilities were investigated by circular dichroism analyses. Steady-state kinetic analyses with a representative panel of β-lactam substrates were carried out to compare the catalytic efficiencies of the VIM variants. Furthermore, a set of metalloenzyme inhibitors were screened to compare their effects on the different VIM variants. The results reveal only small variations in the kinetic parameters of the VIM variants but substantial differences in their thermal stabilities and inhibition profiles. Overall, these results support the proposal that protein stability may be a factor in MBL evolution and highlight the importance of screening MBL variants during inhibitor development programs.
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