ArticleEvolutionary applications2019
The functional convergence of antibiotic resistance in β-lactamases is not conferred by a simple convergent substitution of amino acid.
Article in Evolutionary applications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- A comprehensive dataset of homologous and non-homologous isofunctional enzymes across the tree of life.BMC research notes · 2026Article
- Interpretable machine learning classifies β-lactamase subclasses and prioritizes boundary variants for antimicrobial resistance surveillance.Frontiers in pharmacology · 2026Article
- Large genomic deletions delineate Mycobacterium tuberculosis L4 sublineages in South American countries.PloS one · 2023Article
- Promiscuous Enzyme Activity as a Driver of Allo and Iso Convergent Evolution, Lessons from the β-Lactamases.International journal of molecular sciences · 2020Review
- The functional convergence of antibiotic resistance in β-lactamases is not conferred by a simple convergent substitution of amino acid.Evolutionary applications · 2019Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial resistance to antibiotics is a serious medical and public health concern worldwide. Such resistance is conferred by a variety of mechanisms, but the extensive variability in levels of resistance across bacteria is a common finding. Understanding the underlying evolutionary processes governing this functional variation in antibiotic resistance is important as it may allow the development of appropriate strategies to improve treatment options for bacterial infections. The main objective of this study was to examine the functional evolution of β-lactamases, a common mechanism of enzymatic resistance that inactivates a widely used class of antibiotics. We first obtained β-lactamase protein sequences and minimal inhibitory concentration (MIC), a measure of antibiotic function, from previously published literature. We then used a molecular phylogenetic framework to examine the evolution of β-lactamase functional activity. We found that the functional activity of antibiotic resistance mediated by β-lactamase has evolved in a convergent manner within molecular classes, but is not associated with any single amino acid substitution. This suggests that the dynamics of convergent evolution in this system can vary between the functional and molecular (sequence) levels. Such disassociation may hamper bioinformatic approaches to antibiotic resistance determination and underscore the need for (less efficient but more effective) activity assays as an essential step in evaluating resistance in a given case.
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