ArticleAntimicrobial agents and chemotherapy2015
In vitro prediction of the evolution of GES-1 β-lactamase hydrolytic activity.
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 16 papers.
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16 citing papers in PubMed, 31 citations in OpenAlex.
- Development of simplex and multiplex immunochromatographic assays for rapid detection of GES-, PER-, and VEB-producing gram-negative bacteria.Microbiology spectrum · 2026Article
- Evaluation of carbapenem inactivation method-based phenotypic assays for the detection of GES-type carbapenemases in Enterobacterales,Journal of clinical microbiology · 2026Article
- Mechanistic basis for inhibition of the extended-spectrum β-lactamase GES-1 by enmetazobactam and tazobactam.FEBS letters · 2025Article
- Mechanisms leading toAntimicrobial agents and chemotherapy · 2024Article
- Phylogenetic predictions of carbapenemase activity from the Guiana extended-spectrum (GES) family of β-lactamases.JAC-antimicrobial resistance · 2024Article
- A panel of diverseMicrobial genomics · 2023Article
- In vivo translational assessment of the GES genotype on the killing profile of ceftazidime, ceftazidime/avibactam and meropenem against Pseudomonas aeruginosa.The Journal of antimicrobial chemotherapy · 2022Article
- Genome-wide analysis reveals the emergence of multidrug resistantFrontiers in microbiology · 2022Article
- Extended-spectrum β-lactamases: an update on their characteristics, epidemiology and detection.JAC-antimicrobial resistance · 2021Review
- Article
- Extended Spectrum Beta-Lactamase (ESBL) Produced by Gram-Negative Bacteria in Trinidad and Tobago.International journal of microbiology · 2021Review
- Acquisition of Extended-Spectrum β-Lactamase GES-6 Leading to Resistance to Ceftolozane-Tazobactam Combination inAntimicrobial agents and chemotherapy · 2019Article
- Past and Present Perspectives on β-Lactamases.Antimicrobial agents and chemotherapy · 2018Review
- Nosocomial dissemination of VIM-2-producing ST235 Pseudomonas aeruginosa in Lithuania.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2016Article
- A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes.Clinical microbiology reviews · 2016Review
- Structural and Functional Aspects of Class A Carbapenemases.Current drug targets · 2016Review
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Resistance to β-lactams is constantly increasing due to the emergence of totally new enzymes but also to the evolution of preexisting β-lactamases. GES-1 is a clinically relevant extended-spectrum β-lactamase (ESBL) that hydrolyzes penicillins and broad-spectrum cephalosporins but spares monobactams and carbapenems. However, several GES-1 variants (i.e., GES-2 and GES-5) previously identified among clinical isolates display an extended spectrum of activity toward carbapenems. To study the evolution potential of the GES-1 β-lactamase, this enzyme was submitted to in vitro-directed evolution, with selection on increasing concentrations of the cephalosporin cefotaxime, the monobactam aztreonam, or the carbapenem imipenem. The highest resistance levels were conferred by a combination of up to four substitutions. The A6T-E104K-G243A variant selected on cefotaxime and the A6T-E104K-T237A-G243A variant selected on aztreonam conferred high resistance to cefotaxime, ceftazidime, and aztreonam. Conversely, the A6T-G170S variant selected on imipenem conferred high resistance to imipenem and cefoxitin. Of note, the A6T substitution involved in higher MICs for all β-lactams is located in the leader peptide of the GES enzyme and therefore is not present in the mature protein. Acquired cross-resistance was not observed, since selection with cefotaxime or aztreonam did not select for resistance to imipenem, and vice versa. Here, we demonstrate that the β-lactamase GES-1 exhibits peculiar properties, with a significant potential to gain activity against broad-spectrum cephalosporins, monobactams, and carbapenems.
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