ArticleInfection and drug resistance2025
The Impact of Ser165Glu Substitution Within the Ω-Loop on the Hydrolytic Activity of a Novel Ambler Class A β-Lactamase Variant LAP-3.
Article in Infection and drug resistance, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Introduction: Lactamase activity proteins (LAPs) are narrow-spectrum β-lactamases identified within the Enterobacteriaceae family. In this research, we uncovered a novel variant, LAP-3, while investigating quinolone and carbapenem resistance in Methods: Antimicrobial susceptibility was assessed using the agar dilution method. The Results: Genome sequencing and BLAST analysis revealed a substitution of glutamic acid (Glu165) with serine (Ser165) in LAP-3 compared to LAP-2 within the Ω-loop. The plasmid sequence containing Conclusion: The findings reveal that the novel Ambler class A β-lactamase LAP-3 demonstrates an expanded hydrolysis spectrum against Penicillins, certain cephalosporins, and β-lactamase inhibitors. The Ser165Glu substitution within the Ω-loop may influence the resistance characteristics associated with LAP β-lactamases.
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