Bacterial resistance by β-Lactamases: classification, mechanism of action, and pharmacological inhibition strategies
- Autores: Ruan Sousa Bastos, Jefferson Almeida Rocha
- Localización: Cuadernos de Educación y Desarrollo, ISSN-e 1989-4155, Vol. 17, Nº. 11, 2025
- Idioma: inglés
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Resumen
This review article addresses bacterial resistance, a persistent and growing challenge in global health. The discovery of penicillin in 1928 ushered in the antibiotic era, but indiscriminate use has led to the evolution of microbial defense mechanisms, such as β -lactamase enzymes. The bacterial cell wall is the target of β-lactam antibiotics, with bacteria classified as Gram-positive (single peptidoglycan layer) or Gram-negative (two layers and an outer membrane), which influences their response to antibiotics. β-lactamases, the first of which was isolated from Staphylococcus aureus in the late 1940s, break the β-lactam ring of penicillin, rendering it ineffective. The enzymes are classified functionally (Bush-Jacob-Medeiros) and structurally (Ambler: Classes A, B, C, and D). Classes A, C, and D act through acylation and deacylation involving serine, whereas Class B (metallo-β-lactamases) depends on zinc ions (Zn2+) to directly hydrolyze the substrate. The development of inhibitory drugs, such as Clavulanic Acid, Sulbactam, Tazobactam, and more recently, Avibactam (the only one without the β-lactam ring), is crucial for restoring antibiotic efficacy.
