IBR 13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
artículos
Título:
Metallo-b-lactamases ensure antibiotic resistance under restrictive zinc concentrations via fine-tuning of metal-ligand interactions
Autor/es:
JAVIER M. GONZÁLEZ; MARÍA-ROCÍO MEINI; PABLO E. TOMATIS; FRANCISCO J. MEDRANO MARTÍN; JULIA A. CRICCO1; ALEJANDRO J. VILA
Revista:
NATURE CHEMICAL BIOLOGY
Editorial:
NATURE PUBLISHING GROUP
Referencias:
Año: 2012 p. 698 - 700
ISSN:
1552-4450
Resumen:
A number of multiresistant bacterial pathogens inactivate antibiotics by producing ZnII-dependent β-lactamases. We show that metal uptake leading to an active dinuclear enzyme in the periplasmic space of Gram-negative bacteria is ensured by a cysteine residue, an unusual metal ligand in oxidizing environments. Kinetic, structural and affinity data show that such ZnII-Cys interaction is an adaptive trait tuning the metal binding affinity, thus enabling antibiotic resistance at restrictive ZnII concentrations.
