Structural and Biochemical Characterization of the Novel CTX-M-151 Extended-Spectrum β-Lactamase and Its Inhibition by Avibactam

Author:

Ghiglione Barbara123,Rodríguez María Margarita123,Brunetti Florencia123,Papp-Wallace Krisztina M.4567ORCID,Yoshizumi Ayumi8,Ishii Yoshikazu8,Bonomo Robert A.4567ORCID,Gutkind Gabriel123,Klinke Sebastián9ORCID,Power Pablo123ORCID

Affiliation:

1. Universidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Departamento de Microbiología, Inmunología y Biotecnología, Laboratorio de Resistencia Bacteriana, Buenos Aires, Argentina

2. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires, Argentina

3. Instituto de Investigaciones en Bacteriología y Virología Molecular (IBaViM), Buenos Aires, Argentina

4. Research Service, Louis Stokes Cleveland Department of Veterans Affairs, Cleveland, Ohio, USA

5. Department of Medicine, Case Western Reserve University, Cleveland, Ohio, USA

6. Center for Proteomics and Bioinformatics, Case Western Reserve University, Cleveland, Ohio, USA

7. Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio, USA

8. Department of Microbiology and Infectious Diseases, Toho University, Tokyo, Japan

9. Fundación Instituto Leloir, IIBBA-CONICET, and Plataforma Argentina de Biología Estructural y Metabolómica PLABEM, Buenos Aires, Argentina

Abstract

The diazabicyclooctane (DBO) inhibitor avibactam (AVI) reversibly inactivates most serine β-lactamases, including the CTX-M β-lactamases. Currently, more than 230 unique CTX-M members distributed in five clusters with less than 5% amino acid sequence divergence within each group have been described.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

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