Functional and Structural Characterization of OXA-935, a Novel OXA-10-Family β-Lactamase from Pseudomonas aeruginosa

Author:

Pincus Nathan B.1,Rosas-Lemus Monica12,Gatesy Samuel W. M.3,Bertucci Hanna K.3,Brunzelle Joseph S.4,Minasov George12,Shuvalova Ludmilla A.12,Lebrun-Corbin Marine1,Satchell Karla J. F.12ORCID,Ozer Egon A.35ORCID,Hauser Alan R.13ORCID,Bachta Kelly E. R.13ORCID

Affiliation:

1. Department of Microbiology-Immunology, Northwestern University, Feinberg School of Medicine, Chicago, Illinois, USA

2. Center for Structural Genomics of Infectious Diseases, Northwestern University, Feinberg School of Medicine, Chicago, Illinois, USA

3. Department of Medicine, Division of Infectious Diseases, Northwestern University, Feinberg School of Medicine, Chicago, Illinois, USA

4. Northwestern Synchrotron Research Center, Life Sciences Collaborative Access Team, Northwestern University, Argonne, Illinois, USA

5. Center for Pathogen Genomics and Microbial Evolution, Institute for Global Health, Northwestern University, Feinberg School of Medicine, Chicago, Illinois, USA

Abstract

Resistance to antipseudomonal penicillins and cephalosporins is often driven by the overproduction of the intrinsic β-lactamase AmpC. However, OXA-10-family β-lactamases are a rich source of resistance in Pseudomonas aeruginosa .

Funder

HHS | NIH | National Institute of Allergy and Infectious Diseases

HHS | NIH | National Institute of General Medical Sciences

American Cancer Society

U.S. Department of Energy

Michigan Economic Development Corporation

HHS | NIH | National Cancer Institute

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

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