Mack, A. R.; Department of Molecular Biology and Microbiology, Case Western Reserve University, Cleveland, OH, United States, Research Service, Louis Stokes Cleveland Department of Veterans Affairs, Cleveland, OH, United States
Barnes, M. D.; Department of Medicine, Case Western Reserve University, Cleveland, OH, United States, Research Service, Louis Stokes Cleveland Department of Veterans Affairs, Cleveland, OH, United States
Taracila, M. A.; Department of Medicine, Case Western Reserve University, Cleveland, OH, United States, Research Service, Louis Stokes Cleveland Department of Veterans Affairs, Cleveland, OH, United States
Hujer, A. M.; Department of Medicine, Case Western Reserve University, Cleveland, OH, United States, Research Service, Louis Stokes Cleveland Department of Veterans Affairs, Cleveland, OH, United States
Hujer, K. M.; Department of Medicine, Case Western Reserve University, Cleveland, OH, United States, Research Service, Louis Stokes Cleveland Department of Veterans Affairs, Cleveland, OH, United States
Cabot, G.; Red Española de Investigación en Patología Infecciosa (REIPI), Instituto de Salud Carlos III, Madrid, Spain, Servicio de Microbiolog a, Hospital Universitario Son Espases, Instituto de Investigación Sanitaria Illes Balears (IdISBa), Palma de Mallorca, Spain
Feldgarden, M.; National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, United States
Haft, D. H.; National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, United States
Klimke, W.; National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, United States
Van Den Akker, F.; Department of Biochemistry, Case Western Reserve University, Cleveland, OH, United States
Vila, A. J.; CWRU-Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology (Case VA CARES), Cleveland, OH, United States, Instituto de Biolog a Molecular y Celular de Rosario (IBR, CONICET-UNR), Rosario, Argentina, Plataforma Argentina de Biología Estructural y Metabolómica PLABEM, Buenos Aires, Argentina, Área Biof sica, Facultad de Ciencias Bioqu micas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina
Smania, A.; Centro de Investigaciones en Qu mica Biológica de Córodoba (CIQUIBIC), CONICET, Universidad Nacional de Córdoba, Córdoba, Argentina, Departamento de Qu mica Biológica Ranwel Caputto, Facultad de Ciencias Qu micas, Universidad Nacional de Córdoba, Córdoba, Argentina
Haider, S.; UCL School of Pharmacy, University College London, London, United Kingdom
Papp-Wallace, K. M.; Department of Medicine, Case Western Reserve University, Cleveland, OH, United States, Department of Biochemistry, Case Western Reserve University, Cleveland, OH, United States, Department of Proteomics and Bioinformatics, Case Western Reserve University, Cleveland, OH, United States, Research Service, Louis Stokes Cleveland Department of Veterans Affairs, Cleveland, OH, United States
Bradford, P. A.; Antimicrobial Development Specialists, LLC, Nyack, NY, United States
Rossolini, G. M.; Department of Experimental and Clinical Medicine, University of Florence, Florence, Italy, Microbiology and Virology Unit, Florence Careggi University Hospital, Florence, Italy
Docquier, Jean-Denis ; Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines
Frère, Jean-Marie ; Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques
Galleni, Moreno ; Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques
Hanson, N. D.; Department of Microbiology and Immunology, Creighton School of Medicine, Omaha, NE, United States
Oliver, A.; Red Española de Investigación en Patología Infecciosa (REIPI), Instituto de Salud Carlos III, Madrid, Spain, Servicio de Microbiolog a, Hospital Universitario Son Espases, Instituto de Investigación Sanitaria Illes Balears (IdISBa), Palma de Mallorca, Spain
Plésiat, P.; Laboratoire de Bactériologie, Centre Hospitalier Régional Universitaire, Besançon, France, UMR6249 CNRS Chrono-Environnement, Université de Bourgogne Franche-Comté, Besançon, France, Centre National de Référence de la Résistance aux Antibiotiques, Besançon, France
Poirel, L.; Emerging Antibiotic Resistance Unit, Medical and Molecular Microbiology, Faculty of Science and Medicine, University of Fribourg, Fribourg, Switzerland, Swiss National Reference Center for Emerging Antibiotic Resistance (NARA), University of Fribourg, Fribourg, Switzerland
Nordmann, P.; Emerging Antibiotic Resistance Unit, Medical and Molecular Microbiology, Faculty of Science and Medicine, University of Fribourg, Fribourg, Switzerland, Swiss National Reference Center for Emerging Antibiotic Resistance (NARA), University of Fribourg, Fribourg, Switzerland
Palzkill, T. G.; Department of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, TX, United States, Verna Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, United States
Jacoby, G. A.; Lahey Hospital and Medical Center, Burlington, MA, United States
Bush, K.; Department of Biology, Indiana University Bloomington, Bloomington, IN, United States
Bonomo, R. A.; Department of Molecular Biology and Microbiology, Case Western Reserve University, Cleveland, OH, United States, Department of Medicine, Case Western Reserve University, Cleveland, OH, United States, Department of Pharmacology, Case Western Reserve University, Cleveland, OH, United States, Department of Biochemistry, Case Western Reserve University, Cleveland, OH, United States, Department of Proteomics and Bioinformatics, Case Western Reserve University, Cleveland, OH, United States, Research Service, Louis Stokes Cleveland Department of Veterans Affairs, Cleveland, OH, United States, CWRU-Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology (Case VA CARES), Cleveland, OH, United States, Geriatric Research Education and Clinical Centers (GRECC), Louis Stokes Cleveland Department of Veterans Affairs, Cleveland, OH, United States
Oefner C, D’Arcy A, Daly JJ, Gubernator K, Charnas RL, Heinze I, Hubschwerlen C, Winkler FK. 1990. Refined crystal structure of β-lactamase from Citrobacter freundii indicates a mechanism for β-lactam hydrolysis. Nature 343:284–288. https://doi.org/10.1038/343284a0.
Lobkovsky E, Moews PC, Liu H, Zhao H, Frere JM, Knox JR. 1993. Evolution of an enzyme activity: crystallographic structure at 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc Natl Acad Sci U S A 90:11257–11261. https://doi.org/10.1073/pnas.90.23.11257.
Abraham EP, Chain E. 1940. An enzyme from bacteria able to destroy penicillin. Nature 146:837. https://doi.org/10.1038/146837a0.
Galleni M, Lindberg F, Normark S, Cole S, Honore N, Joris B, Frere JM. 1988. Sequence and comparative analysis of three Enterobacter cloacae ampC β-lactamase genes and their products. Biochem J 250:753–760. https://doi.org/10.1042/bj2500753.
Rodríguez-Martínez J-M, Poirel L, Nordmann P. 2009. Extended-spectrum cephalosporinases in Pseudomonas aeruginosa. Antimicrob Agents Chemother 53:1766–1771. https://doi.org/10.1128/AAC.01410-08.
Berrazeg M, Jeannot K, Enguéné VYN, Broutin I, Loeffert S, Fournier D, Plésiat P. 2015. Mutations in β-lactamase AmpC increase resistance of Pseudomonas aeruginosa isolates to antipseudomonal cephalosporins. Antimicrob Agents Chemother 59:6248–6255. https://doi.org/10.1128/AAC.00825-15.
Drawz SM, Taracila M, Caselli E, Prati F, Bonomo RA. 2011. Exploring sequence requirements for C3/C4 carboxylate recognition in the Pseudomonas aeruginosa cephalosporinase: insights into plasticity of the AmpC β-lactamase. Protein Sci 20:941–958. https://doi.org/10.1002/pro.612.
MacVane SH, Pandey R, Steed LL, Kreiswirth BN, Chen L. 2017. Emergence of ceftolozane-tazobactam-resistant Pseudomonas aeruginosa during treatment is mediated by a single AmpC structural mutation. Antimicrob Agents Chemother 61:e01183-17. https://doi.org/10.1128/AAC.01183-17.
Cabot G, Bruchmann S, Mulet X, Zamorano L, Moyà B, Juan C, Haussler S, Oliver A. 2014. Pseudomonas aeruginosa ceftolozane-tazobactam resistance development requires multiple mutations leading to overexpression and structural modification of AmpC. Antimicrob Agents Chemother 58:3091–3099. https://doi.org/10.1128/AAC.02462-13.
Ambler RP, Coulson AF, Frère JM, Ghuysen JM, Joris B, Forsman M, Levesque RC, Tiraby G, Waley SG. 1991. A standard numbering scheme for the class A β-lactamases. Biochem J 276:269–270. https://doi.org/10.1042/bj2760269.
Galleni M, Lamotte-Brasseur J, Rossolini GM, Spencer J, Dideberg O, Frère J-M, The Metallo-β-Lactamase Working Group. 2001. Standard numbering scheme for class B β-lactamases. Antimicrob Agents Chemother 45:660 – 663. https://doi.org/10.1128/AAC.45.3.660-663.2001.
NCBI Resource Coordinators. 2018. Database resources of the National Center for Biotechnology Information. Nucleic Acids Res 46:D8–D13. https://doi.org/10.1093/nar/gkx1095.
The UniProt Consortium. 2019. UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res 47:D506–D515. https://doi.org/10.1093/nar/gky1049.
Almagro Armenteros JJ, Tsirigos KD, Sønderby CK, Petersen TN, Winther O, Brunak S, von Heijne G, Nielsen H. 2019. SignalP 5.0 improves signal peptide predictions using deep neural networks. Nat Biotechnol 37: 420–423. https://doi.org/10.1038/s41587-019-0036-z.
Edgar RC. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792–1797. https://doi.org/10.1093/nar/gkh340.