Publication:
ZHO-1, an intrinsic MBL from the environmental Gram-negative species Zhongshania aliphaticivorans.

dc.contributor.authorKieffer, Nicolas
dc.contributor.authorGuzman-Puche, Julia
dc.contributor.authorPoirel, Laurent
dc.contributor.authorKang, Hyo Jung
dc.contributor.authorJeon, Che Ok
dc.contributor.authorNordmann, Patrice
dc.contributor.funderSwiss National Science Foundation
dc.contributor.funderUniversity of Fribourg
dc.date.accessioned2023-01-25T10:31:30Z
dc.date.available2023-01-25T10:31:30Z
dc.date.issued2019-01-16
dc.description.abstractOur aim was to characterize the putative MBL of the environmental strain Zhongshania aliphaticivorans isolated from a marine environment. The putative MBL was identified in silico using the NCBI database. The β-lactamase gene was cloned into different Escherichia coli backgrounds. Kinetic parameters were determined using the purified enzyme. The enzyme named ZHO-1 shared 51% amino acid identity with the acquired class B carbapenemases IMP-1, KHM-1 and DIM-1. Expression of the blaZHO-1 gene in a susceptible E. coli resulted in a carbapenemase phenotype. Kinetic parameters determined from purified ZHO-1 enzyme showed that it had significant hydrolytic activity against most β-lactams including penicillins, cephalosporins and carbapenems, with the exception of aztreonam and cefepime. This study adds to the knowledge regarding environmental species as a reservoir of possible clinically relevant MBLs.
dc.description.versionSi
dc.identifier.citationKieffer N, Guzmán-Puche J, Poirel L, Kang HJ, Jeon CO, Nordmann P. ZHO-1, an intrinsic MBL from the environmental Gram-negative species Zhongshania aliphaticivorans. J Antimicrob Chemother. 2019 Jun 1;74(6):1568-1571
dc.identifier.doi10.1093/jac/dkz057
dc.identifier.essn1460-2091
dc.identifier.pmid30778547
dc.identifier.unpaywallURLhttp://doc.rero.ch/record/327453/files/nor_zim.pdf
dc.identifier.urihttp://hdl.handle.net/10668/13586
dc.issue.number6
dc.journal.titleThe Journal of antimicrobial chemotherapy
dc.journal.titleabbreviationJ Antimicrob Chemother
dc.language.isoen
dc.organizationHospital Universitario Reina Sofía
dc.organizationInstituto Maimónides de Investigación Biomédica de Córdoba-IMIBIC
dc.page.number1568-1571
dc.publisherOxford University Press
dc.pubmedtypeJournal Article
dc.pubmedtypeResearch Support, Non-U.S. Gov't
dc.relation.projectIDFNS-31003A_163432
dc.relation.publisherversionhttps://academic.oup.com/jac/article/74/6/1568/5333165?login=true
dc.rights.accessRightsopen access
dc.subject.decsAntibacterianos
dc.subject.decsClonación molecular
dc.subject.decsFarmacorresistencia bacteriana múltiple
dc.subject.decsGammaproteobacteria
dc.subject.decsProteínas bacterianas
dc.subject.decsRegulación bacteriana de la expresión génica
dc.subject.decsSecuencia de aminoácidos
dc.subject.decsbeta-lactamasas
dc.subject.meshAmino acid sequence
dc.subject.meshAnti-bacterial agents
dc.subject.meshBacterial proteins
dc.subject.meshCloning, molecular
dc.subject.meshDrug resistance, multiple, bacterial
dc.subject.meshGammaproteobacteria
dc.subject.meshGene expression regulation, bacterial
dc.subject.meshbeta-lactamases
dc.titleZHO-1, an intrinsic MBL from the environmental Gram-negative species Zhongshania aliphaticivorans.
dc.typeResearch article
dc.type.hasVersionVoR
dc.volume.number74
dspace.entity.typePublication

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