Kieffer, NicolasGuzman-Puche, JuliaPoirel, LaurentKang, Hyo JungJeon, Che OkNordmann, Patrice2023-01-252023-01-252019-01-16Kieffer 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):1568-1571http://hdl.handle.net/10668/13586Our 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.enAmino acid sequenceAnti-bacterial agentsBacterial proteinsCloning, molecularDrug resistance, multiple, bacterialGammaproteobacteriaGene expression regulation, bacterialbeta-lactamasesResearch article30778547open accessAntibacterianosClonación molecularFarmacorresistencia bacteriana múltipleGammaproteobacteriaProteínas bacterianasRegulación bacteriana de la expresión génicaSecuencia de aminoácidosbeta-lactamasas10.1093/jac/dkz0571460-2091http://doc.rero.ch/record/327453/files/nor_zim.pdf