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LMB-1 producing Citrobacter freundii from Argentina, a novel player in the field of MBLs.
Dabos, Laura; Rodriguez, Carlos H; Nastro, Marcela; Dortet, Laurent; Bonnin, Rémy A; Famiglietti, Angela; Iorga, Bogdan I; Vay, Carlos; Naas, Thierry.
Afiliação
  • Dabos L; EA7361 "Structure, dynamic, function and expression of broad spectrum ß-lactamases", Paris-Sud University, Faculty of Medicine, Le Kremlin-Bicêtre, France; Joint research Unit EERA « Evolution and Ecology of Resistance to Antibiotics ¼, Institut Pasteur-APHP-University Paris Sud, Paris, France.
  • Rodriguez CH; Departamento de Bioquímica Clinica, Hospital de Clínicas José de San Martín, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires, Argentina.
  • Nastro M; Departamento de Bioquímica Clinica, Hospital de Clínicas José de San Martín, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires, Argentina.
  • Dortet L; EA7361 "Structure, dynamic, function and expression of broad spectrum ß-lactamases", Paris-Sud University, Faculty of Medicine, Le Kremlin-Bicêtre, France; Joint research Unit EERA « Evolution and Ecology of Resistance to Antibiotics ¼, Institut Pasteur-APHP-University Paris Sud, Paris, France; Depa
  • Bonnin RA; EA7361 "Structure, dynamic, function and expression of broad spectrum ß-lactamases", Paris-Sud University, Faculty of Medicine, Le Kremlin-Bicêtre, France; Joint research Unit EERA « Evolution and Ecology of Resistance to Antibiotics ¼, Institut Pasteur-APHP-University Paris Sud, Paris, France; Fren
  • Famiglietti A; Departamento de Bioquímica Clinica, Hospital de Clínicas José de San Martín, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires, Argentina.
  • Iorga BI; Université Paris-Saclay, CNRS, Institut de Chimie des Substances Naturelles, UPR 2301, Labex LERMIT, 91198, Gif-sur-Yvette, France.
  • Vay C; Departamento de Bioquímica Clinica, Hospital de Clínicas José de San Martín, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires, Argentina.
  • Naas T; EA7361 "Structure, dynamic, function and expression of broad spectrum ß-lactamases", Paris-Sud University, Faculty of Medicine, Le Kremlin-Bicêtre, France; Joint research Unit EERA « Evolution and Ecology of Resistance to Antibiotics ¼, Institut Pasteur-APHP-University Paris Sud, Paris, France; Depa
Int J Antimicrob Agents ; 55(2): 105857, 2020 Feb.
Article em En | MEDLINE | ID: mdl-31785341
Carbapenemase-producing Enterobacterales expressing OXA-48, KPC, NDM, VIM or IMP enzymes are increasingly reported worldwide. We have characterized LMB-1, a novel metallo-ß-lactamase (MBL) of Ambler class B3 from Citrobacter freundii 164 (Cf164) clinical isolate from Buenos Aires, Argentina. Cf164 displayed reduced susceptibility to carbapenems but gave inconsistent results with carbapenemase confirmatory tests, indicating the presence of a weak carbapenemase. Analysis of whole-genome sequencing (WGS) of Cf164 using Resfinder revealed four ß-lactamase genes coding for CTX-M-8, PER-2, TEM-1 and CMY-150, a novel chromosomally-encoded CMY variant. Kinetic parameters of purified CMY-150 did not reveal any carbapenemase activity. However, CMY-150 conferred higher minimum inhibitory concentrations (MICs) to E. coli for ceftazidime and aztreonam compared with CMY-2. The in-house-developed ß-lactamase search software (ResMiner) in WGS data revealed a novel subclass B3 MBL named LMB-1. LMB-1 conferred resistance to penicillins and expanded-spectrum cephalosporins and reduced susceptibility to carbapenems in E. coli. The blaLMB-1 gene was located on a 176-kb IncA/C2 plasmid. LMB-1 shared 99% amino acid sequence identity with the MBL encoded in the chromosome of Rheinheimera pacifica, it's likely progenitor. Despite repeated attempts, LMB-1 could not be purified, thus only specific activities could indicate hydrolysis of carbapenems. Here we report on CMY-150, a novel CMY-2 variant that confers increased ceftazidime and aztreonam MICs to E. coli and the first description of LMB-1 in Argentina. This work underlines the need for several carbapenemase-producing Enterobacteriaceae (CPE) confirmatory tests, as this novel enzyme might have been missed using only one.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Citrobacter freundii / Enterobacteriáceas Resistentes a Carbapenêmicos País/Região como assunto: America do sul / Argentina Idioma: En Revista: Int J Antimicrob Agents Ano de publicação: 2020 Tipo de documento: Article País de afiliação: França País de publicação: Holanda
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Citrobacter freundii / Enterobacteriáceas Resistentes a Carbapenêmicos País/Região como assunto: America do sul / Argentina Idioma: En Revista: Int J Antimicrob Agents Ano de publicação: 2020 Tipo de documento: Article País de afiliação: França País de publicação: Holanda