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Characterization of BKC-1 class A carbapenemase from Klebsiella pneumoniae clinical isolates in Brazil.
Nicoletti, Adriana Giannini; Marcondes, Marcelo F M; Martins, Willames M B S; Almeida, Luiz G P; Nicolás, Marisa F; Vasconcelos, Ana T R; Oliveira, Vitor; Gales, Ana Cristina.
Afiliação
  • Nicoletti AG; Laboratório Alerta, Disciplina de Infectologia, Departamento de Medicina, Universidade Federal de São Paulo, São Paulo, Brazil adrianagn@gmail.com.
  • Marcondes MF; Laboratório de Enzimologia, Departamento de Biofísica, Universidade Federal de São Paulo, São Paulo, Brazil.
  • Martins WM; Laboratório Alerta, Disciplina de Infectologia, Departamento de Medicina, Universidade Federal de São Paulo, São Paulo, Brazil.
  • Almeida LG; Laboratório Nacional de Computação Científica, Petrópolis, Brazil.
  • Nicolás MF; Laboratório Nacional de Computação Científica, Petrópolis, Brazil.
  • Vasconcelos AT; Laboratório Nacional de Computação Científica, Petrópolis, Brazil.
  • Oliveira V; Laboratório de Enzimologia, Departamento de Biofísica, Universidade Federal de São Paulo, São Paulo, Brazil.
  • Gales AC; Laboratório Alerta, Disciplina de Infectologia, Departamento de Medicina, Universidade Federal de São Paulo, São Paulo, Brazil.
Antimicrob Agents Chemother ; 59(9): 5159-64, 2015 Sep.
Article em En | MEDLINE | ID: mdl-26055384
Three Klebsiella pneumoniae clinical isolates demonstrating carbapenem resistance were recovered from different patients hospitalized at two medical centers in São Paulo, Brazil. Resistance to all ß-lactams, quinolones, and some aminoglycosides was observed for these isolates that were susceptible to polymyxin B. Carbapenem hydrolysis, which was inhibited by clavulanic acid, was observed for all K. pneumoniae isolates that belonged to the same pulsed-field gel electrophoresis (PFGE) type and a novel sequence type (ST), ST1781 (clonal complex 442 [CC442]). A 10-kb nonconjugative incompatibility group Q (IncQ) plasmid, denominated p60136, was transferred to Escherichia coli strain TOP10 cells by electroporation. The full sequencing of p60136 showed that it was composed of a mobilization system, ISKpn23, the phosphotransferase aph3A-VI, and a 941-bp open reading frame (ORF) that codified a 313-amino acid protein. This ORF was named bla BKC-1. Brazilian Klebsiella carbapenemase-1 (BKC-1) showed a pI of 6.0 and possessed the highest identity (63%) with a ß-lactamase of Sinorhizobium meliloti, an environmental bacterium. Hydrolysis studies demonstrated that purified BKC-1 not only hydrolyzed carbapenems but also penicillins, cephalosporins, and monobactams. However, the carbapenems were less efficiently hydrolyzed due to their very low kcat values (0.0016 to 0.031 s(-1)). In fact, oxacillin was the best substrate for BKC-1 (kcat /Km , 53,522.6 mM(-1) s(-1)). Here, we report a new class A carbapenemase, confirming the diversity and rapid evolution of ß-lactamases in K. pneumoniae clinical isolates.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Beta-Lactamases / Klebsiella pneumoniae País/Região como assunto: America do sul / Brasil Idioma: En Revista: Antimicrob Agents Chemother Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Beta-Lactamases / Klebsiella pneumoniae País/Região como assunto: America do sul / Brasil Idioma: En Revista: Antimicrob Agents Chemother Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos