An unexpected similarity between antibiotic-resistant NDM-1 and beta-lactamase II from Erythrobacter litoralis
Protein & Cell
;
(12): 250-258, 2011.
Artigo
em Inglês
| WPRIM
| ID: wpr-757102
ABSTRACT
NDM-1 (New Delhi metallo-beta-lactamase) gene encodes a metallo-beta-lactamase (MBL) with high carbapenemase activity, which makes the host bacterial strain easily dispatch the last-resort antibiotics known as carbapenems and cause global concern. Here we present the bioinformatics data showing an unexpected similarity between NDM-1 and beta-lactamase II from Erythrobacter litoralis, a marine microbial isolate. We have further expressed these two mature proteins in E. coli cells, both of which present as a monomer with a molecular mass of 25 kDa. Antimicrobial susceptibility assay reveals that they share similar substrate specificities and are sensitive to aztreonam and tigecycline. The conformational change accompanied with the zinc binding visualized by nuclear magnetic resonance, Zn(2+)-bound NDM-1, adopts at least some stable tertiary structure in contrast to the metal-free protein. Our work implies a close evolutionary relationship between antibiotic resistance genes in environmental reservoir and in the clinic, challenging the antimicrobial resistance monitoring.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Farmacologia
/
Filogenia
/
Zinco
/
Beta-Lactamases
/
Estabilidade Enzimática
/
Aztreonam
/
Dados de Sequência Molecular
/
Homologia de Sequência do Ácido Nucleico
/
Cefalosporinase
/
Química
Idioma:
Inglês
Revista:
Protein & Cell
Ano de publicação:
2011
Tipo de documento:
Artigo
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