What is it about?
Metallo-β-lactamases (MBLs) that require zinc as essential co-factor can catalyze the hydrolysis of almost all β-lactam antibiotics except for monobactams. MBLs are divided into three subclasses (B1, B2, and B3) based on primary amino acid sequence homology and possess two zinc-binding motifs. Resistance to β-lactam antibiotics through acquired MBL genes is one of the most serious problems in Gram-negative pathogenic bacteria. Thus, we might focus on the significance of the MBL in the environmental Gram-negative pathogens. To find antibiotic resistance gene(s) predating our use of antibiotics through metagenomics, we performed functional screening of a metagenomic library from the deep-seep sediments of Edison seamount (about 10,000 years old).
Featured Image
Why is it important?
Among 60 antibiotic resistant clones, a single clone with the highest MIC value for ampicillin was selected. The sequence analysis revealed a new metallo-β-lactamase (MBL) gene, designated as blaPNGM-1. PNGM-1 retains a zinc ion-binding motif (H116XH118XD120H121, H196, and H263), conserved in subclass B3 MBLs. The catalytic parameters of purified PNGM-1 and MIC values of β-lactams for E. coli TOP10 harboring blaPNGM-1 gene were assessed. Antimicrobial susceptibility testing indicated reduced susceptibility to penicillins, narrow- and extended-spectrum cephalosporins, and carbapenems. In addition, kinetic analyses revealed that PNGM-1 hydrolyzed almost all β-lactams.
Perspectives
Read the Original
This page is a summary of: PNGM-1, a Novel Subclass B3 Metallo-β-Lactamase from a Deep-Sea Sediment Metagenome, Journal of Global Antimicrobial Resistance, May 2018, Elsevier,
DOI: 10.1016/j.jgar.2018.05.021.
You can read the full text:
Resources
Contributors
The following have contributed to this page