ArticleScientific reports2018
Biochemical and genetic characterization of a novel metallo-β-lactamase from marine bacterium Erythrobacter litoralis HTCC 2594.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 18 citations in OpenAlex.
- A Novel Metallo-β-Lactamase AMM-1 From Alteromonas mangrovi Reveals a Cryptic Environmental Reservoir of Carbapenem Resistance.Microbial biotechnology · 2025Article
- β-Lactams from the Ocean.Marine drugs · 2023Review
- Carbapenem Resistance among Marine Bacteria-An Emerging Threat to the Global Health Sector.Microorganisms · 2021Review
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Molecular and Functional Characterization of a Novel Plasmid-BorneInfection and drug resistance · 2021Article
- Diversity and Genetic Basis for Carbapenem Resistance in a Coastal Marine Environment.Applied and environmental microbiology · 2020Article
- Structural and biochemical analysis of the metallo-β-lactamase L1 from emerging pathogen Stenotrophomonas maltophilia revealed the subtle but distinct di-metal scaffold for catalytic activity.Protein science : a publication of the Protein Society · 2020Article
- Regulation of the Erythrobacter litoralis DSM 8509 general stress response by visible light.Molecular microbiology · 2019Article
- Shining light on the alphaproteobacterial general stress response: Comment on: Fiebig et al., Mol Microbiol, 2019.Molecular microbiology · 2019Article
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9 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Metallo-β-lactamases (MBLs) are a group of enzymes that can inactivate most commonly used β-lactam-based antibiotics. Among MBLs, New Delhi metallo-β-lactamase-1 (NDM-1) constitutes an urgent threat to public health as evidenced by its success in rapidly disseminating worldwide since its first discovery. Here we report the biochemical and genetic characteristics of a novel MBL, ElBla2, from the marine bacterium Erythrobacter litoralis HTCC 2594. This enzyme has a higher amino acid sequence similarity to NDM-1 (56%) than any previously reported MBL. Enzymatic assays and secondary structure alignment also confirmed the high similarity between these two enzymes. Whole genome comparison of four Erythrobacter species showed that genes located upstream and downstream of elbla2 were highly conserved, which may indicate that elbla2 was lost during evolution. Furthermore, we predicted two prophages, 13 genomic islands and 25 open reading frames related to insertion sequences in the genome of E. litoralis HTCC 2594. However, unlike NDM-1, the chromosome encoded ElBla2 did not locate in or near these mobile genetic elements, indicating that it cannot transfer between strains. Finally, following our phylogenetic analysis, we suggest a reclassification of E. litoralis HTCC 2594 as a novel species: Erythrobacter sp. HTCC 2594.
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