ArticleNature communications2019
Protein determinants of dissemination and host specificity of metallo-β-lactamases.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
64 citing papers in PubMed, 1 synthesis or guideline pooled it, 96 citations in OpenAlex.
- Acinetobacter baumannii as a Model for the Study and Application of Gram-Negative Outer Membrane Vesicles: A Systematic Review.Microbial biotechnology · 2025Pooled it
- The global epidemiology and treatment of metallo-β-lactamase-producing gram-negative pathogens.JAC-antimicrobial resistance · 2026Review
- Targeting Outer Membrane Vesicles ofJournal of microbiology and biotechnology · 2026Review
- Conserved protein sequence-structure signatures identify antibiotic resistance genes from the human microbiome.Microbiome · 2026Article
- Predatory myxobacteria lay at the cross-roads of metallo-β-lactamase evolution.Communications biology · 2026Article
- Cryptic phenotypic variation emerges rapidly during the adaptive evolution of a carbapenemase.Nature ecology & evolution · 2026Article
- Characterization of outer membrane vesicles from Acinetobacter haemolyticus and their role in the dissemination of carbapenem resistance.Medical microbiology and immunology · 2026Article
- Phage-meropenem synergy against OXA-48-producing Klebsiella pneumoniae clinical isolates.npj antimicrobials and resistance · 2026Article
- Zinc starvation uncovers bacterial host-specific proteases that shape NDM adaptability inmBio · 2026Article
- Genetic diversity, biochemical properties, epidemiology, and detection methods of IMP- and VIM-type carbapenemases.Clinical microbiology reviews · 2025Review
- Carbapenem-ResistantMicroorganisms · 2025Review
- Dissecting pOXA-48 fitness effects in clinical Enterobacterales using plasmid-wide CRISPRi screens.Nature communications · 2025Article
- Navigating the complexities of drug development for metallo-β-lactamase inhibitors.RSC medicinal chemistry · 2025Review
- Active site loops of membrane-anchored metallo-β-lactamases from environmental bacteria determine cephalosporinase activity.Antimicrobial agents and chemotherapy · 2025Article
- First Report in the Americas ofAntibiotics (Basel, Switzerland) · 2025Article
- Emergence of NDM-1- and OXA-23-Co-ProducingMicroorganisms · 2025Article
- OXA β-lactamases frommBio · 2025Article
- Outsmarting Nightmare: Drug Resistance inThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2025Review
- The global prevalence, formation, and evolutionary inference of bacteria co-carrying theFrontiers in microbiology · 2025Article
- Exploiting the fitness cost of metallo-β-lactamase expression can overcome antibiotic resistance in bacterial pathogens.Nature microbiology · 2025Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
Abstract
The worldwide dissemination of metallo-β-lactamases (MBLs), mediating resistance to carbapenem antibiotics, is a major public health problem. The extent of dissemination of MBLs such as VIM-2, SPM-1 and NDM among Gram-negative pathogens cannot be explained solely based on the associated mobile genetic elements or the resistance phenotype. Here, we report that MBL host range is determined by the impact of MBL expression on bacterial fitness. The signal peptide sequence of MBLs dictates their adaptability to each host. In uncommon hosts, inefficient processing of MBLs leads to accumulation of toxic intermediates that compromises bacterial growth. This fitness cost explains the exclusion of VIM-2 and SPM-1 from Escherichia coli and Acinetobacter baumannii, and their confinement to Pseudomonas aeruginosa. By contrast, NDMs are expressed without any apparent fitness cost in different bacteria, and are secreted into outer membrane vesicles. We propose that the successful dissemination and adaptation of MBLs to different bacterial hosts depend on protein determinants that enable host adaptability and carbapenem resistance.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.