ArticleNature chemical biology2016
Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
130 citing papers in PubMed, 1 synthesis or guideline pooled it, 198 citations in OpenAlex.
- Drug-resistantClinical microbiology reviews · 2025Pooled it
- Breaking the deadlock of metallo-β-lactamases: evidence and prospects for Aztreonam/Avibactam.Emerging microbes & infections · 2026Review
- The global epidemiology and treatment of metallo-β-lactamase-producing gram-negative pathogens.JAC-antimicrobial resistance · 2026Review
- Zinc displacement and metabolic interference: cobalt ion-mediated therapy for broad-spectrum CRKP-resistant pneumonia via inhalable microspheres.Nature communications · 2026Article
- Article
- Structural and functional characterization of an active site-influencing variant (IMP-1-F218Y) in IMP-1 metallo-β-lactamase.The FEBS journal · 2026Article
- Synergistic eradication of NDM-1Materials today. Bio · 2026Article
- Predatory myxobacteria lay at the cross-roads of metallo-β-lactamase evolution.Communications biology · 2026Article
- Biochemical and structural analyses of metallo-β-lactamase VIM-28: impact of substitutions at residues 224 and 228 on substrate profile, stability, and zinc affinity.Microbiology spectrum · 2026Article
- Characterization of outer membrane vesicles from Acinetobacter haemolyticus and their role in the dissemination of carbapenem resistance.Medical microbiology and immunology · 2026Article
- NDM-63: a novel NDM metallo-β-lactamase variant in the L3 loop, from aAntimicrobial agents and chemotherapy · 2026Article
- Zinc starvation uncovers bacterial host-specific proteases that shape NDM adaptability inmBio · 2026Article
- Bacterial extracellular vesicles as players in biofilm dynamics and community interactions.FEMS microbiology reviews · 2026Review
- Chelerythrine potentiates meropenem activity against NDM-producing carbapenem-resistant Enterobacteriaceae.Frontiers in veterinary science · 2026Article
- Outer membrane vesicles as a versatile nanoplatform for advanced vaccine development and immunotherapy.Frontiers in immunology · 2026Review
- A One Health perspective on bacterial extracellular vesicles as mediators of antimicrobial resistance spread.ISME communications · 2026Article
- Cooperative antibiotic resistance in bacteria: beyond biofilms.Frontiers in microbiology · 2026Review
- The lipoprotein biosynthesis pathway: key to OXA-mediated carbapenem resistance inAntimicrobial agents and chemotherapy · 2025Article
- Identification of Outer Membrane Vesicles as a New Vehicle Mediating Antibiotic Resistance Gene Transfer in Campylobacter.Journal of extracellular vesicles · 2025Article
- Therapeutic optimization against bacteria carrying metalloenzymes: the battle for class B.Revista espanola de quimioterapia : publicacion oficial de la Sociedad Espanola de Quimioterapia · 2025Review
70 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
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Carbapenems, 'last-resort' β-lactam antibiotics, are inactivated by zinc-dependent metallo-β-lactamases (MBLs). The host innate immune response withholds nutrient metal ions from microbial pathogens by releasing metal-chelating proteins such as calprotectin. We show that metal sequestration is detrimental for the accumulation of MBLs in the bacterial periplasm, because those enzymes are readily degraded in their nonmetallated form. However, the New Delhi metallo-β-lactamase (NDM-1) can persist under conditions of metal depletion. NDM-1 is a lipidated protein that anchors to the outer membrane of Gram-negative bacteria. Membrane anchoring contributes to the unusual stability of NDM-1 and favors secretion of this enzyme in outer-membrane vesicles (OMVs). OMVs containing NDM-1 can protect nearby populations of bacteria from otherwise lethal antibiotic levels, and OMVs from clinical pathogens expressing NDM-1 can carry this MBL and the blaNDM gene. We show that protein export into OMVs can be targeted, providing possibilities of new antibacterial therapeutic strategies.
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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.