ArticleAntimicrobial agents and chemotherapy2021
Specific Protein-Membrane Interactions Promote Packaging of Metallo-β-Lactamases into Outer Membrane Vesicles.
Article in Antimicrobial agents and chemotherapy, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed.
- Characterization of outer membrane vesicles from Acinetobacter haemolyticus and their role in the dissemination of carbapenem resistance.Medical microbiology and immunology · 2026Article
- NDM-5-carried outer membrane vesicles impair the efficacy of antibiotics against bacterial infections.Antimicrobial agents and chemotherapy · 2025Article
- OXA β-lactamases frommBio · 2025Article
- OXA β-lactamases frombioRxiv : the preprint server for biology · 2024Article
- Microbial extracellular vesicles contribute to antimicrobial resistance.PLoS pathogens · 2024Review
- Quantitative Proteomic Analysis of Outer Membrane Vesicles from Fusobacterium nucleatum Cultivated in the Mimic Cancer Environment.Microbiology spectrum · 2023Article
- Review
- In silico designing and immunoinformatics analysis of a novel peptide vaccine against metallo-beta-lactamase (VIM and IMP) variants.PloS one · 2023Article
- The biogenesis of β-lactamase enzymes.Microbiology (Reading, England) · 2022Review
- Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Outer membrane vesicles (OMVs) act as carriers of bacterial products such as plasmids and resistance determinants, including metallo-β-lactamases. The lipidated, membrane-anchored metallo-β-lactamase NDM-1 can be detected in Gram-negative OMVs. The soluble domain of NDM-1 also forms electrostatic interactions with the membrane. Here, we show that these interactions promote its packaging into OMVs produced by Escherichia coli. We report that favorable electrostatic protein-membrane interactions are also at work in the soluble enzyme IMP-1 while being absent in VIM-2. These interactions correlate with an enhanced incorporation of IMP-1 compared to VIM-2 into OMVs. Disruption of these interactions in NDM-1 and IMP-1 impairs their inclusion into vesicles, confirming their role in defining the protein cargo in OMVs. These results also indicate that packaging of metallo-β-lactamases into vesicles in their active form is a common phenomenon that involves cargo selection based on specific molecular interactions.
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Registered trials
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