The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase
Open accessAbstract
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, since these enzymes are readily degraded in their non-metallated form. However, the New Delhi Metallo-β-lactamase (NDM-1) is able to persist under conditions of metal depletion. NDM-1 is a lipidated protein anchored 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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NIH Image to ImageJ: 25 years of image analysis
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Nutritional immunity: transition metals at the pathogen–host interface
Hood, M. I., & Skaar, E. P. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2836 · Cited by 1,535
Antimicrobial psoriasin (S100A7) protects human skin from Escherichia coli infection
Gläser, R., Harder, J., Lange, H., Bartels, J., Christophers, E., & Schröder, J.-M. (2005) · Nature Immunology · doi:10.1038/ni1142 · Cited by 651
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ZnuA and zinc homeostasis in Pseudomonas aeruginosa
Pederick, V. G., Eijkelkamp, B. A., Begg, S. L., Ween, M. P., McAllister, L. J., Paton, J. C., & McDevitt, C. A. (2015) · Scientific Reports · doi:10.1038/srep13139 · Cited by 138 · cited 1×
“Moreover, some prokaryotes use ribosomal proteins as a Zn(II) store 43 .”
Haley, K. P., Delgado, A. G., Piazuelo, M. B., Mortensen, B. L., Correa, P., Damo, S. M., Chazin, W. J., Skaar, E. P., & Gaddy, J. A. (2015) · Infection and Immunity · doi:10.1128/iai.00544-15 · Cited by 68
Cited by
The rapid spread of carbapenem-resistant Enterobacteriaceae
Potter, R. F., D’Souza, A. W., & Dantas, G. (2016) · Drug Resistance Updates · doi:10.1016/j.drup.2016.09.002 · Cited by 403
Bacterial Outer Membrane Vesicles: From Discovery to Applications
Sartorio, M. G., Pardue, E. J., Feldman, M. F., & Haurat, M. F. (2021) · Annual Review of Microbiology · doi:10.1146/annurev-micro-052821-031444 · Cited by 398
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Self-citationMolecular Evolution of Transition Metal Bioavailability at the Host–Pathogen Interface
Antelo, G. T., Vila, A. J., Giedroc, D. P., & Capdevila, D. A. (2021) · Trends in Microbiology · doi:10.1016/j.tim.2020.08.001 · Cited by 63
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Metadata
- Authors
- González, L. J., Bahr, G., Nakashige, T. G., Nolan, E. M., Bonomo, R. A., & Vila, A. J.
- Venue
- Nature Chemical Biology
- Published
- 2016-05-16
- Volume
- 12
- Issue
- 7
- Pages
- 516-522
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2397232002
- Cited by
- 208
- References
- 6
- FWCI
- 5.25
- Type
- journal article
- Language
- en
- Open access
- bronze
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- González, L. J., Bahr, G., Nakashige, T. G., Nolan, E. M., Bonomo, R. A., & Vila, A. J. (2016). Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase. Nature Chemical Biology. https://doi.org/10.1038/nchembio.2083
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