The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Phosphoinositide-mediated oligomerization of a defensin induces cell lysis
Open accessAbstract
Cationic antimicrobial peptides (CAPs) such as defensins are ubiquitously found innate immune molecules that often exhibit broad activity against microbial pathogens and mammalian tumor cells. Many CAPs act at the plasma membrane of cells leading to membrane destabilization and permeabilization. In this study, we describe a novel cell lysis mechanism for fungal and tumor cells by the plant defensin NaD1 that acts via direct binding to the plasma membrane phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2). We determined the crystal structure of a NaD1:PIP2 complex, revealing a striking oligomeric arrangement comprising seven dimers of NaD1 that cooperatively bind the anionic headgroups of 14 PIP2 molecules through a unique ‘cationic grip’ configuration. Site-directed mutagenesis of NaD1 confirms that PIP2-mediated oligomerization is important for fungal and tumor cell permeabilization. These observations identify an innate recognition system by NaD1 for direct binding of PIP2 that permeabilizes cells via a novel membrane disrupting mechanism.
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PHENIX : a comprehensive Python-based system for macromolecular structure solution
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Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
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Phosphoinositides in cell regulation and membrane dynamics
Di Paolo, G., & De Camilli, P. (2006) · Nature · doi:10.1038/nature05185 · Cited by 2,790
Plasma membrane phosphoinositide organization by protein electrostatics
McLaughlin, S., & Murray, D. (2005) · Nature · doi:10.1038/nature04398 · Cited by 868
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Cited by
Neutrophil extracellular traps in immunity and disease
Papayannopoulos, V. (2018) · Nature Reviews Immunology · doi:10.1038/nri.2017.105 · Cited by 3,397
Atkin-Smith, G. K., Tixeira, R., Paone, S., Mathivanan, S., Collins, C., Liem, M., Goodall, K. J., Ravichandran, K. S., Hulett, M. D., & Poon, I. K. H. (2015) · Nature Communications · doi:10.1038/ncomms8439 · Cited by 398
Self-citationGulshan, K., Brubaker, G., Conger, H., Wang, S., Zhang, R., Hazen, S. L., & Smith, J. D. (2016) · Circulation Research · doi:10.1161/circresaha.116.308856 · Cited by 66
Analysis of extracellular vesicles generated from monocytes under conditions of lytic cell death
Baxter, A. A., Phan, T. K., Hanssen, E., Liem, M., Hulett, M. D., Mathivanan, S., & Poon, I. K. H. (2019) · Scientific Reports · doi:10.1038/s41598-019-44021-9 · Cited by 60
Self-citationGodwin, J., Djami-Tchatchou, A. T., Velivelli, S. L. S., Tetorya, M., Kalunke, R., Pokhrel, A., Zhou, M., Buchko, G. W., Czymmek, K. J., & Shah, D. M. (2024) · PLOS Pathogens · doi:10.1371/journal.ppat.1012745 · Cited by 6
Metadata
- Authors
- Poon, I. K., Baxter, A. A., Lay, F. T., Mills, G. D., Adda, C. G., Payne, J. A., Phan, T. K., Ryan, G. F., White, J. A., Veneer, P. K., van der Weerden, N. L., Anderson, M. A., Kvansakul, M., & Hulett, M. D.
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2014-04-01
- Volume
- 3
- Pages
- e01808-e01808
- ISSN
- 2050-084X (ISSN-L)
- OpenAlex
- W2109779237
- Cited by
- 185
- References
- 7
- FWCI
- 14.63
- Type
- journal article
- Language
- en
- Open access
- gold
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- Poon, I. K., Baxter, A. A., Lay, F. T., Mills, G. D., Adda, C. G., Payne, J. A., Phan, T. K., Ryan, G. F., White, J. A., Veneer, P. K., van der Weerden, N. L., Anderson, M. A., Kvansakul, M., & Hulett, M. D. (2014). Phosphoinositide-mediated oligomerization of a defensin induces cell lysis. eLife. https://doi.org/10.7554/elife.01808
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
