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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 \u2018cationic grip\u2019 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.<\/jats:p>","DOI":"10.7554\/elife.01808","type":"journal-article","created":{"date-parts":[[2014,4,1]],"date-time":"2014-04-01T11:57:15Z","timestamp":1396353435000},"source":"Crossref","is-referenced-by-count":176,"title":["Phosphoinositide-mediated oligomerization of a defensin induces cell lysis"],"prefix":"10.7554","volume":"3","author":[{"given":"Ivan KH","family":"Poon","sequence":"first","affiliation":[{"name":"Department of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amy A","family":"Baxter","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, 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