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000127580 0247_ $$2doi$$a10.1074/jbc.M114.600676
000127580 0247_ $$2pmid$$apmid:25525270
000127580 0247_ $$2pmc$$apmc:PMC4335225
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000127580 0247_ $$2ISSN$$a1083-351X
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000127580 037__ $$aDKFZ-2017-03603
000127580 041__ $$aeng
000127580 082__ $$a570
000127580 1001_ $$aSubburaj, Yamunadevi$$b0
000127580 245__ $$aToxicity of an α-pore-forming toxin depends on the assembly mechanism on the target membrane as revealed by single molecule imaging.
000127580 260__ $$aBethesda, Md.$$bSoc.$$c2015
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000127580 520__ $$aα-Pore-forming toxins (α-PFTs) are ubiquitous defense tools that kill cells by opening pores in the target cell membrane. Despite their relevance in host/pathogen interactions, very little is known about the pore stoichiometry and assembly pathway leading to membrane permeabilization. Equinatoxin II (EqtII) is a model α-PFT from sea anemone that oligomerizes and forms pores in sphingomyelin-containing membranes. Here, we determined the spatiotemporal organization of EqtII in living cells by single molecule imaging. Surprisingly, we found that on the cell surface EqtII did not organize into a unique oligomeric form. Instead, it existed as a mixture of oligomeric species mostly including monomers, dimers, tetramers, and hexamers. Mathematical modeling based on our data supported a new model in which toxin clustering happened in seconds and proceeded via condensation of EqtII dimer units formed upon monomer association. Furthermore, altering the pathway of EqtII assembly strongly affected its toxic activity, which highlights the relevance of the assembly mechanism on toxicity.
000127580 536__ $$0G:(DE-HGF)POF3-312$$a312 - Functional and structural genomics (POF3-312)$$cPOF3-312$$fPOF III$$x0
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000127580 650_7 $$2NLM Chemicals$$aCnidarian Venoms
000127580 650_7 $$2NLM Chemicals$$aPore Forming Cytotoxic Proteins
000127580 650_7 $$054578-46-0$$2NLM Chemicals$$aequinatoxin
000127580 7001_ $$aRos, Uris$$b1
000127580 7001_ $$aHermann, Eduard$$b2
000127580 7001_ $$aTong, Rudi$$b3
000127580 7001_ $$0P:(DE-HGF)0$$aGarcía-Sáez, Ana J$$b4$$eLast author
000127580 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M114.600676$$gVol. 290, no. 8, p. 4856 - 4865$$n8$$p4856 - 4865$$tThe journal of biological chemistry$$v290$$x1083-351X$$y2015
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000127580 9141_ $$y2015
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