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@ARTICLE{Subburaj:127580,
      author       = {Y. Subburaj and U. Ros and E. Hermann and R. Tong and A. J.
                      García-Sáez$^*$},
      title        = {{T}oxicity of an α-pore-forming toxin depends on the
                      assembly mechanism on the target membrane as revealed by
                      single molecule imaging.},
      journal      = {The journal of biological chemistry},
      volume       = {290},
      number       = {8},
      issn         = {1083-351X},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {DKFZ-2017-03603},
      pages        = {4856 - 4865},
      year         = {2015},
      abstract     = {α-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.},
      keywords     = {Cnidarian Venoms (NLM Chemicals) / Pore Forming Cytotoxic
                      Proteins (NLM Chemicals) / equinatoxin (NLM Chemicals)},
      cin          = {B160},
      ddc          = {570},
      cid          = {I:(DE-He78)B160-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25525270},
      pmc          = {pmc:PMC4335225},
      doi          = {10.1074/jbc.M114.600676},
      url          = {https://inrepo02.dkfz.de/record/127580},
}