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  • Irditoxin, a novel covalently linked heterodimeric three-finger toxin with high taxon-specific neurotoxicity

    Author(s)
    Pawlak, Joanna
    Mackessy, Stephen P
    Sixberry, Nicole M
    Stura, Enrico A
    Le Du, Marie Helene
    Menez, Renee
    Foo, Chun Shin
    Menez, Andre
    Nirthanan, Selvanayagam
    Kini, R Manjunatha
    Griffith University Author(s)
    Nirthanan, Niru
    Year published
    2009
    Metadata
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    Abstract
    A novel heterodimeric three-finger neurotoxin, irditoxin, was isolated from venom of the brown treesnake Boiga irregularis (Colubridae). Irditoxin subunit amino acid sequences were determined by Edman degradation and cDNA sequencing. The crystal structure revealed two subunits with a three-finger protein fold, typical for "nonconventional" toxins such as denmotoxin, bucandin, and candoxin. This is the first colubrid three-finger toxin dimer, covalently connected via an interchain disulfide bond. Irditoxin showed taxon-specific lethality toward birds and lizards and was nontoxic toward mice. It produced a potent neuromuscular ...
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    A novel heterodimeric three-finger neurotoxin, irditoxin, was isolated from venom of the brown treesnake Boiga irregularis (Colubridae). Irditoxin subunit amino acid sequences were determined by Edman degradation and cDNA sequencing. The crystal structure revealed two subunits with a three-finger protein fold, typical for "nonconventional" toxins such as denmotoxin, bucandin, and candoxin. This is the first colubrid three-finger toxin dimer, covalently connected via an interchain disulfide bond. Irditoxin showed taxon-specific lethality toward birds and lizards and was nontoxic toward mice. It produced a potent neuromuscular blockade at the avian neuromuscular junction (IC(50)=10 nM), comparable to alpha-bungarotoxin, but was three orders of magnitude less effective at the mammalian neuromuscular junction. Covalently linked heterodimeric three-finger toxins found in colubrid venoms constitute a new class of venom peptides, which may be a useful source of new neurobiology probes and therapeutic leads.
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    Journal Title
    The FASEB Journal
    Volume
    23
    Issue
    2
    DOI
    https://doi.org/10.1096/fj.08-113555
    Copyright Statement
    © 2009 Federation of American Societies for Experimental Biology. Self-archiving of the author-manuscript version is not yet supported by this publisher. Please refer to the journal link for access to the definitive, published version or contact the authors for more information.
    Subject
    Biochemistry and cell biology
    Zoology
    Basic pharmacology
    Toxicology (incl. clinical toxicology)
    Medical physiology
    Publication URI
    http://hdl.handle.net/10072/34242
    Collection
    • Journal articles

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