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Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics. Stockholm Univ, Dept Biochem & Biophys, SE-10691 Stockholm, Sweden.
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2017 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 8, article id 1637Article in journal (Refereed) Published
Abstract [en]

Botulinum neurotoxins (BoNTs), the most potent toxins known, are potential bioterrorism agents. It is well established that all seven serotypes of BoNTs (BoNT/A-G) require complex gangliosides as co-receptors. Here, we report that BoNT/DC, a presumed mosaic toxin between BoNT/D and BoNT/C1, binds and enters efficiently into neurons lacking complex gangliosides and shows no reduction in toxicity in mice deficient in complex gangliosides. The co-crystal structure of BoNT/DC with sialyl-Thomsen-Friedenreich antigen (Sialyl-T) suggests that BoNT/DC recognizes only the sialic acid, but not other moieties in gangliosides. Using liposome flotation assays, we demonstrate that an extended loop in BoNT/DC directly interacts with lipid membranes, and the co-occurring sialic acid binding and loop-membrane interactions mediate the recognition of gangliosides in membranes by BoNT/DC. These findings reveal a unique mechanism for cell membrane recognition and demonstrate that BoNT/DC can use a broad range of sialic acid-containing moieties as co-receptors.

Place, publisher, year, edition, pages
Nature Publishing Group, 2017. Vol. 8, article id 1637
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:umu:diva-142969DOI: 10.1038/s41467-017-01534-zISI: 000416039000005PubMedID: 29158482OAI: oai:DiVA.org:umu-142969DiVA, id: diva2:1166117
Available from: 2017-12-14 Created: 2017-12-14 Last updated: 2017-12-15Bibliographically approved

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