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The structure of the tetanus toxin reveals pH-mediated domain dynamics
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 3
2017 (English)In: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 18, no 8, 1306-1317 p.Article in journal (Refereed) Published
Abstract [en]

The tetanus neurotoxin (TeNT) is a highly potent toxin produced by Clostridium tetani that inhibits neurotransmission of inhibitory interneurons, causing spastic paralysis in the tetanus disease. TeNT differs from the other clostridial neurotoxins by its unique ability to target the central nervous system by retrograde axonal transport. The crystal structure of the tetanus toxin reveals a closed domain arrangement stabilised by two disulphide bridges, and the molecular details of the toxin's interaction with its polysaccharide receptor. An integrative analysis combining X-ray crystallography, solution scattering and single particle electron cryo-microscopy reveals pH-mediated domain rearrangements that may give TeNT the ability to adapt to the multiple environments encountered during intoxication, and facilitate binding to distinct receptors.

Place, publisher, year, edition, pages
2017. Vol. 18, no 8, 1306-1317 p.
Keyword [en]
clostridial toxin, tentoxilysin, tetanospasmin, tetanus neurotoxin
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-145850DOI: 10.15252/embr.201744198ISI: 000406716000010OAI: oai:DiVA.org:su-145850DiVA: diva2:1135628
Available from: 2017-08-23 Created: 2017-08-23 Last updated: 2017-08-23Bibliographically approved

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Masuyer, GeoffreyConrad, JulianStenmark, Pål
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