The structure of the tetanus toxin reveals pH-mediated domain dynamics
Masuyer, Geoffrey ; Conrad, Julian and Stenmark, Pål LU
(2017)
In EMBO Reports
18(8).
p.1306-1317
- Abstract
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... (More)
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.Update
(Less)
- author
- Masuyer, Geoffrey
; Conrad, Julian
and Stenmark, Pål
LU
- publishing date
- 2017-08
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Animals, Crystallography, X-Ray, Humans, Hydrogen-Ion Concentration, Metalloendopeptidases/chemistry, Microscopy, Electron, Neurotoxins/chemistry, Protein Binding, Protein Domains, Synaptic Transmission/drug effects, Tetanus Toxin/chemistry
- in
- EMBO Reports
- volume
- 18
- issue
- 8
- pages
- 12 pages
- publisher
- Nature Publishing Group
- external identifiers
-
- pmid:28645943
- scopus:85021346163
- ISSN
- 1469-221X
- DOI
- 10.15252/embr.201744198
- language
- English
- LU publication?
- no
- additional info
- © 2017 The Authors.
- id
- acbeef57-4705-4076-bc59-a524dc4cda30
- date added to LUP
- 2019-04-30 07:55:35
- date last changed
- 2024-04-02 02:19:19
@article{acbeef57-4705-4076-bc59-a524dc4cda30,
abstract = {{<p>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.Update</p>}},
author = {{Masuyer, Geoffrey and Conrad, Julian and Stenmark, Pål}},
issn = {{1469-221X}},
keywords = {{Animals; Crystallography, X-Ray; Humans; Hydrogen-Ion Concentration; Metalloendopeptidases/chemistry; Microscopy, Electron; Neurotoxins/chemistry; Protein Binding; Protein Domains; Synaptic Transmission/drug effects; Tetanus Toxin/chemistry}},
language = {{eng}},
number = {{8}},
pages = {{1306--1317}},
publisher = {{Nature Publishing Group}},
series = {{EMBO Reports}},
title = {{The structure of the tetanus toxin reveals pH-mediated domain dynamics}},
url = {{http://dx.doi.org/10.15252/embr.201744198}},
doi = {{10.15252/embr.201744198}},
volume = {{18}},
year = {{2017}},
}