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Structural Analysis...
Structural Analysis of Botulinum Neurotoxins Type B and E by Cryo-EM
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- Kosenina, Sara (author)
- Stockholm University,Stockholms universitet,Institutionen för biokemi och biofysik
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- Martínez-Carranza, Markel (author)
- Stockholm University,Stockholms universitet,Institutionen för biokemi och biofysik
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- Davies, Jonathan R. (author)
- Stockholm University,Stockholms universitet,Institutionen för biokemi och biofysik
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- Masuyer, Geoffrey (author)
- Stockholm University,Stockholms universitet,Institutionen för biokemi och biofysik,University of Bath, UK
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- Stenmark, Pål (author)
- Stockholm University,Lunds universitet,Stockholms universitet,Institutionen för biokemi och biofysik,Lund University, Sweden,Strukturell biokemi,Forskargrupper vid Lunds universitet,LUCC: Lunds universitets cancercentrum,Övriga starka forskningsmiljöer,Structural Biochemistry,Lund University Research Groups,LUCC: Lund University Cancer Centre,Other Strong Research Environments
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(creator_code:org_t)
- 2021-12-23
- 2022
- English.
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In: Toxins. - : MDPI AG. - 2072-6651. ; 14:1
- Related links:
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https://doi.org/10.3...
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http://dx.doi.org/10... (free)
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https://urn.kb.se/re...
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https://doi.org/10.3...
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Abstract
Subject headings
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- Botulinum neurotoxins (BoNTs) are the causative agents of a potentially lethal paralytic disease targeting cholinergic nerve terminals. Multiple BoNT serotypes exist, with types A, B and E being the main cause of human botulism. Their extreme toxicity has been exploited for cosmetic and therapeutic uses to treat a wide range of neuromuscular disorders. Although naturally occurring BoNT types share a common end effect, their activity varies significantly based on the neuronal cell-surface receptors and intracellular SNARE substrates they target. These properties are the result of structural variations that have traditionally been studied using biophysical methods such as X-ray crystallography. Here, we determined the first structures of botulinum neurotoxins using single-particle cryogenic electron microscopy. The maps obtained at 3.6 and 3.7 Å for BoNT/B and /E, respectively, highlight the subtle structural dynamism between domains, and of the binding domain in particular. This study demonstrates how the recent advances made in the field of single-particle electron microscopy can be applied to bacterial toxins of clinical relevance and the botulinum neurotoxin family in particular.
Subject headings
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Clostridium botulinum
- botulism
- botulinum neurotoxin
- BoNT
- B
- E
- cryo-EM
- BoNT/B
- BoNT/E
- Botulinum neurotoxin
- Botulism
- Clostridium botulinum
- Cryo-EM
Publication and Content Type
- ref (subject category)
- art (subject category)
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