Botulinum Toxin Accessory Proteins: Are They Just an Accessory?
Journal
Dermatologic surgery : official publication for American Society for Dermatologic Surgery [et al.]
ISSN: 1524-4725
Titre abrégé: Dermatol Surg
Pays: United States
ID NLM: 9504371
Informations de publication
Date de publication:
12 Jun 2024
12 Jun 2024
Historique:
medline:
12
6
2024
pubmed:
12
6
2024
entrez:
12
6
2024
Statut:
aheadofprint
Résumé
Botulinum neurotoxins produced by Clostridium botulinum consist of a complex of a core neurotoxin protein and one or more nontoxin accessory proteins. The accessory proteins are generally thought to protect the neurotoxin from the gastric environment in botulism poisoning, dissociating away upon absorption. Other than their questionable immunogenicity, they are rarely mentioned in botulinum toxin therapy. To review evidence that accessory proteins potentially play a role in neurotoxin activity. Evidence suggests that the accessory proteins do not dissociate from the neurotoxin complex and enhance neurotoxin activity. Complexed type A botulinum toxin has dramatically higher endopeptidase activity than noncomplexed neurotoxin. A primary accessory protein, hemagglutinin-33, exhibits this same effect on both type A and type E core neurotoxin proteins, the latter not natively having this accessory protein. A clinical study using an objective computer assessment assay has shown a correlation between type A complex size and glabellar strain reduction, which reflects increasing clinical efficacy. Finally, a systematic review found no correlation between type A complex size and neutralizing antibody formation. Accessory proteins may play a role in the efficacy of botulinum toxin and could remain complexed to the neurotoxin for longer than previously reported.
Sections du résumé
BACKGROUND
BACKGROUND
Botulinum neurotoxins produced by Clostridium botulinum consist of a complex of a core neurotoxin protein and one or more nontoxin accessory proteins. The accessory proteins are generally thought to protect the neurotoxin from the gastric environment in botulism poisoning, dissociating away upon absorption. Other than their questionable immunogenicity, they are rarely mentioned in botulinum toxin therapy.
OBJECTIVE
OBJECTIVE
To review evidence that accessory proteins potentially play a role in neurotoxin activity.
RESULTS
RESULTS
Evidence suggests that the accessory proteins do not dissociate from the neurotoxin complex and enhance neurotoxin activity. Complexed type A botulinum toxin has dramatically higher endopeptidase activity than noncomplexed neurotoxin. A primary accessory protein, hemagglutinin-33, exhibits this same effect on both type A and type E core neurotoxin proteins, the latter not natively having this accessory protein. A clinical study using an objective computer assessment assay has shown a correlation between type A complex size and glabellar strain reduction, which reflects increasing clinical efficacy. Finally, a systematic review found no correlation between type A complex size and neutralizing antibody formation.
CONCLUSION
CONCLUSIONS
Accessory proteins may play a role in the efficacy of botulinum toxin and could remain complexed to the neurotoxin for longer than previously reported.
Identifiants
pubmed: 38864825
doi: 10.1097/DSS.0000000000004284
pii: 00042728-990000000-00844
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2024 by the American Society for Dermatologic Surgery, Inc. Published by Wolters Kluwer Health, Inc. All rights reserved.
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