Molecular engineering of a minimal E-cadherin inhibitor protein derived from Clostridium botulinum hemagglutinin.
Clostridium botulinum
E-cadherin inhibitor
cell–cell adhesion
epithelial barrier disruption
hemagglutinin
iPSC culture system
molecular engineering
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
03 2023
03 2023
Historique:
received:
02
11
2022
revised:
19
01
2023
accepted:
20
01
2023
medline:
29
3
2023
pubmed:
28
1
2023
entrez:
27
1
2023
Statut:
ppublish
Résumé
Hemagglutinin (HA), a nontoxic component of the botulinum neurotoxin (BoNT) complex, binds to E-cadherin and inhibits E-cadherin-mediated cell-cell adhesion. HA is a 470 kDa protein complex comprising six HA1, three HA2, and three HA3 subcomponents. Thus, to prepare recombinant full-length HA in vitro, it is necessary to reconstitute the macromolecular complex from purified HA subcomponents, which involves multiple purification steps. In this study, we developed NanoHA, a minimal E-cadherin inhibitor protein derived from Clostridium botulinum HA with a simple purification strategy needed for production. NanoHA, containing HA2 and a truncated mutant of HA3 (amino acids 380-626; termed as HA3
Identifiants
pubmed: 36707052
pii: S0021-9258(23)00076-5
doi: 10.1016/j.jbc.2023.102944
pmc: PMC9958082
pii:
doi:
Substances chimiques
Botulinum Toxins
EC 3.4.24.69
Cadherins
0
Hemagglutinins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102944Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interests The authors declare that they have no conflicts of interest with the contents of this article.