Isolation and characterization of Hc-targeting chimeric heavy chain antibodies neutralizing botulinum neurotoxin type B.
Hc domain
botulinum neurotoxin type B
heavy chain antibody
nanobody
neutralizing antibody
phage display library
Journal
Frontiers in immunology
ISSN: 1664-3224
Titre abrégé: Front Immunol
Pays: Switzerland
ID NLM: 101560960
Informations de publication
Date de publication:
2024
2024
Historique:
received:
02
02
2024
accepted:
11
04
2024
medline:
23
5
2024
pubmed:
23
5
2024
entrez:
23
5
2024
Statut:
epublish
Résumé
Botulinum neurotoxin (BoNT) produced by Herein, neutralizing nanobodies binding to the heavy chain (Hc) domain of BoNT/B (BHc) were screened from a phage display library. Then, BoNT/B-specific clones were identified and fused with the human Fc fragment (hFc) to form chimeric heavy chain antibodies. Finally, the affinity, specificity, and neutralizing activity of antibodies against BoNT/B The B5-hFc, B9-hFc and B12-hFc antibodies demonstrated high affinity for BHc in the nanomolar range. The three antibodies were proven to have potent neutralizing activity against BoNT/B The results demonstrate that inhibiting toxin binding to the host receptor is an efficient strategy and the three antibodies could be used as candidates for the further development of drugs to prevent and treat botulism.
Sections du résumé
Background
UNASSIGNED
Botulinum neurotoxin (BoNT) produced by
Methods
UNASSIGNED
Herein, neutralizing nanobodies binding to the heavy chain (Hc) domain of BoNT/B (BHc) were screened from a phage display library. Then, BoNT/B-specific clones were identified and fused with the human Fc fragment (hFc) to form chimeric heavy chain antibodies. Finally, the affinity, specificity, and neutralizing activity of antibodies against BoNT/B
Results
UNASSIGNED
The B5-hFc, B9-hFc and B12-hFc antibodies demonstrated high affinity for BHc in the nanomolar range. The three antibodies were proven to have potent neutralizing activity against BoNT/B
Conclusion
UNASSIGNED
The results demonstrate that inhibiting toxin binding to the host receptor is an efficient strategy and the three antibodies could be used as candidates for the further development of drugs to prevent and treat botulism.
Identifiants
pubmed: 38779676
doi: 10.3389/fimmu.2024.1380694
pmc: PMC11109933
doi:
Substances chimiques
Antibodies, Neutralizing
0
rimabotulinumtoxinB
0Y70779M1F
Botulinum Toxins, Type A
EC 3.4.24.69
Single-Domain Antibodies
0
Immunoglobulin Heavy Chains
0
Peptide Library
0
Antibodies, Bacterial
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1380694Informations de copyright
Copyright © 2024 Jiang, Wang, Guo, Cheng, Chen, Wang, Li, Du, Gao, Lu, Yu and Yang.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.