Production of monoclonal antibodies against botulinum neurotoxin in Nicotiana benthamiana

Production of monoclonal antibodies against botulinum neurotoxin in Nicotiana benthamiana

Botulism is a fatal neurologic disease caused by the botulinum toxin (BoNT) produced by . It is a rare but highly toxic disease with symptoms, such as cramps, nausea, vomiting, diarrhea, dysphagia, respiratory failure, muscle weakness, and even death. Currently, two types of antitoxin are used: equi...

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Bibliographic Details
Published in:Human vaccines & immunotherapeutics Vol. 20; no. 1; p. 2329446
Main Authors: Sangprasat, Kornchanok, Bulaon, Christine Joy I, Rattanapisit, Kaewta, Srisangsung, Theerakarn, Jirarojwattana, Perawat, Wongwatanasin, Apidsada, Phoolcharoen, Waranyoo
Format: Journal Article
Language:English
Published: United States Taylor & Francis 31-12-2024
Taylor & Francis Group
Subjects:
Animals
Antibodies, Monoclonal
Antitoxins
botulinum neurotoxin
Botulinum Toxins, Type A
Botulism
Botulism - prevention & control
Clostridium botulinum
Horses
Humans
Immunotherapy - Other
monoclonal antibody
Nicotiana
Nicotiana benthamiana
Nicotiana benthamiana
Botulism
Clostridium botulinum
monoclonal antibody
botulinum neurotoxin
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Summary:Botulism is a fatal neurologic disease caused by the botulinum toxin (BoNT) produced by . It is a rare but highly toxic disease with symptoms, such as cramps, nausea, vomiting, diarrhea, dysphagia, respiratory failure, muscle weakness, and even death. Currently, two types of antitoxin are used: equine-derived heptavalent antitoxin and human-derived immunoglobulin (BabyBIG®). However, heptavalent treatment may result in hypersensitivity, whereas BabyBIG®, has a low yield. The present study focused on the development of three anti-BoNT monoclonal antibodies (mAbs), 1B18, C25, and M2, in . The plant-expressed mAbs were purified and examined for size, purity and integrity by SDS-PAGE, western blotting and size-exclusion chromatography. Analysis showed that plant-produced anti-BoNT mAbs can fully assemble in plants, can be purified in a single purification step, and mostly remain as monomeric proteins. The efficiency of anti-BoNT mAbs binding to BoNT/A and B was then tested. Plant-produced 1B18 retained its ability to recognize both mBoNT/A1 and ciBoNT/B1. At the same time, the binding specificities of two other mAbs were determined: C25 for mBoNT/A1 and M2 for ciBoNT/B1. In conclusion, our results confirm the use of plants as an alternative platform for the production of anti-BoNT mAbs. This plant-based technology will serve as a versatile system for the development botulism immunotherapeutics.
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ISSN:2164-5515
2164-554X
DOI:10.1080/21645515.2024.2329446