Abstract |
Affinity-matured human antibodies have demonstrated efficacy as countermeasures for exposure to botulinum neurotoxin (BoNT), which is the cause of the disease botulism category A select bioterror agent. Little is known, however, about the potential role of natural (un-mutated) antibodies in the protective immune response to BoNT. Here we describe the cloning of two human IgM antibodies that bind serotype A BoNT. Both are un-mutated IgM antibodies, consistent with an origin in naive B cells. One of the antibodies is able to fully neutralize a lethal dose of serotype A BoNT in vivo. These results suggest that the natural human antibody repertoire may play a role in protection from exposure to biological toxins.
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Authors | Sharad P Adekar, Fetweh H Al-Saleem, M D Elias, Katherine A Rybinski, Lance L Simpson, Scott K Dessain |
Journal | Hybridoma (2005)
(Hybridoma (Larchmt))
Vol. 27
Issue 2
Pg. 65-9
(Apr 2008)
ISSN: 1554-0014 [Print] United States |
PMID | 18642670
(Publication Type: Journal Article, Research Support, N.I.H., Extramural)
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Chemical References |
- Antibodies, Bacterial
- Immunoglobulin M
- rimabotulinumtoxinB
- Botulinum Toxins
- Botulinum Toxins, Type A
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Topics |
- Amino Acid Sequence
- Antibodies, Bacterial
(administration & dosage, metabolism, physiology)
- Binding Sites, Antibody
- Botulinum Toxins
(antagonists & inhibitors, immunology, metabolism)
- Botulinum Toxins, Type A
(antagonists & inhibitors, immunology, metabolism)
- Botulism
(immunology, prevention & control)
- Cell Line, Tumor
- Cells, Cultured
- Clostridium botulinum
(immunology)
- Humans
- Hybridomas
- Immunoglobulin M
(administration & dosage, metabolism, physiology)
- Molecular Sequence Data
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