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Comparative Immunochemical Characteristics of Botulinum Neurotoxin Type A and its Associated Proteins.
MedLine Citation:
PMID:  23811077     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Clostridium botulinum strains secrete their neurotoxins (BoNT) along with a group of neurotoxin-associated proteins (NAPs) that enhance the oral toxicity and provide protection to the neurotoxin against acidity, temperature and proteases in the G.I. tract. A major component of NAPs is Hn-33, a 33kDa protein, which is also protease resistant and strongly protects BoNT. The complex form of BoNT/A is used as a commercial therapeutic formulation against many neuromuscular disorders and for cosmetic purposes. Immune response against this formulation could hinder its long-term use; therefore, it is important to characterize the immunological properties of the associated proteins. This study aims to understand the immunological reactivity of BoNT/A complex, BoNT, NAPs, and Hn-33 through a series of competitive enzyme-linked immunosorbent assays (ELISA). The results indicated that BoNT/A complex competed 6 times more with complex antibodies compared to the neurotoxin confirming that the higher immunogenicity of BoNT/A complex was indeed a result of the associated proteins with the neurotoxin complex. While the nearly identical immuno-reactivity of BoNT/A complex and Hn-33 with Hn-33 antibodies indicated that the reactivity was due to the higher immunogenicity not the abundance of Hn-33 in the complex. Both the ELISA and immuno-blot results implied that Hn-33 is primarily responsible for eliciting the antibody response in BoNT/A complex, therefore it may be possible to employ Hn-33 as an adjuvant for development of vaccines against botulism.
Authors:
Anne-Marie Bryant; Shuowei Cai; Bal Ram Singh
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-6-27
Journal Detail:
Title:  Toxicon : official journal of the International Society on Toxinology     Volume:  -     ISSN:  1879-3150     ISO Abbreviation:  Toxicon     Publication Date:  2013 Jun 
Date Detail:
Created Date:  2013-7-1     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  1307333     Medline TA:  Toxicon     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013 Elsevier Ltd. All rights reserved.
Affiliation:
Botulinum Research Center and Department of Chemistry and Biochemistry, University of Massachusetts Dartmouth, 285 Old Westport Road, North Dartmouth, MA 02747.
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