Expression, purification and comparative characterisation of enzymatically deactivated recombinant botulinum neurotoxin type A
by Weiping Yang, Paul Lindo, Stephen Riding, Tzuu-Wang Chang, Shuowei Cai, Thuan Van, Roshan Kukreja, Yu Zhou, Kruti Vasa, Bal Ram Singh
The Botulinum J. (TBJ), Vol. 1, No. 2, 2008

Abstract: Botulinum Neurotoxin (BoNT) is responsible for botulism, a severe and often deadly disease. Light chain of BoNT behaves as endopeptidase, cleaving the SNARE proteins, and inhibits the neurotransmitter release. A double-mutant E224A/E262A full-length BoNT Type A was successfully cloned and expressed in E. coli. The purified protein lacks the endopeptidase activity involved in the toxic action, and is structurally compatible with the native BoNT/A. Thus this molecule not only can be used as a safe surrogate for study of BoNT, but also can be potentially used as an antidote against botulism, and as a vaccine candidate for botulism.

Online publication date: Tue, 16-Jun-2009

The full text of this article is only available to individual subscribers or to users at subscribing institutions.

 
Existing subscribers:
Go to Inderscience Online Journals to access the Full Text of this article.

Pay per view:
If you are not a subscriber and you just want to read the full contents of this article, buy online access here.

Complimentary Subscribers, Editors or Members of the Editorial Board of the The Botulinum J. (TBJ):
Login with your Inderscience username and password:

Username:        Password:          Forgotten your password?

Want to subscribe?
A subscription gives you complete access to all articles in the current issue, as well as to all articles in the previous three years (where applicable). See our Orders page to subscribe.

If you still need assistance, please email subs@inderscience.com