alexa Stabilization of Clostridium botulinum Toxin Complex Using Chemical Crosslinkers
ISSN: 2161-1009

Biochemistry & Analytical Biochemistry
Open Access

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Short Communication

Stabilization of Clostridium botulinum Toxin Complex Using Chemical Crosslinkers

Ajay K. Singh*, David Hodge and Shashi K. Sharma*

Divisions of Microbiology, Center for Food Safety and Applied Nutrition, Food and Drug Administration, College Park, USA

*Corresponding Author:
Ajay K. Singh
Divisions of Microbiology
Center for Food Safety and Applied Nutrition
Food and Drug Administration, College Park, USA
Tel: +1 240- 402-1570/1542
Fax: +1 301-432-2632
E-mail: [email protected]
 
Shashi K. Sharma
Divisions of Microbiology
Center for Food Safety and Applied Nutrition
Food and Drug Administration, College Park, USA
Tel: +1 240-402-1570/1542
Fax: +1 301-432-2632
E-mail: [email protected]

Received Date: February 11, 2015; Accepted Date: May 20, 2015; Published Date: May 25, 2015

Citation: Singh AK, Hodge D, Sharma SK (2015) Stabilization of Clostridium botulinum Toxin Complex Using Chemical Crosslinkers. Biochem Anal Biochem 4:180. doi: 10.4172/2161-1009.1000180

Copyright: © 2015 Singh AK, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Clostridium botulinum produces seven antigenically-distinct botulinum neurotoxins (BoNTs) which cause severe neuroparalytic illness botulism in humans and animals. In bacterial cultures, secreted BoNTs are associated with several neurotoxin-associated proteins (NAPs) forming toxin complexes (TCs). NAPs play an important role in the oral toxicity of BoNTs by protecting toxin from degradation and digestion by gastric acid and proteolytic enzymes. TCs are pH sensitive and can easily dissociate to BoNT and NAPs under neutral to basic pH condition. The stabilization of TCs is critically important for studying interaction domains (NAPs and BoNT), and also to develop better antibodies for the use in BoNT detection methods. In this study, cross-linking of TC was performed with three maleimide base sulfhydryl cross-linking reagents (e.g. 1, 4-bis (maleimido) butane (BMB); 1, 11-bismaleimidotriethyl glycol BM (PEG)3, and Tris (2-maleimidoethyl) amine TMEA) to stabilize TC. Based on cross-linking data of TC, BM (PEG)3 was found to be most suitable amongst three tested cross-linking reagents.

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