NDLI: Effect of Nicking the C-terminal Region of the Clostridium botulinum Serotype D Neurotoxin Heavy Chain on its Toxicity and Molecular Properties

Content Provider	Springer Nature Link
Author	Suzuki, Tomori Kouguchi, Hirokazu Watanabe, Toshihiro Hasegawa, Kimiko Yoneyama, Tohru Niwa, Koichi Nishikawa, Atsushi Lee, Jae Chul Oguma, Keiji Ohyama, Tohru
Copyright Year	2007
Abstract	A unique strain of Clostridium botulinum serotype D 4947 produces toxin complexes that are composed of un-nicked components, including a neurotoxin (BoNT) and auxiliary proteins. This BoNT showed aberrant elution upon Superdex gel filtration, indicating a much lower molecular weight, due to hydrophobic interaction with the column. Limited trypsin proteolysis of BoNT produces two nicks; first nick yielded a BoNT 50 kDa light chain disulfide linked to a 100 kDa heavy chain (Hc), and a second nick arose in Hc C-terminal 10 kDa. The second nick occurred in the putative binding domain of the BoNT molecule and induced alterations in its secondary structure, leading to a significant reduction of mouse toxicity in comparison with that of the fully-activated singly nicked BoNT. These results help to clarify the role of the C-terminal half of the Hc in the oral toxicity of single-chain and more complex forms of BoNT.
Starting Page	173
Ending Page	181
Page Count	9
File Format	PDF
ISSN	15723887
Journal	The Protein Journal
Volume Number	26
Issue Number	3
e-ISSN	15734943
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2007-01-03
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Clostridium botulinum neurotoxin nicking receptor binding domain structure Animal Anatomy / Morphology / Histology Organic Chemistry Biochemistry Bioorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Bioengineering

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Mapping of the Synaptosome-Binding Regions on the Heavy Chain of Botulinum Neurotoxin A By Synthetic Overlapping Peptides Encompassing the Entire Chain

Subunit Stoichiometry of the Clostridium botulinum Type A Neurotoxin Complex Determined Using Denaturing Capillary Electrophoresis

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Botulinum Neurotoxin Light Chain Refolds at Endosomal pH for its Translocation

Characterization of Toxin Complex Produced by a Unique Strain of Clostridium botulinum Serotype D 4947

In Vitro Translation of Type A Clostridium botulinum Neurotoxin Heavy Chain and Analysis of Its Binding to Rat Synaptosomes

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Effect of Nicking the C-terminal Region of the Clostridium botulinum Serotype D Neurotoxin Heavy Chain on its Toxicity and Molecular Properties

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