NDLI: Purification and Characterization of Nontoxic Protein Complex from Serotype D 4947 Botulinum Toxin Complex

Content Provider	Springer Nature Link
Author	Miyata, Keita Sagane, Yoshimasa Inui, Ken Miyashita, Shin Ichiro Suzuki, Tomori Oguma, Keiji Ohyama, Tohru Niwa, Koichi Watanabe, Toshihiro
Copyright Year	2012
Abstract	The large-sized botulinum toxin complex (L-TC) is composed of botulinum neurotoxin (BoNT) and nontoxic proteins, e.g. nontoxic nonhemagglutinin (NTNHA) and three types of hemagglutinins (HAs; HA-33, HA-17 and HA-70). The nontoxic proteins play a critical role in L-TC oral toxicity by protecting the BoNT in the digestive tract, and facilitating absorption of the L-TC across the intestinal wall. Under alkaline conditions, the L-TC separates into BoNT and the nontoxic protein complex (NC). In this study, we established a two-step procedure to yield highly pure NC from the L-TC produced by Clostridium botulinum serotype D strain 4947 in which the NC was isolated from the L-TC by gel filtration under alkaline conditions followed by immunoprecipitation with an anti-BoNT antibody to remove contaminating BoNT from the NC fraction. Western blotting and electrophoretic analysis showed that the highly purified NC fraction had only very slight or no BoNT contamination. In addition, the purified NC fraction showed no intraperitoneal (ip) toxicity to mice at a dose of 38 ng per animal whereas the L-TC exhibited an ip median lethal dose of 0.38 ng per mouse. The highly purified NC displayed the same hemagglutination titer as the L-TC. The NC, as well as the L-TC, demonstrated cell binding and monolayer transport in the rat intestinal epithelial cell line IEC-6. Consequently, the highly purified NC can function as a “delivery vehicle” even without the BoNT.
Starting Page	387
Ending Page	392
Page Count	6
File Format	PDF
ISSN	15723887
Journal	The Protein Journal
Volume Number	31
Issue Number	5
e-ISSN	15734943
Language	English
Publisher	Springer US
Publisher Date	2012-05-08
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Clostridium botulinum Toxin complex Nontoxic protein complex Immunoprecipitation Animal Anatomy / Morphology / Histology Biochemistry Bioorganic Chemistry Organic Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Bioengineering

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