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2z5a

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Revision as of 18:48, 22 May 2008

Image:2z5a.jpg

Template:STRUCTURE 2z5a

HA3 subcomponent of botulinum type C progenitor toxin


Overview

It has been reported that Clostridium botulinum type C 16S progenitor toxin (C16S toxin) first binds to the sialic acid on the cell surface of mucin before invading cells [A. Nishikawa, N. Uotsu, H. Arimitsu, J.C. Lee, Y. Miura, Y. Fujinaga, H. Nakada, T. Watanabe, T. Ohyama, Y. Sakano, K. Oguma, The receptor and transporter for internalization of Clostridium botulinum type C progenitor toxin into HT-29 cells, Biochem. Biophys. Res. Commun. 319 (2004) 327-333]. In this study we investigated the binding properties of the C16S toxin to glycoproteins. Although the toxin bound to membrane blotted mucin derived from the bovine submaxillary gland (BSM), which contains a lot of sialyl oligosaccharides, it did not bind to neuraminidase-treated BSM. The binding of the toxin to BSM was inhibited by N-acetylneuraminic acid, N-glycolylneuraminic acid, and sialyl oligosaccharides strongly, but was not inhibited by neutral oligosaccharides. Both sialyl alpha2-3 lactose and sialyl alpha2-6 lactose prevented binding similarly. On the other hand, the toxin also bound well to porcine gastric mucin. In this case, neutral oligosaccharides might play an important role as ligand, since galactose and lactose inhibited binding. These results suggest that the toxin is capable of recognizing a wide variety of oligosaccharide structures.

About this Structure

2Z5A is a Protein complex structure of sequences from Clostridium botulinum d phage. Full crystallographic information is available from OCA.

Reference

Binding properties of Clostridium botulinum type C progenitor toxin to mucins., Nakamura T, Takada N, Tonozuka T, Sakano Y, Oguma K, Nishikawa A, Biochim Biophys Acta. 2007 Apr;1770(4):551-5. Epub 2006 Nov 23. PMID:17196748 Page seeded by OCA on Thu May 22 21:48:00 2008

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