Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1928639 | Biochemical and Biophysical Research Communications | 2013 | 5 Pages |
Abstract
Large-sized botulinum toxin complex (L-TC) is formed by conjugation of neurotoxin, nontoxic nonhemagglutinin and hemagglutinin (HA) complex. The HA complex is formed by association of three HA-70 molecules and three HA-33/HA-17 trimers, comprised of a single HA-17 and two HA-33 proteins. The HA-33/HA-17 trimer isolated from serotype D L-TC has the ability to bind to and penetrate through the intestinal epithelial cell monolayer in a sialic acid-dependent manner, and thus it plays an important role in toxin delivery through the intestinal cell wall. In this study, we determined the solution structure of the HA-33/HA-17 trimer by using small-angle X-ray scattering (SAXS). The SAXS image of HA-33/HA-17 exhibited broadly similar appearance to the crystal image of the complex. On the other hand, in the presence of N-acetylneuraminic acid, glucose and galactose, the solution structure of the HA-33/HA-17 trimer was drastically altered compared to the structure in the absence of the sugars. Sugar-induced structural change of the HA-33/HA-17 trimer may contribute to cell binding and subsequent transport across the intestinal cell layer.
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Authors
Yoshimasa Sagane, Shintaro Hayashi, Takashi Matsumoto, Shin-Ichiro Miyashita, Ken Inui, Keita Miyata, Shunsuke Yajima, Tomonori Suzuki, Kimiko Hasegawa, Akihito Yamano, Atsushi Nishikawa, Tohru Ohyama, Toshihiro Watanabe, Koichi Niwa,