Sugar-induced conformational change found in the HA-33/HA-17 trimer of the botulinum toxin complex |
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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 |
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| Institution: | 1. Department of Food and Cosmetic Science, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Yasaka, Abashiri, Hokkaido 099-2493, Japan;2. Rigaku Corporation, 3-9-12 Matsubara-Cho, Akishima, Tokyo 196-8666, Japan;3. Department of Bioscience, Faculty of Applied Bioscience, Tokyo University of Agriculture, Setagaya-ku, Tokyo 156-8502, Japan;4. Department of Bacteriology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Kita-ku, Okayama 700-8558, Japan;5. Department of Applied Biological Science, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Tokyo 183-8509, Japan;6. Department of Health and Nutrition, Faculty of Human Science, Hokkaido Bunkyo University, 5-196-1 Kogane-chuo, Eniwa, Hokkaido 061-1449, Japan |
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| 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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| Keywords: | Clostridium botulinum Hemagglutinin Toxin complex Small-angle X-ray scattering Structural dynamics |
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