Reversible Association of the Hemagglutinin Subcomplex,HA-33/HA-17 Trimer,with the Botulinum Toxin Complex |
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| Authors: | Yoshimasa Sagane Shingo Mutoh Ryosuke Koizumi Tomonori Suzuki Shin-Ichiro Miyashita Keita Miyata Tohru Ohyama Koichi Niwa Toshihiro Watanabe |
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| Institution: | 1.Department of Food and Cosmetic Science, Faculty of Bioindustry,Tokyo University of Agriculture,Abashiri,Japan;2.Department of Nutritional Science and Food Safety, Faculty of Applied Bioscience,Tokyo University of Agriculture,Tokyo,Japan;3.Department of Health and Nutrition, Faculty of Human Science,Hokkaido Bunkyo University,Eniwa,Japan;4.Department of Health and Nutrition, Faculty of Human Science,Hokkaido Bunkyo University,Eniwa,Japan;5.Department of Biomedical Sciences, College of Life and Health Sciences,Chubu University,Kasugai,Japan |
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| Abstract: | Botulinum neurotoxin (BoNT) associates with nontoxic proteins, either a nontoxic nonhemagglutinin (NTNHA) or the complex of NTNHA and hemagglutinin (HA), to form M- or L-toxin complexes (TCs). Single BoNT and NTNHA molecules are associated and form M-TC. A trimer of the 70-kDa HA protein (HA-70) attaches to the M-TC to form M-TC/HA-70. Further, 1–3 arm-like 33- and 17-kDa HA molecules (HA-33/HA-17 trimer), consisting of 1 HA-17 protein and 2 HA-33 proteins, can attach to the M-TC/HA-70 complex, yielding 1-, 2-, and 3-arm L-TC. In this study, the purified 1- and 2-arm L-TCs spontaneously converted into another L-TC species after acquiring the HA-33/HA-17 trimer from other TCs during long-term storage and freezing/thawing. Transmission electron microscopy analysis provided evidence of the formation of detached HA-33/HA-17 trimers in the purified TC preparation. These findings provide evidence of reversible association/dissociation of the M-TC/HA-70 complex with the HA-33/HA-17 trimers, as well as dynamic conversion of the quaternary structure of botulinum TC in culture. |
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