Abstract
Rotaviruses are the major etiologic agents of acute gastroenteritis. Viral attachment to the cell surface is crucial to initiate infection. The VP8∗ domain, the trypsinized cleavage fragment of the outermost spike protein VP4 of rotavirus, has a galectin-like structure required for binding to the cell surface. We used the evanescent-field fluorescence-assisted assay to understand the complex mechanism underlying the virus-glycan/glycoprotein interaction. Besides, we have described virus infection assays, neutralization assay, and pretreatment assay, using cell culture. These approaches using rotavirus particles will provide novel information that has been difficult to obtain from glycan microarray using recombinant VP8∗.
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Acknowledgments
We appreciate Dr. Osamu Nakagomi, Dr. Toyoko Nakagomi, Dr. Makoto Sugiyama, and Dr. Naoto Ito for their contribution in describing the virus purification. This work was supported by the Japan Society for the Promotion of Science [JSPS, Tokyo, Japan; Grant-in-Aid for Scientific Research (C) no. 17K08398 (to K.Y.) and 18K05504 (to M.I.)].
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Yamada, K., Nio-Kobayashi, J., Inagaki, M. (2020). Screening for Components/Compounds with Anti-Rotavirus Activity: Detection of Interaction Between Viral Spike Proteins and Glycans. In: Hirabayashi, J. (eds) Lectin Purification and Analysis. Methods in Molecular Biology, vol 2132. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0430-4_50
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DOI: https://doi.org/10.1007/978-1-0716-0430-4_50
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