Abstract
Human parainfluenza virus type 1 (hPIV1) and type 3 (hPIV3) are respiratory pathogen viruses that bind to terminal sialic acids of glycoconjugates on the cell surface hemagglutinin-neuraminidase glycoprotein. Sialic acid residues are linked to the galactose residue primarily by α2,3 or α2,6 linkages on the terminal of glycoprotein or glycolipids. One of the major determinants of pathogenicity or tissue tropism is virus binding or infection specificity for each sialyl linkage. Sialic linkage-modified human blood cells or mammalian cells that mainly have α2,3- or α2,6-linked sialic acid residues on the surface can be prepared by treatment with linkage-specific sialidases or sialyltransferases. These linkage-modified cells can be used in hemagglutination assays to estimate virus particles’ binding specificity, hemadsorption assays to estimate virus glycoproteins’ binding specificity, and virus infectivity assays. These methods contribute to identifying the specificity of sialic acid lineage recognition of the hPIV or other sialic acid-binding viruses.
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Acknowledgments
Keijo Fukushima is a recipient of a scholarship by the Honjo International Scholarship Foundation. This work was supported by JSPS KAKENHI, Series of Single-year Grants, 2510690, in part, and by a MEXT/JSPS KAKENHI Grant (number C; 23590549).
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Fukushima, K., Takahashi, T., Suzuki, T. (2022). Characterization of Human Parainfluenza Virus Receptor Using Terminal Sialic Acid Linkage-Modified Cells. In: Suzuki, Y. (eds) Glycovirology. Methods in Molecular Biology, vol 2556. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2635-1_13
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DOI: https://doi.org/10.1007/978-1-0716-2635-1_13
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