title: The effect of glycosylation on cytotoxicity of Ibaraki virus nonstructural protein NS3.
abstract: The cytotoxicity of Ibaraki virus nonstructural protein NS3 was confirmed, and the contribution of glycosylation to this activity was examined by using glycosylation mutants of NS3 generated by site-directed mutagenesis. The expression of NS3 resulted in leakage of lactate dehydrogenase to the culture supernatant, suggesting the cytotoxicity of this protein. The lack of glycosylation impaired the transport of NS3 to the plasma membrane and resulted in reduced cytotoxicity. Combined with the previous observation that NS3 glycosylation was specifically observed in mammalian cells (Urata et al., Virus Research 2014), it was suggested that the alteration of NS3 cytotoxicity through modulating glycosylation is one of the strategies to achieve host specific pathogenisity of Ibaraki virus between mammals and vector arthropods.
authors.affiliation: Laboratory of Veterinary Hygiene, Joint Faculty of Veterinary Medicine, Yamaguchi University, 1677-1 Yoshida, Yamaguchi 753-0841, Japan.
authors.forename: Maho
authors.initials: M
authors.lastname: Urata
authors.forename: Rie
authors.initials: R
authors.lastname: Watanabe
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Iwata
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D003588:Cytopathogenic Effect, Viral; D015967:Gene Expression Regulation, Viral / Q000502:physiology*; D006031:Glycosylation; D057809:HEK293 Cells; D006801:Humans; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D018163:Orbivirus / Q000502:physiology*; D017434:Protein Structure, Tertiary; D017361:Viral Nonstructural Proteins / Q000235:genetics / Q000378:metabolism*; D053586:Virus Internalization; D014779:Virus Replication
chemical_list: D017361:Viral Nonstructural Proteins