title: Viral envelope protein glycosylation is a molecular determinant of the neuroinvasiveness of the New York strain of West Nile virus.
abstract: Two New York (NY) strains of the West Nile (WN) virus were plaque-purified and four variants that had different amino acid sequences at the N-linked glycosylation site in the envelope (E) protein sequence were isolated. The E protein was glycosylated in only two of these strain variants. To determine the relationship between E protein glycosylation and pathogenicity of the WN virus, 6-week-old mice were infected subcutaneously with these variants. Mice infected with viruses that carried the glycosylated E protein developed lethal infection, whereas mice infected with viruses that carried the non-glycosylated E protein showed low mortality. In contrast, intracerebral infection of mice with viruses carrying either the glycosylated or non-glycosylated forms of the E protein resulted in lethal infection. These results suggested that E protein glycosylation is a molecular determinant of neuroinvasiveness in the NY strains of WN virus.
authors.affiliation: Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan.
authors.forename: Kazuya
authors.initials: K
authors.lastname: Shirato
authors.affiliation: Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan.
authors.forename: Hirotsugu
authors.initials: H
authors.lastname: Miyoshi
authors.affiliation: Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan.
authors.forename: Akiko
authors.initials: A
authors.lastname: Goto
authors.affiliation: Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan.
authors.forename: Yoshihiko
authors.initials: Y
authors.lastname: Ako
authors.affiliation: Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan.
authors.forename: Tomotaka
authors.initials: T
authors.lastname: Ueki
authors.affiliation: Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan.
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Kariwa
authors.affiliation: Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan.
authors.forename: Ikuo
authors.initials: I
authors.lastname: Takashima
mesh_terms: D000818:Animals; D001483:Base Sequence; D015153:Blotting, Western; D001921:Brain / Q000821:virology*; D006224:Cricetinae; D005260:Female; D006031:Glycosylation; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000502:physiology*; D014774:Virulence; D014779:Virus Replication; D014902:West Nile virus / Q000472:pathogenicity*
chemical_list: D014759:Viral Envelope Proteins; C065696:glycoprotein E, Flavivirus