%0 Journal Article %A Shirato, Kazuya %A Miyoshi, Hirotsugu %A Goto, Akiko %A Ako, Yoshihiko %A Ueki, Tomotaka %A Kariwa, Hiroaki %A Takashima, Ikuo %T Viral envelope protein glycosylation is a molecular determinant of the neuroinvasiveness of the New York strain of West Nile virus %D 2004 %J Journal of General Virology, %V 85 %N 12 %P 3637-3645 %@ 1465-2099 %R https://doi.org/10.1099/vir.0.80247-0 %I Microbiology Society, %X 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. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.80247-0