@article{mbs:/content/journal/jgv/10.1099/vir.0.80247-0, author = "Shirato, Kazuya and Miyoshi, Hirotsugu and Goto, Akiko and Ako, Yoshihiko and Ueki, Tomotaka and Kariwa, Hiroaki and Takashima, Ikuo", title = "Viral envelope protein glycosylation is a molecular determinant of the neuroinvasiveness of the New York strain of West Nile virus", journal= "Journal of General Virology", year = "2004", volume = "85", number = "12", pages = "3637-3645", doi = "https://doi.org/10.1099/vir.0.80247-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.80247-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", 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.", }