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J Gen Virol 85 (2004), 3637-3645; DOI 10.1099/vir.0.80247-0

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© 2004 Society for General Microbiology

Viral envelope protein glycosylation is a molecular determinant of the neuroinvasiveness of the New York strain of West Nile virus

Kazuya Shirato, Hirotsugu Miyoshi, Akiko Goto, Yoshihiko Ako, Tomotaka Ueki, Hiroaki Kariwa and Ikuo Takashima

Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan

Correspondence
Ikuo Takashima
takasima{at}vetmed.hokudai.ac.jp

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.

The GenBank/EMBL/DDBJ accession numbers for the sequences described in this paper are AB185914–AB185917.




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