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

J Gen Virol. 2004 Dec;85(Pt 12):3637-3645. doi: 10.1099/vir.0.80247-0.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Blotting, Western
  • Brain / virology*
  • Cricetinae
  • Female
  • Glycosylation
  • Male
  • Mice
  • Mice, Inbred BALB C
  • Molecular Sequence Data
  • Viral Envelope Proteins / chemistry
  • Viral Envelope Proteins / physiology*
  • Virulence
  • Virus Replication
  • West Nile virus / pathogenicity*


  • Viral Envelope Proteins
  • glycoprotein E, Flavivirus

Associated data

  • GENBANK/AB185914
  • GENBANK/AB185915
  • GENBANK/AB185916
  • GENBANK/AB185917