The glycosylation site in the envelope protein of West Nile virus (Sarafend) plays an important role in replication and maturation processes

J Gen Virol. 2006 Mar;87(Pt 3):613-622. doi: 10.1099/vir.0.81320-0.

Abstract

The complete genome of West Nile (Sarafend) virus [WN(S)V] was sequenced. Phylogenetic trees utilizing the complete genomic sequence, capsid gene, envelope gene and NS5 gene/3' untranslated region of WN(S)V classified WN(S)V as a lineage II virus. A full-length infectious clone of WN(S)V with a point mutation in the glycosylation site of the envelope protein (pWNS-S154A) was constructed. Both growth kinetics and the mode of maturation were affected by this mutation. The titre of the pWNS-S154A virus was lower than the wild-type virus. This defect was corrected by the expression of wild-type envelope protein in trans. The pWNS-S154A virus matured intracellularly instead of at the plasma membrane as shown for the parental WN(S)V.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Chlorocebus aethiops
  • Genome, Viral*
  • Glycosylation
  • Molecular Sequence Data
  • Sequence Alignment
  • Species Specificity
  • Vero Cells
  • Viral Envelope Proteins / classification
  • Viral Envelope Proteins / genetics
  • Viral Envelope Proteins / metabolism
  • Viral Envelope Proteins / physiology*
  • Virus Replication
  • West Nile virus / chemistry
  • West Nile virus / physiology*

Substances

  • Viral Envelope Proteins

Associated data

  • GENBANK/AY688948