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The glycosylation site in the envelope protein of West Nile virus (Sarafend) plays an important role in replication and maturation processes.
Li, J; Bhuvanakantham, R; Howe, J; Ng, M-L.
Affiliation
  • Li J; Flavivirology Laboratory, Department of Microbiology, 5 Science Drive 2, National University of Singapore, Singapore 117597.
  • Bhuvanakantham R; Flavivirology Laboratory, Department of Microbiology, 5 Science Drive 2, National University of Singapore, Singapore 117597.
  • Howe J; Flavivirology Laboratory, Department of Microbiology, 5 Science Drive 2, National University of Singapore, Singapore 117597.
  • Ng ML; Flavivirology Laboratory, Department of Microbiology, 5 Science Drive 2, National University of Singapore, Singapore 117597.
J Gen Virol ; 87(Pt 3): 613-622, 2006 Mar.
Article in En | MEDLINE | ID: mdl-16476982
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: West Nile virus / Viral Envelope Proteins / Genome, Viral Limits: Animals Language: En Journal: J Gen Virol Year: 2006 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: West Nile virus / Viral Envelope Proteins / Genome, Viral Limits: Animals Language: En Journal: J Gen Virol Year: 2006 Document type: Article