West Nile virus envelope protein glycosylation is required for efficient viral transmission by Culex vectors

Robin M. Moudy, Bo Zhang, Pei Yong Shi, Laura D. Kramer

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


Many, but not all, strains of West Nile virus (WNV) contain a single N-linked glycosylation site on their envelope (E) proteins. Previous studies have shown that E-glycosylated strains are more neuroinvasive in mice than non-glycosylated strains. E protein glycosylation also appears to play a role in attachment and entry of WNV into host cells in vitro; however, studies examining how E protein glycosylation affects the interactions of WNV with its mosquito vectors in vivo have not yet been performed. We mutated the E protein glycosylation site from NYS to IYS in a previously described full-length clone of the NY99 genotype of WNV (WT), resulting in a virus that lacked the glycan at aa154. WNV-N154I replicated less efficiently than WNV-WT in Culex mosquito tissues, although the extent of the decrease was greater in Cx. pipiens than in Cx. tarsalis. Following peroral infection, mosquitoes infected with WNV-N154I were less likely to transmit virus than those infected with WNV-WT. Interestingly, all but one of the mosquitoes infected with WNV-N154I transmitted a revertant virus, suggesting that there is strong selective pressure toward E protein glycosylation. Together these data suggest that loss of the glycan at aa154 on the WNV E protein can severely restrict viral spread in the mosquito vector.

Original languageEnglish (US)
Pages (from-to)222-228
Number of pages7
Issue number1
StatePublished - Apr 25 2009
Externally publishedYes


  • Glycosylation
  • Virus-vector interactions
  • West Nile virus

ASJC Scopus subject areas

  • Virology


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