Glycosylation of the dengue 2 virus E protein at N67 is critical for virus growth in vitro but not for growth in intrathoracically inoculated Aedes aegypti mosquitoes

Virology. 2007 Sep 30;366(2):415-23. doi: 10.1016/j.virol.2007.05.007. Epub 2007 Jun 1.

Abstract

To determine the importance of dengue 2 virus (DEN2V) envelope (E) protein glycosylation, virus mutants in one or both of the N-linked glycosylation motifs were prepared. We found that while the E2 mutant virus (N153Q) replicated in mammalian and mosquito cells, the E1 (N67Q) and E1/2 (N67Q and N153Q) mutant viruses were unable to grow in mammalian cells. Infection of C6/36 mosquito cells with either the E1 or E1/2 mutants resulted in the introduction of a compensatory mutation, K64N, restoring glycosylation in the area. All mutants replicated similarly in inoculated Aedes aegypti mosquitoes, with no change in their mutations. These results suggest that N-linked glycosylation of the E protein is not necessary for DEN2V replication in mosquitoes, however N-linked glycosylation at amino acid N67 (or nearby N64) is critical for the survival of the virus in either mammalian or insect cell culture.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aedes / virology*
  • Amino Acid Substitution / genetics
  • Animals
  • Cell Line
  • Dengue Virus / genetics
  • Dengue Virus / growth & development*
  • Glycosylation
  • Humans
  • Mutagenesis, Site-Directed
  • Viral Envelope Proteins / genetics
  • Viral Envelope Proteins / metabolism*

Substances

  • E-glycoprotein, Dengue virus type 2
  • Viral Envelope Proteins