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
Autor(es): Bryant, Juliet E.; Calvert, Amanda E.; Mesesan, Kyeen; Crabtree, Mary B.; Volpe, Katharine E.; Silengo, Shawn; Kinney, Richard M.; Huang, Claire Y. -H.; Miller, Barry R.; Roehrig, John T.
Resumo: 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 El (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 El or El/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. Published by Elsevier Inc.
Palavras-Chave: E glycosylation; dengue virus; Flavivirus; mosquitoes
Imprenta: Virology, v. 366, n. 2, p. 415-423, 2007
Identificador do objeto digital: 10.1016/j.virol.2007.05.007
Descritores: Aedes aegypti - Cell ; Aedes aegypti - Flaviviridae ; Aedes aegypti - Proteins ; Aedes aegypti - RNA ; Aedes aegypti - Virus
Data de publicação: 2007
