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, J. E.; Calvert, A. E.; Mesesan, K.; Crabtree, M. B.; Volpe, K. E.; Silengo, S.; Kinney, R. M.; Huang, C. Y. H.; Miller, B. R.; Roehrig, J. 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 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.
Palavras-Chave: Virology; Growth; Replication; Mutations; Viruses; Proteins; Cell culture; Aquatic insects; Public health; Cell survival; Envelopes; Amino acids; Mammalian cells; Insect cells; Envelope protein; Glycosylation; Infection; Mutation; Aedes aegypti; Dengue virus type 2
Imprenta: Virology, v. 366, n. 2, p. 415-423, 2007.
Descritores: Aedes aegypti - Cell ; Aedes aegypti - Proteins ; Aedes aegypti - Infectious diseases ; Aedes aegypti - Virus ; Aedes aegypti - Dengue ; Aedes aegypti - Public health
Data de publicação: 2007
