Glycosylation of the West Nile Virus Envelope Protein Increases In Vivo and In Vitro Viral Multiplication in Birds

• Published in: The American journal of tropical medicine and hygiene Vol. 82; no. 4; pp. 696 - 704
• Main Authors: Murata, Ryo, Eshita, Yuki, Maeda, Akihiko, Maeda, Junko, Akita, Saki, Tanaka, Tomohisa, Yoshii, Kentaro, Kariwa, Hiroaki, Umemura, Takashi, Takashima, Ikuo
• Format: Journal Article
• Language: English
• Published: Deerfield, IL ASTMH 01.04.2010; American Society of Tropical Medecine and Hygiene; The American Society of Tropical Medicine and Hygiene
• Subjects: Animals; Biological and medical sciences; Cell Line; Chickens; Cricetinae; Culex; Female; Genes, Viral; Glycosylation; Infectious diseases; Male; Medical sciences; Muscle Cells - pathology; Muscle Cells - virology; Mutation; Poultry Diseases - virology; Viral Envelope Proteins - genetics; Viral Envelope Proteins - metabolism; Viremia; Virus Replication - physiology; West Nile Fever - pathology; West Nile Fever - veterinary; West Nile Fever - virology; West Nile virus - pathogenicity; West Nile virus - physiology; Virus; In vivo; Vertebrata; West Nile virus; Tropical medicine; Glycosylation; Japanese encephalitis group virus; Flaviviridae; Aves; Flavivirus; In vitro; Protein
• ISSN: 0002-9637; 1476-1645
• DOI: 10.4269/ajtmh.2010.09-0262

Many West Nile (WN) virus isolates associated with significant outbreaks possess a glycosylation site on the envelope (E) protein. E-protein glycosylated variants of New York (NY) strains of WN virus are more neuroinvasive in mice than the non-glycosylated variants. To determine how E protein glycosylation affects the interactions between WN virus and avian hosts, we inoculated young chicks with NY strains of WN virus containing either glycosylated or non-glycosylated variants of the E protein. The glycosylated variants were more virulent and had higher viremic levels than the non-glycosylated variants. The glycosylation status of the variant did not affect viral multiplication and dissemination in mosquitoes in vivo. Glycosylated variants showed more heat-stable propagation than non-glycosylated variants in mammalian (BHK) and avian (QT6) cells but not in mosquito (C6/36) cells. Thus, E-protein glycosylation may be a requirement for efficient transmission of WN virus from avian hosts to mosquito vectors.