title: Glycosylation and antigenic variation among Kunjin virus isolates.
abstract: Previous studies have found Kunjin (KUN) virus isolates from within Australia to be genetically homogenous and that the envelope protein of the type strain (MRM61C) was unglycosylated and lacked a potential glycosylation site. We investigated the extent of antigenic variation between KUN virus isolates from Australia and Sarawak using an immunoperoxidase assay and a panel of six monoclonal antibodies. The glycosylation status of the E protein of each virus was also determined by N glycosidase F (PNGase F) digestion and limited sequence analysis. The results showed that KUN viruses isolated within Australia oscillated between three antigenic types defined by two epitopes whose expression was influenced by passage history and host cell type. In contrast an isolate from Sarawak formed a stable antigenic type that was not influenced by passage history and was distinct from all Australian isolates. PNGase F digestions of KUN isolates indicated that 19 of the 33 viruses possessed a glycosylated E protein. Nucleotide sequence of the 5' third of the E gene of selected KUN isolates revealed that a single base change in PNGase F sensitive strains changed the tripeptide N-Y-F (amino acids 154-156 of the published sequence) to the potential glycosylation site N-Y-S. Further analysis revealed that passage history also had a significant influence on glycosylation.
authors.affiliation: Department of Microbiology, University of Western Australia, QEII Medical Centre, Nedlands.
authors.forename: S C
authors.initials: SC
authors.lastname: Adams
authors.forename: A K
authors.initials: AK
authors.lastname: Broom
authors.forename: L M
authors.initials: LM
authors.lastname: Sammels
authors.forename: A C
authors.initials: AC
authors.lastname: Hartnett
authors.forename: M J
authors.initials: MJ
authors.lastname: Howard
authors.forename: R J
authors.initials: RJ
authors.lastname: Coelen
authors.forename: J S
authors.initials: JS
authors.lastname: Mackenzie
authors.forename: R A
authors.initials: RA
authors.lastname: Hall
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D000833:Animals, Suckling; D000911:Antibodies, Monoclonal / Q000276:immunology; D000940:Antigenic Variation; D001666:Binding Sites, Antibody; D001921:Brain / Q000821:virology; D002522:Chlorocebus aethiops; D018349:Encephalitis Viruses, Japanese / Q000276:immunology*; D000939:Epitopes / Q000276:immunology; D006031:Glycosylation; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000276:immunology / Q000378:metabolism
chemical_list: D000911:Antibodies, Monoclonal; D000939:Epitopes; D014759:Viral Envelope Proteins; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase