title: Loss of glycosylation at Asn144 alters the substrate preference of the N8 influenza A virus neuraminidase.
abstract: Role of asparagine-linked (N-linked) oligosaccharide side chains in the maturation and the function of influenza virus neuraminidase (NA) subtype N8 was examined by site-directed mutagenesis and vaccinia virus expression system. Mutations in the consensus sequence for N-linked glycosylation at Asn 84 or 398 prevent the proper maturation of mutant NAs. On the contrary, mutation at Asn 144, that is conserved in all except two strains of influenza virus NA ever sequenced, did not affect the proper maturation and the transport of the mutant NA to the cell surface. Furthermore, this mutation led the alternation of substrate preference of this enzyme. These observations indicate that N-glycosylation at Asn 144 of N8 NA may be conserved from the functional requirement, but not from the structural necessity.
authors.affiliation: Department of Animal Science, Faculty of Agriculture, Kobe University, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Saito
authors.forename: K
authors.initials: K
authors.lastname: Kawano
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001216:Asparagine / Q000032:analysis* / Q000378:metabolism; D001483:Base Sequence; D002469:Cell Separation / Q000379:methods / Q000662:veterinary; D017931:DNA Primers / Q000032:analysis / Q000737:chemistry / Q000235:genetics; D004279:DNA, Viral / Q000032:analysis / Q000737:chemistry / Q000235:genetics; D004285:Dogs; D006031:Glycosylation; D006801:Humans; D009980:Influenza A virus / Q000201:enzymology* / Q000235:genetics; D007668:Kidney / Q000166:cytology / Q000821:virology; D016297:Mutagenesis, Site-Directed; D009439:Neuraminidase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015531:Radioimmunoprecipitation Assay / Q000379:methods / Q000662:veterinary; D013379:Substrate Specificity
chemical_list: D017931:DNA Primers; D004279:DNA, Viral; D001216:Asparagine; D009439:Neuraminidase