title: Comparative analysis of the immunoprotective abilities of glycosylated and deglycosylated parainfluenza virus type 3 surface glycoproteins.
abstract: The role of carbohydrate moieties on the immunoprotective ability of parainfluenza virus type 3 (PIV-3) haemagglutinin-neuraminidase (HN) and fusion (F) glycoproteins was tested in hamsters. HN and F proteins were purified from detergent-solubilized virus by lentil-lectin affinity chromatography and deglycosylated by treatment with endoglycosidase F (endo F). Immunization of hamsters with either 1 or 5 micrograms of mock-treated (glycosylated) affinity-purified proteins elicited strong haemagglutination inhibition and neutralizing antibody responses 4 weeks after the primary injection. In contrast, titres were significantly lower with endo F-treated (deglycosylated) proteins. However, following the booster doses with at least 5 micrograms of antigen, glycosylated and deglycosylated proteins induced comparable antibody titres. There was no significant difference in the ability of the glycosylated or deglycosylated proteins to protect either the upper or lower respiratory tracts of immunized hamsters against PIV-3 challenge. These results suggest that the carbohydrate moieties of the HN and F proteins are not necessary for eliciting a protective response in hamsters.
authors.affiliation: Connaught Centre for Biotechnology Research, Willowdale, Ontario, Canada.
authors.forename: M
authors.initials: M
authors.lastname: Ewasyshyn
authors.forename: A M
authors.initials: AM
authors.lastname: Bonneau
authors.forename: S
authors.initials: S
authors.lastname: Usman
authors.forename: N
authors.initials: N
authors.lastname: Scollard
authors.forename: M
authors.initials: M
authors.lastname: Klein
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000914:Antibodies, Viral / Q000097:blood*; D006224:Cricetinae; D006023:Glycoproteins / Q000276:immunology*; D015707:HN Protein / Q000276:immunology* / Q000302:isolation & purification / Q000378:metabolism; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / Q000378:metabolism; D008969:Molecular Sequence Data; D018184:Paramyxoviridae Infections / Q000276:immunology* / Q000517:prevention & control*; D014760:Viral Fusion Proteins / Q000276:immunology* / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D000914:Antibodies, Viral; D006023:Glycoproteins; D015707:HN Protein; D014760:Viral Fusion Proteins; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase