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Comparative analysis of the immunoprotective abilities of glycosylated and deglycosylated parainfluenza virus type 3 surface glycoproteins

¹ Connaught Centre for Biotechnology Research, 1755 Steeles Avenue West, Willowdale, Ontario, Canada M2R 3T4
and² Bio-Mega/Boehringer Ingelheim Research Inc., 2100 Cunard Street, Laval, Quebec, Canada H7S 2G5

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 lentillectin affinity chromatography and deglycosylated by treatment with endoglycosidase F (endo F). Immunization of hamsters with either 1 or 5 µg of mocktreated (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 µg 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.

Received 26 April 1993; accepted 21 July 1993.