Glycoproteins of Human Parainfluenza Virus Type 3: Characterization and Evaluation as a Subunit Vaccine

Abstract

The envelope glycoproteins of human parainfluenza type 3 virus were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and reactivity with specific monoclonal antibodies. The molecular weight of the hemagglutinin-neuraminidase (HN) glycoprotein was found to be 72,000, and the fusion (F) glycoprotein appeared to consist of 74,000 (F0) or 56,000 (F1) species. Envelope glycoproteins were solubilized with octyl-glucoside and, after removal of the detergent by dialysis, were used for immunization of hamsters. Other animals were immunized with a formalin-inactivated preparation of whole virus. A single subcutaneous immunization with these antigen preparations induced a serum antibody response to the HN and F glycoproteins, as determined by plaque neutralization, hemagglutination inhibition, inhibition of virus-induced cell fusion, and immune precipitation tests. An IgG antibody response to both glycoproteins was also observed in bronchial washings. Animals immunized with the highest dose of envelope glycoproteins showed complete protection from challenge infection, whereas immunization with inactivated virus did not completely protect animals.

Antigenic variation of human and bovine parainfluenza virus type 3 strains

“…A field trial of inactivated human PIV3 vaccine has been done but it did not induce resistance to infection (Chin et al, 1969). Several studies have shown that animals may be protected with whole virus and subunit vaccines containing both human and bovine PIV3 components (Morein et al, 1983;Ray et al, 1985). The two surface glycoproteins HN and F are important for the establishment of protection against disease (Morein et al, 1983;Spriggs et al, 1987).…”

Glycoproteins of Human Parainfluenza Virus Type 3: Affinity Purification, Antigenic Characterization and Reconstitution into Lipid Vesicles

“…Antibodies to these glycoproteins are expected to prevent initiation and spread of the infection process. In an earlier study, the mixed envelope glycoproteins were evaluated as a subunit vaccine and found to confer protection against challenge infection in hamsters (Ray et al, 1985). Purification of measles virus glycoproteins and the fusion protein of mumps virus has been reported using immunoaffinity chromatography with monoclonal antibodies (Bellini et al, 1981 ;Varsanyi el al., 1984Varsanyi el al., , 1985Server et al, 1985).…”

“…The importance of antibodies to parainfluenza virus HN and F glycoproteins for prevention of infection has been documented previously (Merz et al, 1980;Choppin & Scheid, 1980). The virion polypeptides of PI3 virus have been identified in several laboratories (Guskey & Bergtrom, 1981 ;Goswami & Russell, 1983;Storey et al, 1984;Sanchez & Banerjee, 1985;Jambou et al, 1985;Ray et al, 1985). Purified envelope glycoproteins of PI3 virus have been shown to be effective in eliciting an antibody response and confer protection from challenge infection in hamsters (Ray et al, 1985).…”

“…The virion polypeptides of PI3 virus have been identified in several laboratories (Guskey & Bergtrom, 1981 ;Goswami & Russell, 1983;Storey et al, 1984;Sanchez & Banerjee, 1985;Jambou et al, 1985;Ray et al, 1985). Purified envelope glycoproteins of PI3 virus have been shown to be effective in eliciting an antibody response and confer protection from challenge infection in hamsters (Ray et al, 1985). On the other hand, immunization with formalin-inactivated whole virus induced an antibody response to the envelope glycoproteins, but provided only partial protection from challenge infection.…”

“…SDS-PAGE, immunoprecipitation (IP), haemagglutination (HA), haemagglutination inhibition (HI), fusion inhibition (FI) of virus-infected BHK cells, plaque neutralization (NT), immunofluorescence (IF) and protein estimations were carried out following the procedures described previously (Ray et al, 1985). Cleveland peptide mapping was performed using Staphylococcus aureus V8 protease (Cleveland et al, 1977).…”