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Assembly of recombinant rotavirus proteins into virus-like particles and assessment of vaccine potential.
- Source :
-
Vaccine [Vaccine] 1993; Vol. 11 (2), pp. 273-81. - Publication Year :
- 1993
-
Abstract
- Rotavirus structural proteins VP4, VP6 and VP7 from Bovine Rotavirus Strain C486 were cloned and expressed in a baculovirus expression system. Combinations of the proteins were assembled into a series of virus-like particles, and a murine model was used to determine the capacity of the recombinant proteins and particles to induce protective immunity. All of the proteins induced humoral immunity as measured by an ELISA against whole virus. However, only the antisera from animals immunized with VP4 neutralized virus and inhibited haemagglutination. Challenge of neonates born to animals immunized with VP4 protein on assembled particles or in cell lysates showed protection against challenge with both homologous (bovine C486) and heterologous (SA-11) strains of rotavirus. In contrast, the offspring of mice immunized with VP6 were only partially protected. Neonates of animals immunized with virus-like particles composed of VP7 assembled on VP6 spherical particles were protected against challenge with the homotypic virus and significantly protected from a heterotypic challenge whereas unassembled VP7 protein provided only partial protection against challenge.
- Subjects :
- Animals
Animals, Newborn immunology
Antibodies, Viral biosynthesis
Antibodies, Viral immunology
Antibody Specificity
Capsid ultrastructure
Cattle microbiology
Female
Mice
Pregnancy
Vaccines, Attenuated immunology
Antigens, Viral
Baculoviridae
Capsid immunology
Capsid Proteins
Hemagglutinins, Viral immunology
Recombinant Fusion Proteins immunology
Rotavirus immunology
Rotavirus Infections prevention & control
Vaccines, Synthetic immunology
Viral Vaccines immunology
Subjects
Details
- Language :
- English
- ISSN :
- 0264-410X
- Volume :
- 11
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Vaccine
- Publication Type :
- Academic Journal
- Accession number :
- 8382422
- Full Text :
- https://doi.org/10.1016/0264-410x(93)90029-w