Immunological properties of hepatitis B core antigen fusion proteins.
The immunogenicity of a 19 amino acid peptide from foot-and-mouth disease virus has previously been shown to approach that of the inactivated virus from which it was derived after multimeric particulate presentation as an N-terminal fusion with hepatitis B core antigen. In this report we demonstrate that rhinovirus peptide-hepatitis B core antigen fusion proteins are 10-fold more immunogenic than peptide coupled to keyhole limpet hemocyanin and 100-fold more immunogenic than uncoupled peptide with an added helper T-cell epitope. The fusion proteins can be readily administered without adjuvant or with adjuvants acceptable for human and veterinary application and can elicit a response after nasal or oral dosing. The fusion proteins can also act as T-cell-independent antigens. These properties provide further support for their suitability as presentation systems for "foreign" epitopes in the development of vaccines.
Francis
M J
MJ
Department of Virology, Wellcome Biotechnology Ltd., Beckenham, Kent, United Kingdom.
Hastings
G Z
GZ
Brown
A L
AL
Grace
K G
KG
Rowlands
D J
DJ
Brown
F
F
Clarke
B E
BE
D000276:Adjuvants, Immunologic; D000818:Animals; D000917:Antibody Formation; D002678:Chimera; D004797:Enzyme-Linked Immunosorbent Assay; D005260:Female; D006168:Guinea Pigs; D006512:Hepatitis B Core Antigens / Q000032:analysis / Q000235:genetics / Q000276:immunology*; D051379:Mice; D008807:Mice, Inbred BALB C; D010455:Peptides / Q000138:chemical synthesis; D010957:Plasmids; D011993:Recombinant Fusion Proteins / Q000032:analysis / Q000276:immunology*; D015183:Restriction Mapping; D013601:T-Lymphocytes / Q000276:immunology
D000276:Adjuvants, Immunologic; D006512:Hepatitis B Core Antigens; D010455:Peptides; D011993:Recombinant Fusion Proteins