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Immunological properties of hepatitis B core antigen fusion proteins.

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  • 1. Department of Virology, Wellcome Biotechnology Ltd., Beckenham, Kent, United Kingdom.
      Authors
    • Francis MJ 1
    (1 author)

Proceedings of the National Academy of Sciences of the United States of America, 01 Apr 1990, 87(7):2545-2549
https://doi.org/10.1073/pnas.87.7.2545 PMID: 2320575 PMCID: PMC53726

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Abstract 

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.

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Proc Natl Acad Sci U S A. 1990 Apr; 87(7): 2545–2549.
PMCID: PMC53726
PMID: 2320575

Immunological properties of hepatitis B core antigen fusion proteins.

M J Francis, G Z Hastings, A L Brown, K G Grace, D J Rowlands, F Brown, and B E Clarke
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Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
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