| Autor: |
Francis, M. J., Fry, C. M., Rowlands, D. J., Bittle, J. L., Houghten, R. A., Lerner, R. A., Brown, F. |
| Předmět: |
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| Zdroj: |
Immunology; May87, Vol. 61 Issue 1, p1-6, 6p |
| Abstrakt: |
Uncoupled synthetic peptide representing the sequence of amino acids 141–160 of foot-and-mouth disease virus (FMDV) protein VP1 induced a virus-neutralizing antibody response in guinea-pigs. This response required incomplete Freund's adjuvant (IFA) for the primary inoculation and was dependent on the presence of an added cysteine residue with an unblocked sulphydryl group at the carboxy-terminus. Secondary immunization could be carried out in the absence of adjuvant. A study of the relative activities of nested sets of uncoupled peptides from 150–160 to 135–160 and 141–160 to 141–155 indicated that amino acids 146–156 were critical for the induction of virus-neutralizing antibodies and that extension to 137–160 further improved this response. Results of in vitro proliferation studies demonstrated that the carboxy-terminal residues on this peptide may form a T- cell epitope. The significance of these observations in the broader context of synthetic peptide vaccines is discussed. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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