Drug – bio-affecting and body treating compositions – Lymphokine
Patent
1984-11-08
1987-11-24
Phillips, Delbert R.
Drug, bio-affecting and body treating compositions
Lymphokine
530329, 435 7, A61K 3900, C07K 706, G01N 5300
Patent
active
047088710
DESCRIPTION:
BRIEF SUMMARY
This invention relates to the identification and chemical synthesis of peptides (or amino acid sequences) which constitute the immunogenic determinant(s) of an immunologically important coat protein, VP1, of foot-and-mouth disease virus, and to the use of these peptides for example, in the production of vaccines and diagnostic reagents.
In the search for more effective means of protection against infective disease in man and animals, major advances have been made in the last decade. It is now clear that immunization is possible using an isolated component of the whole causative agent, such as for example in the influenza virus sub-unit vaccines.
Current efforts are directed at reducing the scale of the immunizing component still further, first to the polypeptide (protein) carrying the necessary trigger for the immune system and secondly to the trigger itself. Recombinant DNA technology has provided the means, by translation from the determined nucleotide sequences, of obtaining reliable amino acid sequences for biologically important proteins including such proteins which were not readily available from natural sources. However, methods for identifying the loci of a protein which constitute the trigger(s) or immunogenic determinant(s) are few and very time consuming and form the bottle neck to further rapid progress
The determination of the immunogenic determinant(s) for biologically important proteins, particularly proteins derived from the causative agents of infective disease in man and animals, is regarded as being of particular importance since, once these determinants have been identified, they can be simply and economically synthesised so as to provide the desired peptide sequences for use in vaccines which will have a high degree of specificity, and which will avoid any undesired effects from unnecessary amino acid or peptide sequences which might still be present in, for example, sub-unit type vaccines.
The immunogenicity of a polypeptide can be defined as the immune response directed against a limited number of immunogenic determinants, which are confined to a few loci on the polypeptide molecule, (see Crumpton, M. J., in The Antigens (ed. Sela, M., Academic Press, New York, 1974); Benjamini, E. et al., Curr. Topics Microbiol. Immunol. 58 85-135 (1972); and Atassi, M. Z., Immunochemistry 12, 423-438 (1975).) Antisera prepared against chemically synthesized peptides corresponding to short linear stretches of the polypeptide sequence have been shown to react well with the whole polypeptide, (see Green, N. et al., Cell 28, 477-487 (1982); Bittle, J. L. et al., Nature 298, 30-33 (1982); Dreesman et al., Nature 295, 158-160 (1982); Prince, A. M., Ikram, H., Hopp, T. P., Proc. Nat. Acad. Sci. USA 79, 579-582 (1982); Lerner, R. A. et al., Proc. Nat. Acad. Sci. USA 78, 3403-3407 (1981); and Neurath, A. R., Kent, S. B. H., Strick, N., Proc.Nat.Acad.Sci. USA 79, 7871-7875 (1982).) However, interactions have been found to occur even when the site of interaction does not correlate with the immunogenic determinants of the native protein, (see Green, N., et al, Supra). Conversely, since antibodies produced against the native protein are by definition directed to the immunogenic determinants, it follows that a peptide interacting with these antibodies must contain at least a part of an immunogenic determinant.
From a study of the few proteins for which the immunogenic determinants have been accurately mapped, it is clear that a determinant can consist of a single sequence, (continuous), or of several sequences (discontinuous) brought together from linearly distant regions of the polypeptide chain by the folding of that chain as it exists in the native state, (see Atassi, M. Z., Immunochemistry 15, 909-936 (1978).). As in the case of lysozyme several of the elements consist of only one amino acid, the size of a contributing element can then vary between one and the maximum number of amino acids consistent with the dimensions of the antibody combining site, and is likely to be of the order of five to six, (see At
REFERENCES:
patent: 4544500 (1985-10-01), Bittle et al.
patent: 4554101 (1985-11-01), Hopp
patent: 4605512 (1986-08-01), Schaller et al.
Commonwealth Serum Laboratories Commission
Phillips Delbert R.
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