Design and synthesis of a self-assembling peptide derived from the envelope proteins of HIV type 1. An approach to heterovalent immunogens

Tripathy, S. P. ; Kumar, A. ; Manivel, V. ; Panda, S. K. ; Rao, K. V. (1992) Design and synthesis of a self-assembling peptide derived from the envelope proteins of HIV type 1. An approach to heterovalent immunogens The Journal of Immunology, 148 (12). pp. 4012-4020. ISSN 0022-1767

Full text not available from this repository.

Official URL: http://www.jimmunol.org/content/148/12/4012.short

Abstract

A chimeric peptide that included sequences from gp120 and gp41 of HIV type 1 was synthesized. Cleavage from solid support yielded a composite of self-oligomerized products with molecular masses ranging from 5 to about 9 kDa. The oligomer but not its reduced, monomeric form was recognized by human anti-HIV sera and at least one of the two lysines in the sequence was involved in antibody binding. The oligomeric peptide was immunogenic, yielding a conformation-specific antibody response. Co-oligomerization of a hepatitis B surface Ag-derived peptide and the HIV type 1-derived peptide yielded a bivalent product in which conformational integrity of the individual components was maintained. Immunization with this hybrid peptide resulted in conformation-specific antibodies to both epitopes in all four murine strains tested. Lymphocyte proliferation assays revealed that the T epitopes resident in both peptide sequences remained active in the hybrid peptide. These results demonstrate the potential of this approach in generating multi- and heterovalent immunogens which may eventually find application as vaccines.

Item Type:Article
Source:Copyright of this article belongs to American Association of Immunologists.
ID Code:41349
Deposited On:28 May 2011 08:03
Last Modified:28 May 2011 08:03

Repository Staff Only: item control page