Niederhauser, S.; Zahno, M.L.; Nenci, C.; Vogt, H.R.; Zanoni, R.; Peterhans, E.; Bertoni, G. (2009). A Gag peptide encompassing B- and T-cell epitopes of the caprine arthritis encephalitis virus functions as modular carrier peptide. Journal of immunological methods, 342(1-2), pp. 82-90. Amsterdam: Elsevier 10.1016/j.jim.2008.11.015
Full text not available from this repository. (Request a copy)Short synthetic peptides are important tools in biomedical research permitting to generate hapten specific polyclonal sera for analytical purposes or functional studies. In this paper we provide proof of principle that a peptide located in a highly conserved portion of the Gag protein of the caprine arthritis encephalitis virus and carrying an immunodominant T helper cell epitope functions as an efficient carrier peptide, mediating a strong antibody response to a peptidic hapten encompassing a well-characterized B cell epitope of Env. The carrier and hapten peptides were collinearly synthesized permutating their molecular arrangement. While the antibody response to the hapten was similar for both constructs, the antibody response to a B cell epitope overlapping the T helper cell epitope of the Gag carrier peptide was considerably different. This permits a modular use of the carrier peptide to generate antibody directed exclusively to the hapten peptide or a strong humoral response to both carrier- and hapten-peptide. Finally, we have mapped the epitopes involved in this polarized antibody response and discussed the potential immunological implications.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
05 Veterinary Medicine > Department of Infectious Diseases and Pathobiology (DIP) > Institute of Virology and Immunology |
UniBE Contributor: |
Vogt, Hans-Rudolf, Zanoni, Reto Giacomo, Peterhans, Ernst, Bertoni, Giuseppe |
ISSN: |
0022-1759 |
Publisher: |
Elsevier |
Language: |
English |
Submitter: |
Factscience Import |
Date Deposited: |
04 Oct 2013 15:25 |
Last Modified: |
05 Dec 2022 14:26 |
Publisher DOI: |
10.1016/j.jim.2008.11.015 |
Web of Science ID: |
000264685300010 |
URI: |
https://boris.unibe.ch/id/eprint/38311 (FactScience: 220994) |
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