Journal
PEPTIDES
Volume 34, Issue 1, Pages 232-241Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2011.10.003
Keywords
Phage display; Peptide; Mimotopes; Paramyosin; Taenia solium; Secondary structure prediction
Funding
- Consejo Nacional de Ciencia y Tecnologia, Mexico [25166IN, LOO42-M9607]
- Direccion General de Asuntos de Personal Academica - Universidad Nacional Autonoma de Mexico [IN24797, IN225798]
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Paramyosin of the pig-human parasite Taenia solium (TPmy) is a alpha-helical protein located on the worm surface that is suggested to fulfill an immunomodulatory role protecting the parasite against host immune system. Besides, in challenging experiments the protein shows a vaccine potential. These observations imply that TPmy harbors antigenic determinants for each of these contrasting actions. However the suggestion was not given a support from experimental data because respective epitopes have not been described thus far. To circumvent this difficulty, we use synthetic peptides with sequences of regions composed of alpha-helical or linear structure to induce rabbit antibody responses for phage-display mapping of epitope core amino-acid sets. Antibodies to alpha-helical regions were weak binders and M13 phage-displayed peptides selected by them from two different libraries exhibited no amino-acid similarities with the original protein site. In contrast, the antibodies produced in response to non-helical segment within alpha-helical structure were better binders and selectors of perfect structural mimics of the protein site. This first phage display epitope analysis of TPmy supports the notion that the rod-like alpha-helix, which encompasses over 90% of the total amino acids, may serve as an immunomodulatory shield that protects the parasite. Further, the seven non-helical segments of the TPmy molecule may represent the only anti-parasite discrete immunogenic epitopes whose representative mimotopes can be utilized in development of pure epitope vaccines. (C) 2011 Elsevier Inc. All rights reserved.
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