Synthetic peptide-targeted selection of phage display mimotopes highlights immunogenic features of 伪-helical vs non-helical epitopes of Taenia solium paramyosin: Implications for parasite- and host-protective roles of the protein

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• 作者：Karlen G. Gazarian^a ; ^{karlen@servidor.unam.mx} ; Carlos F. Solis^b ; Tatiana G. Gazarian^a ; ^c ; Merrill Rowley^d ; Juan P. Laclette^b
• 关键词：Phage display ; Peptide ; Mimotopes ; Paramyosin ; Taenia solium ; Secondary structure prediction
• 刊名：Peptides
• 出版年：2012
• 期刊代码：59_01969781
• 类别：neu
• 出版时间：March, 2012
• 卷：34
• 期：1
• 页码：232-241
• 文件大小：1290 K

摘要

Paramyosin of the pig-human parasite Taenia solium (TPmy) is a 伪-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 伪-helical or linear structure to induce rabbit antibody responses for phage-display mapping of epitope core amino-acid sets. Antibodies to 伪-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 伪-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 伪-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.