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BioMed Research International
Volume 2013, Article ID 165342, 9 pages
http://dx.doi.org/10.1155/2013/165342
Research Article

Analysis of Structures and Epitopes of Surface Antigen Glycoproteins Expressed in Bradyzoites of Toxoplasma gondii

1Department of Human Parasitology, School of Medicine, Shandong University, No. 44 Wenhuaxi Road, Jinan, Shandong 250012, China
2Laboratory of Morphology, School of Medicine, Shandong University, No. 44 Wenhuaxi Road, Jinan, Shandong 250012, China
3Cancer Research Center, School of Medicine, Shandong University, No. 44 Wenhuaxi Road, Jinan, Shandong 250012, China
4Department of College English, Shandong University, No. 44 Wenhuaxi Road, Jinan, Shandong 250012, China
5School Hospital of Shandong University, No. 73 Jingshi Road, Jinan, Shandong 250012, China

Received 14 November 2012; Accepted 18 February 2013

Academic Editor: María Sol Arias Vázquez

Copyright © 2013 Hua Cong et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Toxoplasma gondii is a protozoan parasite capable of infecting humans and animals. Surface antigen glycoproteins, SAG2C, -2D, -2X, and -2Y, are expressed on the surface of bradyzoites. These antigens have been shown to protect bradyzoites against immune responses during chronic infections. We studied structures of SAG2C, -2D, -2X, and -2Y proteins using bioinformatics methods. The protein sequence alignment was performed by T-Coffee method. Secondary structural and functional domains were predicted using software PSIPRED v3.0 and SMART software, and 3D models of proteins were constructed and compared using the I-TASSER server, VMD, and SWISS-spdbv. Our results showed that SAG2C, -2D, -2X, and -2Y are highly homologous proteins. They share the same conserved peptides and HLA-I restricted epitopes. The similarity in structure and domains indicated putative common functions that might stimulate similar immune response in hosts. The conserved peptides and HLA-restricted epitopes could provide important insights on vaccine study and the diagnosis of this disease.