ArticleBioMed research international2013
Analysis of structures and epitopes of surface antigen glycoproteins expressed in bradyzoites of Toxoplasma gondii.
Article in BioMed research international, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Prediction of Proto-Oncogene Using Bidirectional GRU and Attention.Asian Pacific journal of cancer prevention : APJCP · 2025Article
- Descriptive Comparison of ELISAs for the Detection ofPathogens (Basel, Switzerland) · 2021Review
- Screening and identification of host proteins interacting with Toxoplasma gondii SAG2 by yeast two-hybrid assay.Parasites & vectors · 2017Article
- Comparative efficacy of a multi-epitope DNA vaccine via intranasal, peroral, and intramuscular delivery against lethal Toxoplasma gondii infection in mice.Parasites & vectors · 2014Article
- Protein sequence classification with improved extreme learning machine algorithms.BioMed research international · 2014Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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