ArticleParasites & vectors2013
SAG2A protein from Toxoplasma gondii interacts with both innate and adaptive immune compartments of infected hosts.
Article in Parasites & vectors, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 30 citations in OpenAlex.
- Parasites and Infection: Strategies to Control, Diagnose, and Treat Parasitic Diseases.Microorganisms · 2025Article
- A Structural In Silico Analysis of Novel Epitopes fromInternational journal of molecular sciences · 2025Article
- Mouse innate resistance tomSphere · 2024Article
- Recombinant SAG2A Protein fromMicroorganisms · 2024Article
- Seroprevalence and Risk Factors for Toxoplasma gondii Infection in Women of Reproductive Age in Nigeria in 2018.The American journal of tropical medicine and hygiene · 2024Article
- AdvancingMicrobiology spectrum · 2024Article
- Host cell proteins modulated upon Toxoplasma infection identified using proteomic approaches: a molecular rationale.Parasitology research · 2022Review
- Immunoinformatic analysis of immunogenic B- and T-cell epitopes of MIC4 protein to designing a vaccine candidate againstClinical and experimental vaccine research · 2021Article
- Article
- 14-3-3 Protein ofFrontiers in microbiology · 2019Article
- Screening and identification of host proteins interacting with Toxoplasma gondii SAG2 by yeast two-hybrid assay.Parasites & vectors · 2017Article
- Cloning, expression and purification of a polytopic antigen comprising of surface antigens ofIranian journal of microbiology · 2017Article
- Importance of serological cross-reactivity among Toxoplasma gondii, Hammondia spp., Neospora spp., Sarcocystis spp. and Besnoitia besnoiti.Parasitology · 2017Review
- A new Toxoplasma gondii chimeric antigen containing fragments of SAG2, GRA1, and ROP1 proteins-impact of immunodominant sequences size on its diagnostic usefulness.Parasitology research · 2015Article
- Design and evaluation of a recombinant multi-epitope antigen for serodiagnosis of Toxoplasma gondii infection in humans.Parasites & vectors · 2015Article
- High expression of water-soluble recombinant antigenic domains of Toxoplasma gondii secretory organelles.The Korean journal of parasitology · 2014Article
- A comparative study of Toxoplasma gondii seroprevalence in three healthy Chinese populations detected using native and recombinant antigens.Parasites & vectors · 2013Article
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundToxoplasma gondii is an intracellular parasite that causes relevant clinical disease in humans and animals. Several studies have been performed in order to understand the interactions between proteins of the parasite and host cells. SAG2A is a 22 kDa protein that is mainly found in the surface of tachyzoites. In the present work, our aim was to correlate the predicted three-dimensional structure of this protein with the immune system of infected hosts.
methodsTo accomplish our goals, we performed in silico analysis of the amino acid sequence of SAG2A, correlating the predictions with in vitro stimulation of antigen presenting cells and serological assays.
resultsStructure modeling predicts that SAG2A protein possesses an unfolded C-terminal end, which varies its conformation within distinct strain types of T. gondii. This structure within the protein shelters a known B-cell immunodominant epitope, which presents low identity with its closest phyllogenetically related protein, an orthologue predicted in Neospora caninum. In agreement with the in silico observations, sera of known T. gondii infected mice and goats recognized recombinant SAG2A, whereas no serological cross-reactivity was observed with samples from N. caninum animals. Additionally, the C-terminal end of the protein was able to down-modulate pro-inflammatory responses of activated macrophages and dendritic cells.
conclusionsAltogether, we demonstrate herein that recombinant SAG2A protein from T. gondii is immunologically relevant in the host-parasite interface and may be targeted in therapeutic and diagnostic procedures designed against the infection.
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