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ARS Home » Northeast Area » Beltsville, Maryland (BARC) » Beltsville Agricultural Research Center » Animal Parasitic Diseases Laboratory » Research » Publications at this Location » Publication #302860
Title: Effectiveness of a novel immunogenic nanoparticle platform for Toxoplasma peptide vaccine in HLA transgenic mice

Author
item BISSATI, K - University Of Chicago
item DASGUPTA, D - Walter Reed Army Institute
item COBB, D - George Washington University
item Dubey, Jitender
item BURKHARD, P - University Of Connecticut
item LANAR, D - Walter Reed Army Institute
item MCLEOD, RIMA - University Of Chicago

Submitted to: Vaccine
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 4/18/2014
Publication Date: 4/12/2014
Citation: El Bissati, K., Zhou, Y., Dasgupta, D., Cobb, D., Dubey, J.P., Burkhard, P., Lanar, D., Mcleod, R. 2014. Effectiveness of a novel immunogenic nanoparticle platform for Toxoplasma peptide vaccine in HLA transgenic mice. Vaccine. 32:3243-3248.

Interpretive Summary: Toxoplasmosis is a major public health and food safety issue. The disease is caused by a single celled parasite, Toxoplasma gondii that causes mental retardation in humans and abortion in livestock. At present there is no effective vaccine against this disease, and there are no medicines to cure it. In the present study authors report a new method to vaccinate mice against this parasite. The results will be helpful in developing a vaccine against this parasite and would be of interest to biologists and parasitologists.

Technical Abstract: We created and produced a novel self-assembling nanoparticle platform for delivery of peptide epitopes that induce CD8+ and CD4+T cells that are protective against T. gondii infection. These self-assembling polypeptide nanoparticles (SAPNs) are composed of linear peptide (LP) monomers which contain two coiled-coil oligomerization domains, the dense granule 7 (GRA7 20-28 LPQFATAAT) peptide and a universal CD4+ T cell epitope (derived from PADRE). Purified LPs assemble into nanoparticles with icosahedral symmetry, similar to the capsids of small viruses. These particles were evaluated for their efficacy in eliciting interferon gamma by splenocytes of HLA-B*0702 transgenic mice and for their ability to protect against subsequent T. gondii challenge. This work demonstrates the feasibility of using this platform approached with a CD8+ epitope that binds HLA-B7 and tests the biological activity of potentially protective peptides restricted by human major histocompatibility complex (HLA) class I molecules in HLA transgenic mice.