ArticleActa biochimica et biophysica Sinica2022
Identification of a dominant murine T-cell epitope in recombinant protein P29 from Echinococcus granulosus
Article in Acta biochimica et biophysica Sinica, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 7 citations in OpenAlex.
- Article
- Enhancing the therapeutic potential of P29 protein-targeted monoclonal antibodies in the management of alveolar echinococcosis through CDC-mediated mechanisms.PLoS pathogens · 2024Article
- A subunit vaccine based onActa biochimica et biophysica Sinica · 2024Article
- Immunoprotective effect and mechanism of rEg.P29 against CD4Acta biochimica et biophysica Sinica · 2024Article
- Optimizing sheep B-cell epitopes inFrontiers in immunology · 2024Article
- Immunogenicity of peptide-based vaccine composed of epitopes from Echinococcus granulosus rEg.P29.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023Article
- Recombinant antigen P29 ofFrontiers in immunology · 2023Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Echinococcus granulosus causes echinococcosis, an important zoonotic disease worldwide and a major public health issue. Vaccination is an economical and practical approach for controlling E. granulosus. We have previously revealed that a recombinant protein P29 (rEg.P29) is a good vaccine candidate against E. granulosus. However, T cell immunogenic epitopes have not been identified. In the present study, we use rEg.P29-immunized mice as models to screen immunogenic epitopes for the construction of a novel multi-epitope vaccine. We search for immunodominant epitopes from an overlapping peptide library to screen the peptides of rEg.P29. Our results confirm that rEg.P29 immunization in mice elicits the activation of T cells and induces cellular immune responses. Further analyses show that a T cell epitope within amino acids 86–100 of rEg.P29 elicits significant antigen-specific IFN-γ production in CD4+ and CD8+ T cells and promotes specific T-cell activation and proliferation. Collectively, these results provide a reference for the construction of a novel vaccine against broad E. granulosus genotypes based on epitopes of rEg.P29.
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