Fusion protein of rotavirus VP6 and SARS-CoV-2 receptor binding domain induces T cell responses

Kirsi Tamminen, Suvi Heinimäki, Stina Gröhn, Vesna Blazevic

    Tutkimustuotos: ArtikkeliScientificvertaisarvioitu

    2 Lataukset (Pure)


    Vaccines based on mRNA and viral vectors are currently used in the frontline to combat the ongoing pandemic caused by the novel Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). However, there is still an urgent need for alternative vaccine technologies inducing/boosting long-lasting and cross-reactive immunity in different populations. As a possible vaccine candidate, we employed the rotavirus VP6-protein platform to construct a fusion protein (FP) displaying receptor-binding domain (RBD) of SARS-CoV-2 spike protein (S) at the N-terminus of VP6. The recombinant baculovirus-insect cell produced VP6-RBD FP was proven antigenic in vitro and bound to the human angiotensin-converting enzyme 2 (hACE2) receptor. The FP was used to immunize BALB/c mice, and humoral-and T cell-mediated immune responses were investigated. SARS-CoV-2 RBD-specific T cells were induced at a high quantity; however, no RBD or S-specific antibodies were detected. The results suggest that conformational B cell epitopes might be buried inside the VP6, while RBD-specific T cell epitopes are available for T cell recognition after the processing and presentation of FP by the antigen-presenting cells. Further immunogenicity studies are needed to confirm these findings and to assess whether, under different experimental conditions, the VP6 platform may present SARS-CoV-2 antigens to B cells as well.

    DOI - pysyväislinkit
    TilaJulkaistu - heinäk. 2021
    OKM-julkaisutyyppiA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä


    • Jufo-taso 1

    !!ASJC Scopus subject areas

    • Immunology
    • Pharmacology
    • Drug Discovery
    • Infectious Diseases
    • Pharmacology (medical)


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