Fusion Protein of Rotavirus VP6 and SARS-CoV-2 Receptor Binding Domain Induces T Cell Responses
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...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-07-01
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| Series: | Vaccines |
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| Online Access: | https://www.mdpi.com/2076-393X/9/7/733 |
| _version_ | 1797526014457282560 |
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| author | Kirsi Tamminen Suvi Heinimäki Stina Gröhn Vesna Blazevic |
| author_facet | Kirsi Tamminen Suvi Heinimäki Stina Gröhn Vesna Blazevic |
| author_sort | Kirsi Tamminen |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T09:21:12Z |
| format | Article |
| id | doaj.art-e3b59fa5129f4ca69725b475c5ac25dd |
| institution | Directory Open Access Journal |
| issn | 2076-393X |
| language | English |
| last_indexed | 2024-03-10T09:21:12Z |
| publishDate | 2021-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Vaccines |
| spelling | doaj.art-e3b59fa5129f4ca69725b475c5ac25dd2023-11-22T05:12:12ZengMDPI AGVaccines2076-393X2021-07-019773310.3390/vaccines9070733Fusion Protein of Rotavirus VP6 and SARS-CoV-2 Receptor Binding Domain Induces T Cell ResponsesKirsi Tamminen0Suvi Heinimäki1Stina Gröhn2Vesna Blazevic3Vaccine Development and Immunology/Vaccine Research Center, Faculty of Medicine and Health Technology, Tampere University, Arvo Ylpön katu 34, FI-33520 Tampere, FinlandVaccine Development and Immunology/Vaccine Research Center, Faculty of Medicine and Health Technology, Tampere University, Arvo Ylpön katu 34, FI-33520 Tampere, FinlandVaccine Development and Immunology/Vaccine Research Center, Faculty of Medicine and Health Technology, Tampere University, Arvo Ylpön katu 34, FI-33520 Tampere, FinlandVaccine Development and Immunology/Vaccine Research Center, Faculty of Medicine and Health Technology, Tampere University, Arvo Ylpön katu 34, FI-33520 Tampere, FinlandVaccines 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.https://www.mdpi.com/2076-393X/9/7/733SARS-CoV-2COVID-19delivery platformvaccinesVP6T cells |
| spellingShingle | Kirsi Tamminen Suvi Heinimäki Stina Gröhn Vesna Blazevic Fusion Protein of Rotavirus VP6 and SARS-CoV-2 Receptor Binding Domain Induces T Cell Responses Vaccines SARS-CoV-2 COVID-19 delivery platform vaccines VP6 T cells |
| title | Fusion Protein of Rotavirus VP6 and SARS-CoV-2 Receptor Binding Domain Induces T Cell Responses |
| title_full | Fusion Protein of Rotavirus VP6 and SARS-CoV-2 Receptor Binding Domain Induces T Cell Responses |
| title_fullStr | Fusion Protein of Rotavirus VP6 and SARS-CoV-2 Receptor Binding Domain Induces T Cell Responses |
| title_full_unstemmed | Fusion Protein of Rotavirus VP6 and SARS-CoV-2 Receptor Binding Domain Induces T Cell Responses |
| title_short | Fusion Protein of Rotavirus VP6 and SARS-CoV-2 Receptor Binding Domain Induces T Cell Responses |
| title_sort | fusion protein of rotavirus vp6 and sars cov 2 receptor binding domain induces t cell responses |
| topic | SARS-CoV-2 COVID-19 delivery platform vaccines VP6 T cells |
| url | https://www.mdpi.com/2076-393X/9/7/733 |
| work_keys_str_mv | AT kirsitamminen fusionproteinofrotavirusvp6andsarscov2receptorbindingdomaininducestcellresponses AT suviheinimaki fusionproteinofrotavirusvp6andsarscov2receptorbindingdomaininducestcellresponses AT stinagrohn fusionproteinofrotavirusvp6andsarscov2receptorbindingdomaininducestcellresponses AT vesnablazevic fusionproteinofrotavirusvp6andsarscov2receptorbindingdomaininducestcellresponses |