Fusion protein of rotavirus VP6 and SARS-CoV-2 receptor binding domain induces T cell responses
Tamminen, Kirsi; Heinimäki, Suvi; Gröhn, Stina; Blazevic, Vesna (2021-07)
Tamminen, Kirsi
Heinimäki, Suvi
Gröhn, Stina
Blazevic, Vesna
07 / 2021
733
Julkaisun pysyvä osoite on
https://urn.fi/URN:NBN:fi:tuni-202108116509
https://urn.fi/URN:NBN:fi:tuni-202108116509
Kuvaus
Peer reviewed
Tiivistelmä
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.
Kokoelmat
- TUNICRIS-julkaisut [19225]