All the obtained proteins demonstrated high level of immunogenicity after triplicate parenteral administration to mice. To enable purification on the heparin-containing sorbents, a short fragment from the heparin-binding hemagglutinin of Mycobacterium tuberculosis was inserted at the C-terminus of the hybrid proteins. For the purpose of multimerization, either aldolase from Thermotoga maritima, which forms a trimer in solution, or alpha-helical trimerizer of the Spike protein from SARS‑CoV‑2, was attached to the epitopes incorporated into the Rop-like protein. The conformation was additionally fixed by a disulfide bond formed between the cysteine residues present within the epitopes. Loop epitopes were inserted into the turn region. The homologue of Rop protein from the Escherichia coli ColE1 plasmid containing helix-turn-helix motif was used as an epitope scaffold for the convergence of C- and N-termini of the loop-like epitopes. To fix conformation of the selected epitopes, an approach using protein scaffolds was used. Two types of hybrid proteins, including one of the two selected epitopes, were constructed. Two loop-like epitopes with lengths of 22 and 42 amino acid residues were selected from the receptor-binding motif of the Spike protein from the SARS‑CoV‑2 virus that participate in a large number of protein-protein interactions in the complexes with ACE2 and neutralizing antibodies. A new platform for creating anti-coronavirus epitope vaccines has been developed.
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