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Biochemical characterization of artificially designed long peptide fusion protein HR1-VV-HR2-VS. (A) AlphaFold2 prediction of HR1-VV-HR2-VS protein suggested a homo-trimer form. The spike protein structure was shown with key regions highlighted: VV (S 976-1008 aa, red), VS (S 1129-1170 aa, cyan), HR1 (S 910-974 aa, blue), and HR2 (S 1168-1203 aa, purple). A schematic representation of the designed protein domains was provided below the structure. A flexible SGGRGG linker was introduced between the domains. (B) Purification and analysis of HR1-HR2 and HR1-VV-HR2-VS fusion proteins expressed in <t>HEK293F</t> cells. The purified proteins were characterized by size-exclusion chromatography and SDS-PAGE. HR1-VV-HR2-VS and HR1-HR2 proteins were indicated in blue and purple, respectively. (C) The HR1-VV-HR2-VS and HR1-HR2 recombinant proteins were crosslinked using disuccinimidyl suberate, and were further analysed via SDS-PAGE. (D) Circular dichroism spectroscopy analysis of the HR1-VV-HR2-VS protein. Scans recorded at 20°C (red), 50°C (blue), and 95°C (purple) are shown.
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Biochemical characterization of artificially designed long peptide fusion protein HR1-VV-HR2-VS. (A) AlphaFold2 prediction of HR1-VV-HR2-VS protein suggested a homo-trimer form. The spike protein structure was shown with key regions highlighted: VV (S 976-1008 aa, red), VS (S 1129-1170 aa, cyan), HR1 (S 910-974 aa, blue), and HR2 (S 1168-1203 aa, purple). A schematic representation of the designed protein domains was provided below the structure. A flexible SGGRGG linker was introduced between the domains. (B) Purification and analysis of HR1-HR2 and HR1-VV-HR2-VS fusion proteins expressed in <t>HEK293F</t> cells. The purified proteins were characterized by size-exclusion chromatography and SDS-PAGE. HR1-VV-HR2-VS and HR1-HR2 proteins were indicated in blue and purple, respectively. (C) The HR1-VV-HR2-VS and HR1-HR2 recombinant proteins were crosslinked using disuccinimidyl suberate, and were further analysed via SDS-PAGE. (D) Circular dichroism spectroscopy analysis of the HR1-VV-HR2-VS protein. Scans recorded at 20°C (red), 50°C (blue), and 95°C (purple) are shown.
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Biochemical characterization of artificially designed long peptide fusion protein HR1-VV-HR2-VS. (A) AlphaFold2 prediction of HR1-VV-HR2-VS protein suggested a homo-trimer form. The spike protein structure was shown with key regions highlighted: VV (S 976-1008 aa, red), VS (S 1129-1170 aa, cyan), HR1 (S 910-974 aa, blue), and HR2 (S 1168-1203 aa, purple). A schematic representation of the designed protein domains was provided below the structure. A flexible SGGRGG linker was introduced between the domains. (B) Purification and analysis of HR1-HR2 and HR1-VV-HR2-VS fusion proteins expressed in HEK293F cells. The purified proteins were characterized by size-exclusion chromatography and SDS-PAGE. HR1-VV-HR2-VS and HR1-HR2 proteins were indicated in blue and purple, respectively. (C) The HR1-VV-HR2-VS and HR1-HR2 recombinant proteins were crosslinked using disuccinimidyl suberate, and were further analysed via SDS-PAGE. (D) Circular dichroism spectroscopy analysis of the HR1-VV-HR2-VS protein. Scans recorded at 20°C (red), 50°C (blue), and 95°C (purple) are shown.

Journal: Emerging Microbes & Infections

Article Title: Receptor binding domain-independent pancoronavirus vaccine design by fusion of conserved T/B Epitopes

doi: 10.1080/22221751.2026.2631206

Figure Lengend Snippet: Biochemical characterization of artificially designed long peptide fusion protein HR1-VV-HR2-VS. (A) AlphaFold2 prediction of HR1-VV-HR2-VS protein suggested a homo-trimer form. The spike protein structure was shown with key regions highlighted: VV (S 976-1008 aa, red), VS (S 1129-1170 aa, cyan), HR1 (S 910-974 aa, blue), and HR2 (S 1168-1203 aa, purple). A schematic representation of the designed protein domains was provided below the structure. A flexible SGGRGG linker was introduced between the domains. (B) Purification and analysis of HR1-HR2 and HR1-VV-HR2-VS fusion proteins expressed in HEK293F cells. The purified proteins were characterized by size-exclusion chromatography and SDS-PAGE. HR1-VV-HR2-VS and HR1-HR2 proteins were indicated in blue and purple, respectively. (C) The HR1-VV-HR2-VS and HR1-HR2 recombinant proteins were crosslinked using disuccinimidyl suberate, and were further analysed via SDS-PAGE. (D) Circular dichroism spectroscopy analysis of the HR1-VV-HR2-VS protein. Scans recorded at 20°C (red), 50°C (blue), and 95°C (purple) are shown.

Article Snippet: The medium for the HEK293F cell line was purchased from Sino Biological (M293CD1).

Techniques: Purification, Size-exclusion Chromatography, SDS Page, Recombinant, Circular Dichroism, Spectroscopy