AI Article Synopsis
- Immediate virus detection kits and vaccines are crucial in the event of a new viral disease outbreak, as seen with COVID-19.
- Researchers used a baculovirus-silkworm expression system to create a rapid production process for the SARS-CoV-2 spike protein (S protein), though challenges arose with the protein's solubility and production efficiency.
- Modifying the S protein's furin protease target site improved its secretion and purification, leading to valuable tools for developing immunodetection kits, immunization antigens, and vaccines.
Article Abstract
In the case of a new viral disease outbreak, an immediate development of virus detection kits and vaccines is required. For COVID-19, we established a rapid production procedure for SARS-CoV-2 spike protein (S protein) by using the baculovirus-silkworm expression system. The baculovirus vector-derived S proteins were successfully secreted to silkworm serum, whereas those formed insoluble structure in the larval fat body and the pupal cells. The ectodomain of S protein with the native sequence was cleaved by the host furin-protease, resulting in less recombinant protein production. The S protein modified in furin protease-target site was efficiently secreted to silkworm serum and was purified as oligomers, which showed immunoreactivity for anti-SARS-CoV-2 S2 antibody. By using the direct transfection of recombinant bacmid to silkworms, we achieved the efficient production of SARS-CoV-2 S protein as fetal bovine serum (FBS)-free system. The resultant purified S protein would be useful tools for the development of immunodetection kits, antigen for immunization for immunoglobulin production, and vaccines.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7280120 | PMC |
| http://dx.doi.org/10.1016/j.bbrc.2020.06.020 | DOI Listing |
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