PMC:7100515 / 6319-7885 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7100515","sourcedb":"PMC","sourceid":"7100515","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7100515","text":"Expression of SARS-CoV-2 S protein\nTo enhance expression of the S protein of SARS-CoV-2 in mammalian cells, a codon-optimized cDNA encoding the S protein and 3xFLAG tag was synthesized, and to facilitate incorporation of S protein into lentiviral pseudovirons, the last 19 amino acids containing an endoplasmic reticulum (ER)-retention signal from the cytoplasmic tail of the S protein was removed (Fig. 1a). The construct was named SARS-CoV-2 S. HEK293T cells were transfected with SARS-CoV-2 S plasmid and expression of SARS-CoV-2 S protein was determined by western blot. There were two major bands, 180 kDa, and 90 kDa, detected by mouse anti-FLAG M2 antibody (Fig. 1b, lane 2), reflecting the full-length and cleaved S proteins, respectively. The band above 250 kDa likely results from dimeric or trimeric S proteins. Consistent with our previous report29, MERS-CoV S protein was detected by polyclonal goat anti-MHV S antibodies AO4 (Fig. 1c). AO4 also detected SARS-CoV-2 and SARS-CoV S proteins, suggesting the presence of a conserved immunogenic epitope among all four different CoVs. This presumably linear epitope is likely in S229. S1 subunits of SARS-CoV-2 and SARS-CoV share almost 64% in amino acid identities. Nevertheless, SARS-CoV-2 S protein was barely detected by rabbit polyclonal anti-SARS S1 antibodies T62 (Fig. 1d), suggesting that the major epitope(s) for T62 antibodies include non-conserved regions of S1. The SARS-CoV-2 S protein was not detected by either a monoclonal anti-SARS S1 antibody (Fig. 1e) or anti-MERS S2 antibody 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