Eukaryotic expression and purification of SARS coronavirus protein S1

Objective: To clone protein S1 encoding DNA of SARS coronavirus (SARS CoV) and construct the expression vector pGEX 5T/S1 to express GST S1 fusion protein.Methods: The S1 fragment was amplified by PCR and was cloned into TMD 18T vector.After verified by sequencing,the recombinant was transformed into the prokaryotic expression vector pGEX 5T.The recombinant vector was transformed into E.coli K802 and the expressed fusion protein was detected by antibody positive serum. Results: The fusion protein was expressed in soluble form; the purified protein was detected by ELISA, complying with the control method. Conclusion: Expression and purification of prokaryotic GST S1 fusion protein provide a foundation to obtain a large quantity of recombinant S1 for experimental and clinical study of SARS CoV.