Cloning and Expression of Influenza H1N1 NS1 Protein in Escherichia Coli BL21

The influenza virus is globally pathogenic and it is usually associated with zoonotic respiratory diseases. This virus has caused a number of pandemics with high mortality rates. The non-structural protein-1 (NS1) of influenza A viruses is a non-essential virulence factor that has multiple accessory functions during a viral infection. This protein is highly conservative. It has been shown that this protein plays a major role against the immunity responses of host cells. The aim of this study was to produce the recombinant influenza NS1 protein by the use of a bacterial production system, in order to evaluate the immunological and structural features of this protein in future researches. The NS1 gene construct was artificially synthesized; subsequently it was sub-cloned into the pQE30 expression vector. The expression vector was then transformed into the BL21 cells and induced by IPTG. Finally, the expression was evaluated by SDS-PAGE and Western blotting techniques. The NS1 gene was successfully cloned and transformed into expression cells. As a result, a 23 kDa band was observed both on the SDS-PAGE and nitrocellulose paper after Western blotting. Based on the results of this study, it could be concluded that the NS1 gene of influenza A H1N1 virus (A/Shiraz/14/2010 strain) could be cloned and the rNS1 protein (recombinant NS1 protein) could be expressed using a bacterial protein translation system. Since this protein is a conservative protein among influenza A viruses, it could be used as a potent vaccine for the prevention of various types of pandemics caused by influenza A.