中国生物工程杂志

HIV-1 envelope glycoprotein gp41, which is a hopeful target for HIV-1 fusion inhibitors, plays a critical role in the fusion of viral and cellular membranes. In order to build up the screening assay of HIV-1 fusion inhibitors targeting gp41, HIV-1 gp41 5-helix and 6-helix were expressed in prokaryotic cells. Gp41 5-helix and 6-helix recombined plasmids were constructed by using PCR, enzyme digestion and ligation taking the clade B HIV-1 genome as a template. The plasmid was transferred into E. coli BL21（DE3）and then induced by IPTG. The expressed protein was purified by affinity chromatography after denaturation and renaturation. The SDS-PAGE analysis was used during expression and purification. Native-PAGE was used to identify the interaction between gp41 5-helix and T-20. It will be helpful to build up the screening assay of HIV-1 fusion inhibitors targeting gp41.