Background: To obtain thermal stable, soluble, biologically active hepatitis E virus recombinant antigen using thioredoxin fusion expression system.
Methods: HEV ORF2 gene fragment (6964-7126 nt) was inserted into thioredoxin fusion expression vector pThioHisA. The recombinant plasmid was transformed into E. coli BL21 strain. After induction with IPTG, cells were lysed and the supernatant was subjected to 80 degree treatment for 10 minutes. After centrifugation, the supernatant was tested by ELISA.
Results: SDS-PAGE analysis showed the thioredoxin. HEV fusion protein was highly expressed and was thermally stable, soluble. HEV specific ELISA confirmed this fusion protein possessing HEV specific antigenicity.
Conclusions: Using thioredoxin fusion expression system, a soluble, thermal stable, biologically active HEV recombinant antigen was successfully expressed.