Enhanced-Transient Expression of Hepatitis C Virus Core Protein in Nicotiana tabacum, a Protein With Potential Clinical Applications

Mohammadzadeh, Sara; Khabiri, Alireza; Roohvand, Farzin; Memarnejadian, Arash; Salmanian, Ali Hatef; Ajdary, Soheila; Ehsani, Parastoo

Finally, the results of ELISA in our study ( Figure 5 ) demonstrated that the transient expression of pHCVcp in tobacco leaves could provide the proper protein for diagnostic purposes and indicated its full functionality to react with poly/monoclonal anticore antibodies and HCV infected human sera compared to that of eHCVcp (14) . In addition, the proper conformation of pHCVcp to interact with specific monoclonal antibody against 21-40 amino acids of the core antigen (coated at the bottom of the ELISA plates) and the polyclonal anticore antibodies (at the top of the pHCVcp in ELISA), supported the presence of various interactive epitopes on pHCVcp. The monoclonal antibody used in this study was against amino acids 21-40 on HCV core antigen. This region carries two important immunological epitopes which are conserved between HCV strains: 1a, 1b, and 2 (57): Moreover, the amino acids of 23-44 are highly promiscuous CD4+ T cell epitopes and the 35-44 amino acids are HCVspecific HLA-A2-restricted CTL epitopes. They have been shown to be effective immunogens in the vaccine phase of two clinical trials while are present on the HCV core particle or in multi-epitope complexes (58) . Therefore, the primary results have proposed that the plant-produced pHCVcp might have the promising structure to be used as a vaccine candidate too. However, these primary results should be confirmed through animal and immunization studies.