Bio-functional enhancement of plant based-haemagglutinin by fusion with IgMFc

Abstract

The creation of recombinant oligomeric haemagglutinin proteins from A/H5N1 virus is a new concern for many scientists. In this study, the gene encoding the haemagglutinin protein (H5TG) derived from virus A/duck/Vietnam/TG24-01/2005 was fused with three different motifs (GCN4pII, GCN4pII-IgMFc and GCN4pII-ELP-IgMFc) in order to form three recombinant proteins (trimeric H5TGpII, oligomeric H5TGplI-IgMFc and ELPylated oligomeric H5TGplI-ELP-IgMFc, respectively) for enhancing protein expression, bio-function and purification of H5TG. These H5TG fragments have been attached to expression cassettes in the pCB301 shuttle vector, transiently expressed in Nicotiana benthamiana by agroinfiltration, then the protein expression was confirmed by SDS-PAGE and Western blot analysis.