CLONING, EXPRESSION AND BIOACTIVITY OF HEMAGGLUTININBINDING DOMAIN PROTEIN OF AVIAN INFLUENZA VIRUSIN THE YEAST PICHIA PASTORIS AND E. COLI
The hemagglutinin (HA) protein is a glycosylated integral membrane protein that forms a homotrimer on the surface of the avian influenza virus, and the antibody against hemagglutinin protein is the main antibody for protection in the host. HA1, one of two hemagglutinin structure subunits, bears the ligand binding domain of hemagglutinin which is generally a hairpin form with antigen activity. A hairpin form of HA1 named HA1 - 3 was chosen as a low molecular weight protein and was secreted in a recombinant form in the yeast Pichia pastoris and E. coli. A DNA fragment encoding HA1 - 3 protein was cloned and inserted into the P. pastoris expression plasmid pPIC9K and E. coli expression plasmid pET21b. HA1 - 3 protein was separately expressed in the yeast P. Pichia and E. coli BL21 (DE3). Recombinant proteins secreted from P. pastoris and E. coli had the same molecular weight of 29 kDa, but they were different in solubility and bioactivity. This continuous culturing process resulted in a feasible method in pharmaceutical production and should be applicable to the production of other recombinant proteins in P. pastoris.
Avian influenza virus (AIV) hemagglutinin (HA) pichia pastoris
Zhou Kai He Hongxuan Wang Xinwei Wang Fengyang Duan Mingxing
National Research Center for Wildlife Born Diseases, Key Laboratory of Animal Ecology and Conservati College of Life Science and Agriculture, Key Laboratory of Tropic Biological Resources of Ministryof State Key Laboratory of Biomembrane & Membrane Biotechnology, Department of Biological Sciences and
国际会议
The 6th International Forum on Post-genome Technologies(6IFPT)(第六届国际后基因组生命科学技术学术论坛)
北京
英文
219-223
2009-09-17（万方平台首次上网日期，不代表论文的发表时间）