Mannose addition by yeast Pichia Pastoris on recombinant HER-2 protein inhibits recognition by the monoclonal antibody herceptin

We report here the generation of a full-length, highly glycosylated HER-2 oncoprotein using yeast strain, Pichia Pastoris. Upon treatment of secreted HER-2 with alpha-mannosidase, reactivity with the monoclonal antibody Herceptin is significantly increased. This phenomenon is due to glycosylation via mannose of the full-length HER-2 protein that extends over the antigenic epitope, which is recognized by Herceptin. The extensive glycosylation of HER-2 in Pichia Pastoris significantly increases its recognition and uptake by dendritic cells, which could be associated with increased vaccine performance.