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

Vaccine. 2009 Jul 23;27(34):4704-8. doi: 10.1016/j.vaccine.2009.05.063. Epub 2009 Jun 9.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal / immunology*
  • Antibodies, Monoclonal, Humanized
  • Dendritic Cells / immunology
  • Glycosylation
  • Humans
  • Mannose / metabolism*
  • Pichia / metabolism*
  • Protein Binding
  • Receptor, ErbB-2 / immunology*
  • Receptor, ErbB-2 / metabolism
  • Recombinant Proteins / immunology*
  • Recombinant Proteins / metabolism
  • Trastuzumab


  • Antibodies, Monoclonal
  • Antibodies, Monoclonal, Humanized
  • Recombinant Proteins
  • Receptor, ErbB-2
  • Trastuzumab
  • Mannose