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.
Vlahopoulos
Spiros
S
Immunology Center, St. Savas Cancer Hospital, Athens, Greece. sblachop@med.uoa.gr
Gritzapis
Angelo D
AD
Perez
Sonia A
SA
Cacoullos
Nike
N
Papamichail
Michail
M
Baxevanis
Constantine N
CN
D000911:Antibodies, Monoclonal / Q000276:immunology*; D061067:Antibodies, Monoclonal, Humanized; D003713:Dendritic Cells / Q000276:immunology; D006031:Glycosylation; D006801:Humans; D008358:Mannose / Q000378:metabolism*; D010843:Pichia / Q000378:metabolism*; D011485:Protein Binding; D018719:Erb-b2 Receptor Tyrosine Kinases / Q000276:immunology* / Q000378:metabolism; D011994:Recombinant Proteins / Q000276:immunology* / Q000378:metabolism; D000068878:Trastuzumab
D000911:Antibodies, Monoclonal; D061067:Antibodies, Monoclonal, Humanized; D008358:Mannose; D018719:Erb-b2 Receptor Tyrosine Kinases; D011994:Recombinant Proteins; D000068878:Trastuzumab