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• W2029188514 endingPage "4708" @default.
• W2029188514 startingPage "4704" @default.
• W2029188514 abstract "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." @default.
• W2029188514 created "2016-06-24" @default.
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• W2029188514 date "2009-07-01" @default.
• W2029188514 modified "2023-09-27" @default.
• W2029188514 title "Mannose addition by yeast Pichia Pastoris on recombinant HER-2 protein inhibits recognition by the monoclonal antibody herceptin" @default.
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• W2029188514 doi "https://doi.org/10.1016/j.vaccine.2009.05.063" @default.
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