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

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

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  • 1Immunology Center, St. Savas Cancer Hospital, Athens, Greece. sblachop@med.uoa.gr

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.

PMID:
19520203
[PubMed - indexed for MEDLINE]
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