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At least two Fc Neu5Gc residues of monoclonal antibodies are required for binding to anti-Neu5Gc antibody

Abstract:
Two non-human glycan epitopes, galactose-Į-1,3-galactose (Į-gal) and Neu5Gc-Į-2-6-galactose (Neu5Gc) have been shown to be antigenic when attached to Fab oligosaccharides of monoclonal antibodies (mAbs) , while Į-gal attached to Fc glycans were not. However, the antigenicity of Neu5Gc on the Fc glycans remains unclear in the context that most mAbs carry only Fc glycans. After studying two clinical mAbs carrying significant amounts of Fc Neu5Gc, we show that their binding activity with anti-Neu5Gc antibody resided in a small subset of mAbs carrying two or more Fc Neu5Gc, while mAbs harboring only one Neu5Gc showed no reactivity. Since most Neu5Gc epitopes were distributed singly on the Fc of mAbs, our results suggest that the potential antigenicity of Fc Neu5Gc is low. Our study could be referenced in the process design and optimization of mAb production in murine myeloma cells and in the quality control of mAbs for industries and regulatory authorities.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/srep20029

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Publisher:
Nature Publishing Group
Journal:
Scientific Reports More from this journal
Volume:
6
Article number:
20029
Publication date:
2016-01-29
Acceptance date:
2015-12-14
DOI:
ISSN:
2045-2322


Pubs id:
pubs:579985
UUID:
uuid:65885792-2405-4e01-94ea-413712e27dc3
Local pid:
pubs:579985
Source identifiers:
579985
Deposit date:
2015-12-14
ARK identifier:

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