Towards the development of a surface plasmon resonance assay to evaluate the glycosylation pattern of monoclonal antibodies using the extracellular domains of CD16a and CD64

被引:23
作者
Dorion-Thibaudeau, July [1 ,2 ]
Raymond, Celine [2 ,3 ]
Lattova, Erika [4 ]
Perreault, Helene [4 ]
Durocher, Yves [2 ,3 ]
De Crescenzo, Gregory [1 ]
机构
[1] Ecole Polytech Montreal, Groupe Rech Sci & Technol Biomed, Dept Chem Engn, Bio P2 Res Unit, Montreal, PQ, Canada
[2] Natl Res Council Canada, NRC Human Hlth Therapeut Portfolio, Life Sci, Montreal, PQ H4P 2R2, Canada
[3] Univ Montreal, Dept Biochem, Montreal, PQ, Canada
[4] Univ Manitoba, Dept Chem, Winnipeg, MB R3T 2N2, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
CD16a; CD64; Monoclonal antibody; Glycosylation; Surface plasmon resonance (SPR); Anti-histidine capture; Aggregation; FC-GAMMA RECEPTORS; HUMAN IGG-FC; CRYSTAL-STRUCTURE; BINDING; AFFINITY; FUCOSE; RECOGNITION; CELLS; RIII; THERAPEUTICS;
D O I
10.1016/j.jim.2014.04.010
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
We here report the production and purification of the extracellular domains of two Fc gamma receptors, namely CD16a and CD64, by transient transfection in mammalian cells. The use of these two receptor ectodomains for the development of quantitative assays aiming at controlling the quality of monoclonal antibody production lots is then discussed. More specifically, the development of surface plasmon resonance-based biosensor assays for the evaluation of the glycosylation pattern and the aggregation state of monoclonal antibodies is presented. Our biosensor approach allows discriminating between antibodies harboring different galactosylation profiles as well as to detect low levels (i.e., less than 2%) of monoclonal antibody aggregates. (C) 2014 Elsevier B.V. All rights reserved.
引用
收藏
页码:24 / 34
页数:11
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