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

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DOIResolve DOI: http://doi.org/10.1016/j.jim.2014.04.010
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TypeArticle
Journal titleJournal of Immunological Methods
ISSN1872-7905
Volume408
Pages2434; # of pages: 11
SubjectCD16a antigen; CD64 antigen; Fc receptor; glycan; immunoglobulin G; monoclonal antibody; unclassified drug; animal cell; antibody production; article; binding kinetics; biosensor; controlled study; gel permeation chromatography; glycosylation; human; human cell; in vitro study; mammal cell; matrix assisted laser desorption ionization time of flight mass spectrometry; nonhuman; priority journal; protein purification; quantitative assay; surface plasmon resonance; transient transfection; Mammalia
AbstractWe here report the production and purification of the extracellular domains of two Fcγ 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. © 2014 Elsevier B.V.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); Human Health Therapeutics (HHT-TSH)
Peer reviewedYes
NPARC number21272229
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Record identifier851280c3-aeab-4339-ab92-f0a545bc43bb
Record created2014-07-23
Record modified2016-05-09
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