A Method to Detect the Binding of Hyper-Glycosylated Fragment Crystallizable (Fc) Region of Human IgG1 to Glycan Receptors.

Blundell, Pat ORCID: https://orcid.org/0000-0003-3386-5660 and Pleass, Richard ORCID: https://orcid.org/0000-0001-7438-8296 (2018) 'A Method to Detect the Binding of Hyper-Glycosylated Fragment Crystallizable (Fc) Region of Human IgG1 to Glycan Receptors.'. Methods in Molecular Biology, Vol 1904, pp. 417-421.

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Abstract

Engineering the fragment crystallizable (Fc) of human IgG can bring improved effector functions to monoclonal antibodies and Fc-fusion-based medicines and vaccines. Such Fc-effector functions are largely controlled by posttranslational modifications (PTMs) within the Fc, including the addition of glycans that introduce structural and functional heterogeneity to this class of therapeutic. Here, we describe a detailed method to allow the detection of hyper-sialylated Fcs to glycan receptors that will facilitate the future development of new mAbs and Fc-fragment therapies and vaccines.

Item Type:	Article
Subjects:	QU Biochemistry > Proteins. Amino Acids. Peptides > QU 55 Proteins QW Microbiology and Immunology > Antigens and Antibodies. Toxins and Antitoxins > QW 575 Antibodies
Faculty: Department:	Biological Sciences > Department of Tropical Disease Biology
Digital Object Identifer (DOI):	https://doi.org/10.1007/978-1-4939-8958-4_20
Depositing User:	Stacy Murtagh
Date Deposited:	09 Jan 2019 12:24
Last Modified:	25 Jan 2022 10:49
URI:	https://archive.lstmed.ac.uk/id/eprint/9944

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