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

Pat Blundell; Richard Pleass

doi:10.1007/978-1-4939-8958-4_20

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

Pat Blundell
, Richard Pleass

Tropical Disease Biology

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

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.

Original language	English
Pages (from-to)	417-421
Number of pages	5
Journal	Methods in Molecular Biology
DOIs	https://doi.org/10.1007/978-1-4939-8958-4_20
Publication status	Published - 12 Dec 2018

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

ADCC
ADCP
CDC
Effector function
Fc-receptors
Glycans
Glycosylation
IgG
Therapeutic antibodies

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10.1007/978-1-4939-8958-4_20

Detect binding IgG1Accepted author manuscript, 224 KB

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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.",

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AB - 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.

KW - ADCC

KW - ADCP

KW - CDC

KW - Effector function

KW - Fc-receptors

KW - Glycans

KW - Glycosylation

KW - IgG

KW - Therapeutic antibodies

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JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

ER -

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

Abstract

UN SDGs

Keywords

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