Issue 37, 2023
From the journal:

Chemical Communications

Study on antibody Fc-glycosylation for optimal effector functions†

Vidya S. Shivatare,a   Po-Kai Chuang,a   Tzu-Hao Tseng,a   Yi-Fang Zeng,a   Han-Wen Huang,a   Gannedi Veeranjaneyulu, ORCID logo a   Han-Chung Wub  and  Chi-Huey Wong ORCID logo *ac  

* Corresponding authors

a Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA
E-mail: wong@scripps.edu

b Institute of Cellular and Organismic Biology, Academia Sinica, Taipei 11529, Taiwan

c Genomics Research Center, Academia Sinica, Taipei 115, Taiwan

Abstract

A comprehensive structure–activity relationship study on antibody Fc-glycosylation has been performed using the chimeric anti-SSEA4 antibody chMC813-70 as a model. The α-2,6 sialylated biantennary complex type glycan was identified as the optimal Fc-glycan with significant enhancement in antibody effector functions, including binding to different Fc receptors and ADCC.

Graphical abstract: Study on antibody Fc-glycosylation for optimal effector functions

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Article information

DOI
https://doi.org/10.1039/D3CC00672G
Article type
Communication
Submitted
14 Feb 2023
Accepted
11 Apr 2023
First published
18 Apr 2023

Chem. Commun., 2023,59, 5555-5558

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Study on antibody Fc-glycosylation for optimal effector functions

V. S. Shivatare, P. Chuang, T. Tseng, Y. Zeng, H. Huang, G. Veeranjaneyulu, H. Wu and C. Wong, Chem. Commun., 2023, 59, 5555 DOI: 10.1039/D3CC00672G

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