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. 2023 May 4;59(37):5555-5558.
doi: 10.1039/d3cc00672g.

Study on antibody Fc-glycosylation for optimal effector functions

Vidya S Shivatare  1 , Po-Kai Chuang  1 , Tzu-Hao Tseng  1 , Yi-Fang Zeng  1 , Han-Wen Huang  1 , Gannedi Veeranjaneyulu  1 , Han-Chung Wu  2 , Chi-Huey Wong  1   3
Affiliations

Study on antibody Fc-glycosylation for optimal effector functions

Vidya S Shivatare et al. Chem Commun (Camb). .

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.

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Conflict of interest statement

Conflicts of interest

Authors declare no conflict of interest.

Figures

figure 1:
figure 1:
a general strategy for in-vitro glycan remodeling through the combined use of endoglycosidase and glycosynthase.
figure 2:
figure 2:
glycoengineered antibodies with homogeneous glycoforms of high mannose, hybrid, and complex types. homogeneous antibodies g8, g11, g17, g18, and g20–24 are prepared using chmc813-70, while all other glycoforms are reported using rituximab.
figure 3:
figure 3:
. adcc activity of selected glycoforms tested against pancreatic adenocarcinoma epithelial cell line (hpac).
See this image and copyright information in PMC

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