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Chemoenzymatic synthesis of glycoengineered IgG antibodies and glycosite-specific antibody–drug conjugates
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Chemoenzymatic synthesis of glycoengineered IgG antibodies and glycosite-specific antibody–drug conjugates
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Journal Article
Chemoenzymatic synthesis of glycoengineered IgG antibodies and glycosite-specific antibody–drug conjugates
2017
Overview
Glycoengineering of IgG antibodies and glycosite-specific antibody–drug conjugates is an important tool for enhancing their therapeutic efficacy. Tang
et al
. describe a protocol for efficient and homogeneous chemoenzymatic antibody glycoengineering.
Glycoengineered therapeutic antibodies and glycosite-specific antibody–drug conjugates (gsADCs) have generated great interest among researchers because of their therapeutic potential. Endoglycosidase-catalyzed
in vitro
glycoengineering technology is a powerful tool for IgG Fc (fragment cystallizable)
N
-glycosylation remodeling. In this protocol, native heterogeneously glycosylated IgG
N
-glycans are first deglycosylated with a wild-type endoglycosidase. Next, a homogeneous
N
-glycan substrate, presynthesized as described here, is attached to the remaining
N
-acetylglucosamine (GlcNAc) of IgG, using a mutant endoglycosidase (also called endoglycosynthase) that lacks hydrolytic activity but possesses transglycosylation activity for glycoengineering. Compared with
in vivo
glycoengineering technologies and the glycosyltransferase-enabled
in vitro
engineering method, the current approach is robust and features quantitative yield, homogeneous glycoforms of produced antibodies and ADCs, compatibility with diverse natural and non-natural glycan structures, convenient exploitation of native IgG as the starting material, and a well-defined conjugation site for antibody modifications. Potential applications of this method cover a broad scope of antibody-related research, including the development of novel glycoengineered therapeutic antibodies with enhanced efficacy, site-specific antibody–drug conjugation, and site-specific modification of antibodies for fluorescent labeling, PEGylation, protein cross-linking, immunoliposome formation, and so on, without loss of antigen-binding affinity. It takes 5–8 d to prepare the natural or modified
N
-glycan substrates, 3–4 d to engineer the IgG
N
-glycosylation, and 2–5 d to synthesize the small-molecule toxins and prepare the gsADCs.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82/16
/ 82/58
/ Antigens
/ Biological Products - chemical synthesis
/ Biological Products - metabolism
/ Computational Biology/Bioinformatics
/ Glycan
/ Glycoconjugates - chemical synthesis
/ Glycoconjugates - metabolism
/ Immunoglobulin G - metabolism
/ Immunologic Factors - chemical synthesis
/ Immunologic Factors - metabolism
/ protocol
/ Toxins
