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Glyco-Engineering Antibody

Glyco-Engineering AntibodyHuman IgGs have a single conserved N-glycosylation site at N297 in the CH2 domain of their constant region. This glycosylation occurs in multiple different forms, which results in an IgG being a "collection of closely related structures" often referred as microheterogeneity.

In support of our mission to enable cutting edge advances in the life sciences, we Creative Biolabs recently launched the following glyco-engineering therapeutic MAbs that describe the biological effects exerted by different glycan forms attached to N297 of an IgG Fc or Fab, and how engineering of those glycans (antibody glyco-engineering) can be used to obtain therapeutic MAb candidates with widely different biological properties:

Non-glycosylated IgGs for lowered effector function
Low- or non-fucosylated oligosaccharides result in higher ADCC
FAb glycosylation typically enhance the solubility of the antibody

Cat Product Name Molecular target Major indication Protein format
Gly-001CL Romiplostim TPO-R Thrombocytopenia Fc-peptide fusion (“peptibody”) produced in E. coli; non-glycosylated
Gly-002CL TRX4 CD3 Type 1 diabetes Non-glycosylated, humanized IgG1
Gly-003CL Obinutuzumab CD20 Front-line CLL and other cancers IgG1κ humanized; non-fucosylated form generated using Glycart technology
Gly-004CL Clazakizumab IL-6 Non-small cell lung cancer-related fatigue and cachexia Non-glycosylated, humanized IgG produced in yeast
Gly-005CL Blisibimod Blys RA Anti-BLys peptibody - produced in E. coli; non-glycosylated
Gly-006CL Benralizumab IL-5R SLE Non-fucosylated IgG1κ
Gly-007CL Mogamulizumab CCR4 Inflammation and oncology Humanized IgG1; non-fucosylated
Gly-008CL Anti-CD70 monoclonal antibody (MDX-1411) CD70 Inflammation and oncology Human IgG; non-fucosylated
Gly-009CL Anti-CD30 monoclonal antibody (MDX-1401) CD30 Inflammation and oncology Human IgG1; non-fucosylated
Gly-011CL Anti-CD19 fully human monoclonal antibody MDX-1342 CD19 CLL, RA Human IgG1; non-fucosylated
Gly-012CL Anti-IGF-1R human monoclonal antibody (BIIB022) IGF-1R Solid tumors Human IgG4; non-glycosylated
Gly-013CL Anti-ganglioside GM2 monoclonal antibody BIW-8962 GM2 Blood tumors IgG1; non-fucosylated
Gly-015CL Cetuximab EGFR Metastatic colorectal cancer, metastatic non-small cell lung cancer and head and neck cancer The only commercial antibody to possess V-region glycosylation, which contains an N-linked oligosaccharide occupying N88 of the VH chain

Other new launched Glyco-Engineering Antibodies are designed and classified as below:

Classify Biological properties
Deglycosylated antibody (Non-glycosylated IgGs) Lowered effector function
Reduced binding to Fcγ receptors and C1q
Retains some residual minor binding to FcγRI, resulting in in vitro cellbased Fc-mediated activities such as ADCP and induction of TNF-α release by PBMCs
Decreased thermostability
More susceptible to proteolysis than glycosylated IgGs
Manageable differences
Retain the FcRn interactions and long serum half-life
Lower stability caused by “superclosed” conformation and C’E loop modified on CH2
Fab glycosylation A significant role in antigen binding and thus host defense
A positive, neutral, or negative impact on the binding of certain antigens, and typically enhance the solubility of the antibody
Fc glycosylation The N-glycans attached to N297 of antibody Fc domains are usually very heterogeneous, which results in an IgG being a “collection of closely related structures” often referred as microheterogeneity. A significant feature is that they are buried between the two Fc chains and are not as accessible to various glycan-modifying enzymes as most protein glycans.
N-glycosides from N297 in the CH2 domain of a human IgG is typically bi-antennary, fucosylated G0, G1, and G2 (top), with minor non-fucosylated (middle) and sialylated (bottom).
Generation of mostly or completely non-fucosylated IgG, with or without bisecting N-acetyl-glucosamine (GlcNAc; middle), results in significantly higher FcγRIIIa binding and higher ADCC.
Generation of highly α-2,6-sialylated oligoglycans (bottom) results in immunosuppressive effects at high IgG concentrations.
Low- or non-fucosylated oligosaccharides Possessing terminal galactose residues
Bind FcγRIIIa with higher affinity (up to 50-fold), resulting in significantly higher ADCC
Greater neutrophilmediated phagocytosis
Physiologically significant modification that can confer significant advantages to the antibody in vivo
Sialylated IgG glycans Present in IVIG
Anti-inflammatory properties
Reduced affinity for both FcγRIIIa and to their immobilized cell-surface targets, resulting in decreased ADCC
Bind the B cell surface receptor CD22 and down-regulated the activation, proliferation, and function of B cells, thereby yielding an immunosuppressive effect
Non-hyper galactosylated Reduced anti-drug immune response
Hyper-galactosylated Enhanced CDC and ADCC
High-mannose glycoforms Lower C1q binding and lower activation of the complement system
Non-fucosylated high mannose oligosaccharides bind FcγRIIIa better and display higher ADCC
Shorter half-life

Dozens more Glyco-Engineering Antibody will soon be available. Should you need further information, please feel free to contact us at

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