About GlycoMAb

It is based on Roche Schlieren's pioneering demonstration that antibody glycosylation can be engineered in a fashion which dramatically and specifically increases antibody-dependent cellular cytotoxicity (ADCC). This immune effector mechanism is crucial for the in vivo target-cell killing activity of antibodies.

GlycoMAb® works by genetically engineering the antibody-producing cells with a gene encoding an oligosaccharide-modifying enzyme. The modified cells produce new molecular variants of the antibody, bearing bisected non-fucosylated oligosaccharides. These special oligosaccharides are not made by the standard production cell lines.

Antibodies produced using GlycoMAb® are highly enriched in bisected non-fucosylated glycosylation variants. The modified antibodies bind with higher affinity to the human FcgRIIIa receptor on immune effector cells. Increased binding affinity for this receptor translates into more efficient killing of the antibody-targeted cells by the immune effectors, a mechanism called antibody-dependent cellular cytotoxicity, or ADCC.

  • Expanding the therapeutic window of a given antibody and providing treatment for patients which do not respond to current treatment options

  • Reducing product attrition and avoiding costly failures, especially in late-stage clinical trials

  • Enabling life cycle management by producing second generation versions of innovator’s own product

  • Generating economically more attractive products (i.e., lower use of manufacturing capacity, reduced investment costs for manufacturing, reduced doses and frequency of injection, higher patient benefit and convenience)

  • Providing a unique competitive advantage for unconjugated antibodies in a highly competitive market

ADCC potency increases of over 100-fold can be typically achieved with GlycoMAb® with the lowest being about 10-fold and the highest 10,000-fold, depending on the antibody and target cell. In the standard ADCC potency assay, target cells, antibody and freshly isolated immune effector cells are incubated together. After a few hours, the fraction of antibody-dependent target cell killing is determined.

In the production of the clinical grade material, application of GlycoMAb did not change antibody productivity or cell growth. Very stable glycoengineered cell lines were generated and the production process remained unchanged.

It is based on Roche Glycart AG's pioneering demonstration that antibody glycosylation can be engineered in a fashion which dramatically and specifically increases antibody-dependent cellular cytotoxicity (ADCC). This immune effector mechanism is crucial for the in vivo target-cell killing activity of antibodies.

  • GlycoMAb® does not affect specific antibody productivity or cell growth (in suspension in serum- and protein-free cell culture medium).

  • By genetically modifying the antibody-producing cell line with efficient and robust vectors, high increases in potency are obtained while maintaining a simple and standard production process. No new steps, reagents, equipments, personnel, costs or risks are added to the antibody production process.

  • GlycoMAb® conserves the bivalent target-binding nature of antibodies and does not use toxic, immunogenic or radioactive moieties that can lead to higher side effects, elevated production costs or complex logistics from production to administration to patients.

  • GlycoMAb® can be applied to any industrial antibody-production cell line.

  • GlycoMAb® can be applied to chimeric, humanized and fully human antibodies.

  • GlycoMAb® is protected by one issued patent (US 6,602,684) and a number of pending patent applications from three patent families.

GlycoMAb technology is specifically designed for increasing the potency of therapeutic antibodies. For products blocked at any stage of development due to poor efficacy, GlycoMAb may be able to return them back into development.

Yes, GlycoMAb operates in the constant region of therapeutic antibodies and is therefore applicable to chimeric, humanized or fully human antibodies, independent of their variable regions.

Yes, we have successfully implemented our GlycoMAb in a wide variety of standard antibody producing cell lines commonly used in the biotechnology and pharmaceutical industries. We are regularly able to generate stable clones that maintain their specific antibody productivity and growth rate.

GlycoMAb leads to robust and highly stable production cell lines. GlycoMAb offers the flexibility to choose the pathway for its implementation; i.e. to apply GlycoMAb to an antibody producing cell line or to incorporate the antibody genes in an “empty” GlycoMAb cell line. It is rapidly implemented via standard procedures widely used in industry. It does not affect the specific antibody productivity or the growth rate of the parent cell line. GlycoMAb is a natural and cost efficient technology that does not use toxic, immunogenic, or radioactive moieties that can lead to complex logistics from production to administration to patients. Implementation of GlycoMAb does not add new unit operations to the production process.

Recent scientific work for some target-cell killing antibodies shows a correlation between objective patient response rates and increased binding affinity of the constant region of the antibody to CD16 (Fc-receptor expressed in immune effector cells). Such binding is largely increased with GlycoMAb.

GlycoMAb can deliver the maximal increase in binding affinity to FcgRIIIa that can be achieved by Fc de-fucosylation. The efficient and robust method to achieve high levels of non-fucosylated complex oligosaccharides in antibodies produced in any cell line was taught in US patent 6,602,684 (priority date April 1998).


Roche Glycart AG
Wagistrasse 10
CH- 8952 Schlieren

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