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You are here: Home / Archives for Antibody Engineering & Therapeutics

Engineering of human sialidase Neu2 as novel immunotherapy

January 29, 2023 by Janice Reichert

Post written by Czeslaw Radziejewski, Ph.D.

Antibody Engineering & Therapeutics, held in December 2022, offered many opportunities to hear exciting and informative presentations by experts in the field, including Li Peng, Ph.D., who discussed “Engineering of human Sialidase Neu2 as Novel Immunotherapy for Degrading Immunosuppressive Sialoglycans to Enhance Antitumor T-Cell Immunity”.

Glycans are the most abundant structures on the cell surface. They are involved in cell communication with immune cells, and abnormal glycans can cause immune dysfunction in cancer and inflammatory diseases. Glycans typically terminate in sialic acid, but in cancer cells, sialic acid is present at a much higher abundance. The most common sialic acid in humans is N-acetylneuraminic acid, which plays a crucial role in numerous intercellular interactions, including with immune cells in the extracellular matrix, epithelial cells, and antibodies. Many studies have shown that sialoglycans are immunosuppressive and that high levels of surface sialoglycans are linked with poor outcomes in many tumor types. Hypersialylation of the surface of cancer cells makes these cells prime ligands for sialic acid-binding immunoglobulin-type lectins (Siglecs), which are found on the surface of immune cells. Once bound to sialylated glycans, Siglecs promote immunosuppressive signaling, thus conferring protection on the tumor cell. There are 15 human Siglecs. In addition, CD-28 is also known to bind sialoglycans. Most immune cells express more than one Siglec.

In her plenary lecture at the 2022 Antibody Engineering & Therapeutics conference, Professor Carolyn Bertozzi, outlined opportunities for the development of cancer treatments based on understanding the cell-surface glycome. She favored degrading sialoglycans with the enzyme sialidase to eliminate the immunosuppression promoted by Siglecs. As proof of concept, a fusion protein was created in Bertozzi’s lab using click chemistry, linking bacterial sialidase to the C-terminus of trastuzumab. The conjugate was tested in a mouse model of a trastuzumab-resistant HER2+ breast cancer model, and the results showed that the treatment essentially abrogated tumor growth. Based on these promising findings, Bertozzi cofounded Palleon Pharmaceuticals to explore sialidase-based biotherapies for cancer treatment.

At the conference, Dr. Li Peng, Chief Scientific Officer of Palleon Pharmaceuticals, presented the company’s progress in moving this concept toward the clinic. Palleon created a set of proprietary Siglec-based reagents for immunohistological hypersialylation detection and probing its role in immunotherapy resistance. Using such reagents, Palleon examined tissues from metastatic melanoma patients treated with PD1 blockade and showed that patients with a high level of sialylation fared much worse than patients with lower levels of sialoglycans. Following Bertozzi’s line of reasoning, the company pursued a strategy of using the enzymatic functionality of sialidase to remove excessive cell-surface sialylation. To translate this idea into a human therapeutic, Palleon decided to use a genetic fusion of sialidase with human Fc.

[Read more…]

Filed Under: Antibody Engineering & Therapeutics Tagged With: antibody engineering, antibody therapeutics

Therapeutic Opportunities in Glycoscience: Bioorthogonal chemistry in translation

December 29, 2022 by Janice Reichert

Lecture summary written by Czeslaw Radziejewski, PhD.

Antibody Engineering & Therapeutics, held in December 2022, offered many opportunities to hear exciting and informative presentations by experts in the field, including Carolyn Bertozzi, Professor of Chemistry at Stanford University and 2022 Nobel prize laureate in Chemistry.

In her plenary lecture, Therapeutic Opportunities in Glycoscience: Bioorthogonal chemistry in translation, Prof. Bertozzi presented a retrospective of her remarkable contributions to chemical biology. She almost singlehandedly created the field of bioorthogonal chemistry, which is now used in the development of human biotherapeutics. Since its inception, bioorthogonal chemistry has had enormous scientific impact by enabling mechanisms to address a wide variety of biological questions.

Prof. Bertozzi was trained in traditional synthetic organic chemistry, but rapid advancements in biology inspired her to consider how chemical reactions might be reliably controlled within organisms. She started with the idea of performing chemical reactions in live cells. In contrast to organic synthesis, which is generally executed in organic solvents, often at high temperatures, chemistry done in live cells must occur in water at a pH close to physiological, at temperatures close to 37oC, and generally away from equilibrium. Carrying out reactions in living organisms is additionally complicated because the molecules used in-vivo cannot be toxic and cannot be metabolized faster than the reaction rate with a biological target. For such chemistry, Bertozzi coined the name and formulated the concept of bioorthogonal chemistry, which is chemistry that does not interact or interfere with a biological system. Bioorthogonal reagents and reactions must not have counterparts in biological systems. [1]

Prof. Bertozzi’s research focused on glycans, which are complex polysaccharides that decorate the surface of every mammalian cell. Notably, the structure and composition of glycans displayed on the cell surface undergo alterations in response to the physiological state of an organism. In normal cells, oligosaccharide structures terminate with the sialic acid, but it has been known since the 1960s that the glycosylation pattern on cancer cells is dramatically different from normal cells. Cancer cells tend to have a much higher abundance of sialic acids, which are attached to different sugars and in different linkages than in healthy cells. This difference in glycosylation architecture could potentially be exploited for imaging glycosylation using bioorthogonal chemistry. To begin with, the oligosaccharides would have to be labeled with a bioorthogonal sugar derivative bearing a functional group. In the next step, the functional group on the incorporated unnatural sugar would react with a bioorthogonal, detectable probe molecule. The early idea for a molecule that could be metabolically incorporated in place of sialic acid came from the work of a German carbohydrate chemist, Werner Reutter, who reported that N-acetyl-modified mannosamine could be used by cells as a precursor of side-chain modified sialic acid. Based on this observation, Bertozzi’s conceived the idea that the methyl group in the N-acetyl group could be appended with azide functionality. Then, a reactive, abiotic molecule could serve as the probe. Nucleophilic azide can enter a reaction called Staudinger reduction with triphenylphosphine, but this reaction results in azide reduction to a primary amine. However, when one of the phenyl rings was modified with an ester leaving group, hydrolysis of the transition product (azo-ylide) resulted in a stable linkage of the phosphine to sialic acid. The stable coupling of phosphine to azide group on a sugar moiety is known as Staudinger ligation.

[Read more…]

Filed Under: Antibody Engineering & Therapeutics Tagged With: bioorthogonal chemistry, Carolyn Bertozzi

Thanks to all who participated in Antibody Engineering & Therapeutics Europe!

June 9, 2022 by The Antibody Society

Another very successful Antibody Engineering & Therapeutics Europe has concluded!

The Antibody Society thanks all the volunteers who helped at the booth:

 

  • Demelza Willemsz (Genmab)
  • Thomas Wesselink (Genmab)
  • Chalana Zilvold – van den Oever (Genmab)
  • Charlotte Berendsen (Genmab)
  • Lisa King (Amsterdam UMC)
  • Milon de Jong (Amsterdam UMC)

In addition to Thomas, Milon and Lisa, Kerry Chester (Board of Directors member), Janine Schuurman (Society Vice President) and Sally Ward (Society President) appear in the image above.

We hope to see you in Amsterdam in June 2023 for the next Antibody Engineering & Therapeutics Europe.

Filed Under: Antibody Engineering & Therapeutics, The Antibody Society Tagged With: antibody engineering, antibody therapeutics

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