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E610 sialidase

Development stage: Preclinical
Lead developer: Palleon Pharmaceuticals
Modality: Replacement Enzymes → Therapeutic Enzymes → Recombinant Proteins and Enzymes

Overview

E610 sialidase is an experimental recombinant human sialidase enzyme developed by Palleon Pharmaceuticals as part of its EAGLE (Enzyme Antibody Glyco-Ligand Editing) glyco-immunology platform for cancer immunotherapy. It catalyzes the cleavage of terminal sialic acids from sialoglycoconjugates on stromal and immune cells, thereby reducing engagement of inhibitory Siglec receptors (such as Siglec-10) and reversing stromal cell–induced immunosuppression of macrophages and natural killer cells in the tumor microenvironment.[7][10] In preclinical colorectal cancer models, E610-mediated desialylation of cancer-associated fibroblasts and mesenchymal stromal cells decreased immunosuppressive marker expression, increased macrophage activation and NK cell cytotoxicity, and promoted sustained systemic antitumor immunity.[7]

Other names: sialidase (E610)

Targets

SA (Sialic acid)

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