Title : Glycoproteomic Analysis of
MGL-Binding Proteins on Acute T-Cell Leukemia Cells
Abstract :
- C-type lectins are a diverse group of proteins involved in many human physiological and pathological processes
- Most C-type lectins are glycan-binding proteins, some of which are pivotal for innate immune responses against pathogens
- Other C-type lectins, such as the macrophage galactose-type lectin ( MGL ), have been shown to induce immunosuppressive responses upon the recognition of aberrant glycosylation on cancer cells
- MGL is known to recognize terminal N-acetylgalactosamine (GalNAc) , such as the Tn antigen, which is commonly found on malignant cells
- Even though this glycan specificity of MGL is well described, there is a lack of understanding of the actual glycoproteins that bind MGL
- We present a glycoproteomic workflow for the identification of MGL-binding proteins, which we applied to study MGL ligands on the human Jurkat leukemia cell line
- In addition to the known MGL ligands and Tn antigen-carrying proteins CD43 and CD45 on these cells, we have identified a set of novel cell-surface ligands for MGL
- Importantly, for several of these, O-glycosylation has hitherto not been described
- Altogether, our data provide new insight into the identification and structure of novel MGL ligands that presumably act as modulatory molecules in cancer immune responses