Human T cell glycosylation and implications on immune therapy for cancer

• Published in: Human vaccines & immunotherapeutics Vol. 16; no. 10; pp. 2374 - 2388
• Main Authors: De Bousser, Elien, Meuris, Leander, Callewaert, Nico, Festjens, Nele
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 02.10.2020; Taylor & Francis Group
• Subjects: engineering; glycan-binding protein; Glycosylation; human T cell; Humans; immunotherapy; Neoplasms - therapy; Polysaccharides; Protein Processing, Post-Translational; Review; T-Lymphocytes; glycan-binding protein; Glycosylation; engineering; human T cell; immunotherapy
• ISSN: 2164-5515; 2164-554X
• DOI: 10.1080/21645515.2020.1730658

Glycosylation is an important post-translational modification, giving rise to a diverse and abundant repertoire of glycans on the cell surface, collectively known as the glycome. When focusing on immunity, glycans are indispensable in virtually all signaling and cell-cell interactions. More specifically, glycans have been shown to regulate key pathophysiological steps within T cell biology such as T cell development, thymocyte selection, T cell activity and signaling as well as T cell differentiation and proliferation. They are of major importance in determining the interaction of human T cells with tumor cells. In this review, we will describe the role of glycosylation of human T cells in more depth, elaborate on the importance of glycosylation in the interaction of human T cells with tumor cells and discuss the potential of cancer immunotherapies that are based on manipulating the glycome functions at the tumor immune interface. 1 , 2