Blockade of N-Glycosylation Promotes Antitumor Immune Response of T Cells

J Immunol. 2020 Mar 1;204(5):1373-1385. doi: 10.4049/jimmunol.1900937. Epub 2020 Jan 22.

Abstract

Adoptive cellular therapy and its derivative, chimeric AgR T cell therapy, have achieved significant progress against cancer. Major barriers persist, however, including insufficient induction of cytotoxic T cells and exhaustion of tumor-infiltrating lymphocytes. In this study, we discovered a new role for 2-deoxy-d-glucose (2DG) in enhancing the antitumor activity of human T cells against NKG2D ligand-expressing tumor cells. Human T cells treated with 2DG upregulated the NK-specific transcription factors TOX2 and EOMES, thereby acquiring NK cell properties, including high levels of perforin/granzyme and increased sensitivity to IL-2. Notably, rather than inhibiting glycolysis, 2DG modified N-glycosylation, which augmented antitumor activity and cell surface retention of IL-2R of T cells. Moreover, 2DG treatment prevented T cells from binding to galectin-3, a potent tumor Ag associated with T cell anergy. Our results, therefore, suggest that modifying N-glycosylation of T cells with 2DG could improve the efficacy of T cell-based immunotherapies against cancer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Deoxyglucose / pharmacology*
  • Glycosylation / drug effects
  • HMGB Proteins / immunology
  • Humans
  • Immunity, Cellular / drug effects*
  • Immunotherapy
  • Interleukin-2 / immunology
  • K562 Cells
  • NK Cell Lectin-Like Receptor Subfamily K / immunology
  • Neoplasm Proteins / immunology
  • Neoplasms / immunology*
  • Neoplasms / pathology
  • Neoplasms / therapy
  • T-Box Domain Proteins / immunology
  • T-Lymphocytes / immunology*
  • T-Lymphocytes / pathology

Substances

  • EOMES protein, human
  • HMGB Proteins
  • IL2 protein, human
  • Interleukin-2
  • KLRK1 protein, human
  • NK Cell Lectin-Like Receptor Subfamily K
  • Neoplasm Proteins
  • T-Box Domain Proteins
  • Tox2 protein, human
  • Deoxyglucose