Transient 40 °C-shock potentiates cytotoxic responses of Vδ2+ γδ T cell via HSP70 upregulation

Cancer Immunol Immunother. 2022 Oct;71(10):2391-2404. doi: 10.1007/s00262-022-03164-x. Epub 2022 Feb 23.

Abstract

Vδ2+ γδ T cell, one of promising strategies for tumor immunotherapy, recognizes and kills cancer cells in a non-MHC dependent manner. Previously, we pioneeringly proved the clinical safety and efficacy of allogeneic Vδ2+ γδ T cells, in vitro expanded from healthy donors, in the treatment of late-stage cancer patients. Nevertheless, how to profoundly potentiate cytotoxic function of expanded Vδ2+ γδ T cells remains to be further explored. Here, we proposed that 40 °C-Shock could be a simple and reliable approach to in vitro boost the effector function. We found that 40 °C-shock could phosphorylate two MAPK proteins ERK and p38 through HSP70, which facilitated actyl-α-tubulin and actin augments and reorganization, elevated Ki-67 expression and cell surface adhesion, and promoted releases of cytokines IFN-γ, perforin and granzyme B, as well as downregulated LAG3 expression. We also observed 40 °C-shock induced elevations of mitochondrial metabolism. These altogether led to potentiated cytotoxic responses against cancer cells. This proof-of-concept work demonstrated that 40 °C-shock would be probably developed into an effective method to in vitro boost the cytotoxicity of Vδ2+ γδ T cell before applying it in immunotherapy, and provided scientific evidences for the view that fever can activate immune responses of innate immune cells.

Keywords: 40 °C-shock; Cytotoxicity; HSP70; Vδ2+ γδ T cell.

MeSH terms

  • Cytokines / metabolism
  • HSP70 Heat-Shock Proteins* / metabolism
  • Hot Temperature
  • Humans
  • Immunotherapy
  • Intraepithelial Lymphocytes* / cytology
  • Neoplasms / therapy
  • Receptors, Antigen, T-Cell, gamma-delta
  • T-Lymphocytes* / cytology
  • Up-Regulation

Substances

  • Cytokines
  • HSP70 Heat-Shock Proteins
  • Receptors, Antigen, T-Cell, gamma-delta