Phenotypically distinct helper NK cells are required for gp96-mediated anti-tumor immunity

Sci Rep. 2016 Jul 19:6:29889. doi: 10.1038/srep29889.

Abstract

A number of Heat Shock Proteins (HSPs), in the extracellular environment, are immunogenic. Following cross-presentation of HSP-chaperoned peptides by CD91(+) antigen presenting cells (APCs), T cells are primed with specificity for the derivative antigen-bearing cell. Accordingly, tumor-derived HSPs are in clinical trials for cancer immunotherapy. We investigate the role of NK cells in gp96-mediated anti-tumor immune responses given their propensity to lyse tumor cells. We show that gp96-mediated rejection of tumors requires a unique and necessary helper role in NK cells. This helper role occurs during the effector phase of the anti-tumor immune response and is required for T cell and APC function. Gp96 activates NK cells indirectly via APCs to a phenotype distinct from NK cells activated by other mechanisms such as IL-2. While NK cells have both lytic and cytokine producing properties, we show that gp96 selectively activates cytokine production in NK cells, which is important in the HSP anti-tumor immune response, and leaves their cytotoxic capacity unchanged.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigen-Presenting Cells / immunology
  • Antigens, Neoplasm / immunology
  • Cross-Priming / immunology
  • Heat-Shock Proteins / immunology*
  • Heat-Shock Proteins / therapeutic use
  • Humans
  • Immunity, Cellular*
  • Interleukin-2 / immunology
  • Killer Cells, Natural / immunology*
  • Low Density Lipoprotein Receptor-Related Protein-1 / immunology
  • Membrane Glycoproteins / immunology
  • Molecular Chaperones
  • Peptides / immunology
  • Peptides / therapeutic use
  • T-Lymphocytes / immunology
  • T-Lymphocytes, Helper-Inducer / immunology*

Substances

  • Antigens, Neoplasm
  • Heat-Shock Proteins
  • Interleukin-2
  • Low Density Lipoprotein Receptor-Related Protein-1
  • Membrane Glycoproteins
  • Molecular Chaperones
  • Peptides
  • endoplasmin