Enhanced endoplasmic reticulum entry of tumor antigen is crucial for cross-presentation induced by dendritic cell-targeted vaccination

J Immunol. 2013 Dec 15;191(12):6010-21. doi: 10.4049/jimmunol.1302312. Epub 2013 Nov 11.

Abstract

Efficient cross-presentation of protein Ags to CTLs by dendritic cells (DCs) is essential for the success of prophylactic and therapeutic vaccines. In this study, we report a previously underappreciated pathway involving Ag entry into the endoplasmic reticulum (ER) critically needed for T cell cross-priming induced by a DC-targeted vaccine. Directing the clinically relevant, melanoma Ag gp100 to mouse-derived DCs by molecular adjuvant and chaperone Grp170 substantially facilitates Ag access to the ER. Grp170 also strengthens the interaction of internalized protein Ag with molecular components involved in ER-associated protein dislocation and/or degradation, which culminates in cytosolic translocation for proteasome-dependent degradation and processing. Targeted disruption of protein retrotranslocation causes exclusive ER retention of tumor Ag in mouse bone marrow-derived DCs and splenic CD8(+) DCs. This results in the blockade of Ag ubiquitination and processing, which abrogates the priming of Ag-specific CD8(+) T cells in vitro and in vivo. Therefore, the improved ER entry of tumor Ag serves as a molecular basis for the superior cross-presenting capacity of Grp170-based vaccine platform. The ER access and retrotranslocation represents a distinct pathway that operates within DCs for cross-presentation and is required for the activation of Ag-specific CTLs by certain vaccines. These results also reinforce the importance of the ER-associated protein quality control machinery and the mode of the Ag delivery in regulating DC-elicited immune outcomes.

Publication types

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

MeSH terms

  • ADP Ribose Transferases / pharmacology
  • Adjuvants, Immunologic*
  • Adoptive Transfer
  • Animals
  • Antigen Presentation / immunology*
  • Bacterial Toxins / pharmacology
  • Bone Marrow Cells / immunology
  • Cancer Vaccines / immunology*
  • Cancer Vaccines / pharmacokinetics
  • Cell Lineage
  • Cells, Cultured
  • Cross-Priming / immunology*
  • Cytosol / metabolism
  • Dendritic Cells / classification
  • Dendritic Cells / immunology*
  • Endocytosis / immunology
  • Endoplasmic Reticulum / immunology*
  • Endosomes / metabolism
  • Exotoxins / pharmacology
  • Glycoproteins / immunology*
  • HSP70 Heat-Shock Proteins / immunology*
  • Membrane Proteins / antagonists & inhibitors
  • Membrane Proteins / genetics
  • Membrane Proteins / physiology
  • Mice
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Protein Processing, Post-Translational
  • Protein Transport
  • Proteolysis
  • Pseudomonas aeruginosa Exotoxin A
  • RNA, Small Interfering / pharmacology
  • Recombinant Fusion Proteins / immunology
  • Recombinant Fusion Proteins / pharmacokinetics
  • SEC Translocation Channels
  • Spleen / cytology
  • Spleen / immunology
  • T-Lymphocytes, Cytotoxic / immunology*
  • Ubiquitination
  • Vaccination / methods*
  • Virulence Factors / pharmacology
  • gp100 Melanoma Antigen / genetics
  • gp100 Melanoma Antigen / immunology*
  • gp100 Melanoma Antigen / pharmacokinetics

Substances

  • Adjuvants, Immunologic
  • Bacterial Toxins
  • Cancer Vaccines
  • Exotoxins
  • Glycoproteins
  • HSP70 Heat-Shock Proteins
  • Membrane Proteins
  • RNA, Small Interfering
  • Recombinant Fusion Proteins
  • SEC Translocation Channels
  • SEC61A1 protein, mouse
  • Virulence Factors
  • glucose-regulated protein 170
  • gp100 Melanoma Antigen
  • ADP Ribose Transferases