Preprint Review Version 1 NOT YET PEER-REVIEWED

The Telomerase-Derived Anticancer Peptide Vaccine GV1001 as an Extracellular Heat Shock Protein-Mediated Cell-Penetrating Peptide

  1. Department of Microbiology and Immunology, Liver Research Institute, SNUMRC, College of Medicine, Seoul National University, Seoul 110-799, Korea
  2. Department of Microbiology, Konkuk University School of Medicine, Seoul 05029, Korea
Version 1 : Received: 11 November 2016 / Approved: 11 November 2016 / Online: 11 November 2016 (09:59:30 CET)

A peer-reviewed article of this Preprint also exists.

Kim, H.; Seo, E.-H.; Lee, S.-H.; Kim, B.-J. The Telomerase-Derived Anticancer Peptide Vaccine GV1001 as an Extracellular Heat Shock Protein-Mediated Cell-Penetrating Peptide. Int. J. Mol. Sci. 2016, 17, 2054. Kim, H.; Seo, E.-H.; Lee, S.-H.; Kim, B.-J. The Telomerase-Derived Anticancer Peptide Vaccine GV1001 as an Extracellular Heat Shock Protein-Mediated Cell-Penetrating Peptide. Int. J. Mol. Sci. 2016, 17, 2054.

Journal reference: Int. J. Mol. Sci. 2016, 17, 2054
DOI: 10.3390/ijms17122054

Abstract

Cell-penetrating peptides (CPPs), a group of small peptides capable of promoting the transport of molecular cargo across the plasma membrane, have become important tools in promoting the cellular uptake of exogenously delivered macromolecules. GV1001, a peptide derived from a reverse-transcriptase subunit of telomerase (hTERT) and developed as a vaccine against various cancers, reportedly has unexpected CPP properties. Unlike typical CPPs, such as the HIV-1 TAT peptide, GV1001 enabled the cytosolic delivery of macromolecules such as proteins, DNA and siRNA via extracellular heat shock protein 90 (eHSP90) and 70 (eHSP70) complexes. The eHSP-GV1001 interaction may have biological effects in addition to its cytosolic delivery function. GV1001 was originally designed as a MHC class II-binding cancer epitope, but its CPP properties may contribute to its strong anti-cancer immune response relative to other telomerase peptide-based vaccines. Cell signaling via eHSP-GV1001 binding may lead to unexpected biological effects, such as direct anticancer or antiviral effects. In this review, we focus on the CPP effects of GV1001 bound to eHSP90 and ehsp70.

Subject Areas

cell-penetrating peptides (CPPs); reverse-transcriptase-subunit of telomerase (hTERT); GV1001; heat shock protein 90

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