Secreted heat shock protein gp96-Ig: An innovative vaccine approach

Natasa Strbo, Eckhard R. Podack

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Heat shock proteins (HSPs) are a large family of proteins with different molecular weights and different intracellular localizations. These proteins undertake crucial functions in maintaining cell homeostasis, and therefore they have been conserved during evolution. HSP gp96 also known as glucose-regulated protein grp94, is the primary chaperone of the endoplasmatic reticulum. Gp96/grp94, because of its peptide chaperone capacity and its ability to interact actively with professional antigen-presenting cells (APCs), is also endowed with crucial immunological functions such as natural adjuvant for priming innate and adaptive immunity. To make gp96 accessible to the immune system without biochemical purification and without cell lysis, we generated a secreted form of gp96. The immunological properties of secreted gp96 and its implications for vaccine in human cancer and infectious diseases will be discussed.

Original languageEnglish
Pages (from-to)407-416
Number of pages10
JournalAmerican Journal of Reproductive Immunology
Volume59
Issue number5
DOIs
StatePublished - May 1 2008

Fingerprint

Heat-Shock Proteins
Vaccines
Reticulum
Adaptive Immunity
Antigen-Presenting Cells
Innate Immunity
Communicable Diseases
Immune System
Proteins
Homeostasis
Molecular Weight
Peptides
Neoplasms
glucose-regulated proteins

Keywords

  • CD8 CTL
  • gp96
  • Heat shock proteins
  • Immunotherapy
  • Vaccine

ASJC Scopus subject areas

  • Immunology
  • Obstetrics and Gynecology

Cite this

Secreted heat shock protein gp96-Ig : An innovative vaccine approach. / Strbo, Natasa; Podack, Eckhard R.

In: American Journal of Reproductive Immunology, Vol. 59, No. 5, 01.05.2008, p. 407-416.

Research output: Contribution to journalArticle

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