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

Natasa Strbo, Eckhard R Podack

Research output: Contribution to journalReview articlepeer-review

29 Scopus citations


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


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

ASJC Scopus subject areas

  • Immunology
  • Obstetrics and Gynecology


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