Premium
REVIEW ARTICLE: Secreted Heat Shock Protein gp96‐Ig: An Innovative Vaccine Approach
Author(s) -
Strbo Natasa,
Podack Eckhard R.
Publication year - 2008
Publication title -
american journal of reproductive immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.071
H-Index - 97
eISSN - 1600-0897
pISSN - 1046-7408
DOI - 10.1111/j.1600-0897.2008.00594.x
Subject(s) - heat shock protein , chaperone (clinical) , biology , microbiology and biotechnology , immune system , hsp90 , hsp70 , endoplasmic reticulum , acquired immune system , adjuvant , immunology , biochemistry , gene , medicine , pathology
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.