Journal
FRONTIERS IN BIOSCIENCE-LANDMARK
Volume 7, Issue -, Pages D43-D52Publisher
FRONTIERS IN BIOSCIENCE INC
DOI: 10.2741/manjili
Keywords
heat shock proteins (Hsps); danger signal; antigen presentation; chaperon; vaccine; immunogenicity; review
Categories
Funding
- NATIONAL CANCER INSTITUTE [P30CA016056, R01CA071599] Funding Source: NIH RePORTER
- NCI NIH HHS [CA71599, P30CA16056] Funding Source: Medline
- NIGMS NIH HHS [GM45944] Funding Source: Medline
Ask authors/readers for more resources
Tumor derived heat shock protein (hsp)-peptide complexes (particularly hsp70 and grp94/ gp96) have been demonstrated to serve as effective vaccines, producing antitumor immune responses in animals and in man. This approach utilizes the peptide binding properties of stress proteins which are responsible for their functions as molecular chaperones in numerous cellular processes. The present review briefly introduces the reader to the basic stress protein families, i.e. heat shock and glucose regulated proteins, their regulation, compartmentalization and family members. It then introduces the reader to aspects of hsps/grp function and interactions with the host's immune system. An overview of the conventional uses of hsp/grp vaccines as autologous vaccines derived from cancers is presented. We then discuss other stress protein related vaccination approaches. This includes the use of recombinant antigens, both proteins and peptides, naturally complexed to hsp/grps; hsp/grp DNA vaccines, hsp/grp fusion proteins and cell based hsp/grp vaccines. The advantages and disadvantages of each vaccination approach are discussed. Lastly, means of further enhancing the already potent activity of stress protein vaccines are presented, specifically the use of hyperthermia or CTLA-4 blockade as adjuvants.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available