Abstract

One major challenge in developing effective vaccines is to design a vaccine that can induce effective immune responses to the desired antigen with no or very limited side effects. The immunogenicity can be improved by using appropriate carriers and adjuvant molecules. Heat shock proteins (HSPs) are some of the most conserved proteins present in all prokaryotes and eukaryotes which posses highly immunogenic effect and function as adjuvants that may play a crucial role in integrating innate and adaptive immunity. Mycobacterium tuberculosis HSP70 (mHSP70) consists of three functionally distinct domains: an N-terminal 44 kDa ATPase portion (amino acids 1-358), followed by an 18 kDa peptide-binding domain (amino acids 359-494) and a 10 kDa fragment (amino acids 495-610). However, the C-terminal portion (amino acids 359-610) was proven to stimulate the production of CC chemokines, interleukin-12 (IL-12), tumor necrosis factor-alfa (TNF-á), nitric oxide (NO) and the maturation of dendritic cells (DCs). In addition, a cytotoxic cell-inducing function was demonstrated in the ATPase portion (amino acids 161-370) of mHSP70. In this review, we peruse about several HSP-based vaccines as background for more detailed discussions about M. tuberculosis HSP molecule structure, function and usage as a novel vaccine adjuvants. © IDOSI Publications, 2011.