Chaperone protein DnaK (Heat shock protein 70) from Mycobacterium tuberculosis (DnaK (Hsp70))

Chaperone protein DnaK, commonly referred to as heat shock protein 70 (Hsp70) in Mycobacterium tuberculosis, is an essential and highly conserved molecular chaperone that facilitates protein folding, refolding, and cellular recovery from stress. It possesses intrinsic ATPase activity and operates as part of a protein complex with nucleotide exchange factors such as GrpE. DnaK plays key roles in the pathogen’s survival within host macrophages by protecting against environmental and immune-mediated stress. In addition to its cellular housekeeping activities, M. tuberculosis DnaK modulates host immunity: it can impair dendritic cell maturation, induce anti-inflammatory cytokine production (notably IL-10), and both stimulate and suppress immune responses depending on context. These properties make DnaK both a marker of infection/stress and a target of interest in infection, inflammation, and novel vaccine strategies, including its use as an adjuvant to boost immune responses in tuberculosis and cancer settings.

Other names

Heat shock protein 70Hsp70DnaKTBhsp70

Drugs or biologics targeting DnaK (Hsp70) may inhibit its ATPase activity, disrupt its protein folding function, or use recombinant forms to activate immune pathways (such as activation of TLR2/TLR4 or CD40 on dendritic cells, or enhance antigen processing/presentation).