Heat shock protein (HSPs) is a group of highly conserved proteins, which is produced by cells under stress conditions. HSP70 family is the most conservative and important class in HSPs. HSP70 widely appears in various cells and participates in the protein metabolism in emergency and non-emergency conditions, such as protein folding, translocation across membranes, degradation of misfolded peptides and regulation of the processes. With the detailed studies, the role of HSP70 in anti-tumor and intracellular microbial infection has been discovered and confurmed. HSP70 molecule is composed of three different regions. The C-terminal domain has a substrate binding domain, which is different in various species. This article reviewed the basic structure of Toxoplasma gondii heat shock protein 70 (TgHSP70), the role of TgHSP70 on immune protection and its toxicity, as well as its function on the stage conversion of Toxoplasma gondii.