Mechanism and complex roles of HSC70/HSPA8 in viral entry

•HSPA8 (heat shock protein family A member 8: also known as HSC70) is a major molecular chaperone protein and a member of the heat shock proteins.•The complex role and the regulatory mechanisms of HSC70 during viral entry are summarized.•These researches may provide a potential therapeutic target against the virus. The process of viruses entering host cells is complex, involving multiple aspects of the molecular organization of the cell membrane, viral proteins, the interaction of receptor molecules, and cellular signaling. Most viruses depend on endocytosis for uptake, when viruses reach the appropriate location, they are released from the vesicles, undergo uncoating, and release their genomes. Heat shock cognate protein 70(HSC70): also known as HSPA8, a protein involved in mediating clathrin-mediated endocytosis (CME), is involved in various viral entry processes. In this mini-review, our goal is to provide a summary of the function of HSC70 in viral entry. Understanding the interaction networks of HSC70 with viral proteins helps to provide new directions for targeted therapeutic strategies against viral infections.