The Expression Patterns Of Hsp70 Induced By Hantavirus Infection In Vivo

The expression of heat-shock proteins (HSPs), the representive of heat shock response (HSR), is characteristic of all organisms in response to a variety of stresses, and it is required for the survival of cells. HSP70, one member of HSPs families, play important physiological roles in protein folding, assembling and transportation, and protect cell from the deleterious effects of stresses, and also recruited by virus as a crucial part of viral survival strategies. We previously found that HSPs could be induced both in vivo and in vitro in the cells infected by Hantavirus (HTV), the causative agent of hemorrhagic fever with renal syndrome (HFRS), and intereact with viral proteins. On the basis of those findings, the goal of present study is to explore the pattern and quantify the stress response after cells infected with HTV. We perform quantitive study on the relationship between the virus infection and the HSP70 induction at the protein and mRNA levels and explore significance of stress response in Vero-E6 cell and Human umbilical vein vascular endothelial cell (HUVEC) induced by HTV infection.Vero-E6 cell, as a conventional host cell for HTV, was used as infection model. HTV nucleicapsid protein was detected 24 hr after infection, confirming the successful infection by hantaan 76-118. In situ hybridization and RT-PCR were used to evaluate the level of HSP70 mRNA during virus infection. HSP70 mRNA increased 0.5 hr after infection, reached its peak by 12 hr and gradually declined to steady state level by 72 hr. The expression of...