Figure 5.

A model of the “guardian of Hsp70” function of TPR-containing co-chaperones. The ATP-dependent Hsp70 molecular chaperone is usurped by TBSV to facilitate recruitment of viral components to the subcellular (peroxisomal) membranes and also to promote VRC assembly. However, TPR-containing co-chaperones, such as the yeast Cyp40-like Cpr7p, Ttc4 oncogene-like Cns1p, and the Hop/Sti1 co-chaperones, might protect the Hsp70 chaperones from falling easy “prey” to TBSV by interacting with viral components. These events lead to the inhibition of viral processes, as shown, explaining how these co-chaperones work as CIRFs.