Heat shock cognate protein 70 is required for rice stripe tenuivirus accumulation and transmission in small brown planthopper.

Rice stripe tenuivirus (RSV) is mainly transmitted by the insect vector small brown planthopper (SBPH, Laodelphax striatellus) in a persistent-propagative manner. Virus transmission is dependent on the interplay between viral proteins and vector factors. Pc2, a nonstructural protein of RSV, plays an important role in virus transmission. However, the vector proteins that interact with Pc2 are unknown. In this study, we identified three SBPH proteins that interact with the N-terminal 381 amino acids of Pc2 (Pc2N) by using a yeast two-hybrid system (Y2H). The interaction of Pc2N with heat shock protein cognate 70 (HSC70) was studied further. HSC70 was verified to interact with RSV Pc2N by biomolecular fluorescence complementation and co-immunoprecipitation assays. HSC70 colocalized with RSV Pc2N in both Sf9 cells and the hemocytes of SBPHs. Inhibition of HSC70 expression via RNA interference reduced virus levels in hemolymph and salivary glands of SBPHs and resulted in decreased virus transmission efficiency. These data provide evidence that a vector protein, HSC70, is employed by RSV to facilitate virus accumulation in the hemolymph and thereby promote virus transmission. These findings are important for a better understanding of the interactions between plant viruses and insect vectors.