Heat shock protein 90 of Pacific white shrimp (Litopenaeus vannamei) is possibly involved in promoting white spot syndrome virus infection

Viruses cause up to 60% of disease-associated losses in shrimp aquaculture, and the white spot syndrome virus (WSSV) is a major viral pathogen in shrimp. Heat shock proteins (HSPs) are host chaperones that help promote many viral infections. We investigated the involvement of Litopenaeus vannamei (Lv) HSP90 in WSSV infections. Expression of LvHSP90 at the transcript and protein levels were upregulated after WSSV infection. Silencing LvHSP90 resulted in the increased cumulative mortality rate and the reduction of circulating hemocytes. The inhibition of LvHSP90 also induced the expression of apoptosis-related genes which indicated the induction of apoptotic pathway and might lead to shrimp death. However, lower the number of WSSV-infected cells and viral copy numbers were detected in the LvHSP90-silenced shrimp compared with those of the controls, corresponding with significantly decreased expressions of viral genes, including the immediate-early genes WSV083 and WSV249 and viral DNA polymerase. Conversely, injecting shrimp with WSSV that had been co-incubated with a recombinant LvHSP90 (rLvHSP90) promoted WSSV infection as evidenced by an increased cumulative mortality rate and viral copy numbers at 40-48 h post infection (hpi). Subcellular localization of LvHSP90 in WSSV-infected hemocytes at 3, 6 and 12 hpi demonstrated increased expression and translocation of LvHSP90 into the nucleus where WSSV DNA can replicate. Thus, LvHSP90 might be involved in the WSSV pathogenesis by promoting WSSV replication.