The role of heat shock protein 90 in the proliferation of Babesia gibsoni in vitro

The present study investigated the role of heat shock protein 90 (HSP90) in the proliferation and survival of Babesia gibsoni in vitro. To detect the effect on the entry of B. gibsoni into host erythrocytes, the parasite was incubated with an antibody against B. gibsoni HSP90 (BgHSP90) for 24 h. The results of this experiment demonstrated that both the incorporation of [3H]hypoxanthine into the nucleic acids of B. gibsoni and the number of parasites were not altered, indicating that an anti-BgHSP90 antibody did not directly inhibit the entry of the parasite into erythrocytes. Moreover, two HSP90 inhibitors, geldanamycin (GA) and tanespimycin (17AAG), were used to evaluate the function of BgHSP90. GA and 17-AAG decreased both the incorporation of [3H] hypoxanthine and the number of infected erythrocytes, suggesting that BgHSP90 plays important roles in DNA synthesis and the proliferation of B. gibsoni. The effect of 17-AAG on the parasites was weaker than that of GA. Additionally, the effect of GA on the survival and superoxide generation of canine neutrophils was assessed. The survival of canine neutrophils was not affected. The superoxide generation was strongly suppressed by GA. This result indicated that GA inhibited the function of canine neutrophils. Additional studies are necessary to elucidate the role of BgHSP90 in the proliferation of the parasite.

Automated summary

This study investigated the role of heat shock protein 90 (HSP90) in the proliferation and survival of Babesia gibsoni in vitro. It was found that an anti-BgHSP90 antibody did not directly inhibit the entry of the parasite into erythrocytes. Two HSP90 inhibitors, geldanamycin (GA) and tanespimycin (17AAG), were shown to decrease DNA synthesis and the number of infected erythrocytes, indicating the important roles of BgHSP90 in the proliferation of the parasite. GA was found to suppress the superoxide generation in canine neutrophils.