LAUSR

Heat shock protein 90 (HSP90) is a molecular chaperon and an essential component for stage differentiation and intracellular growth inside the host cells of many protozoans. HSP90 of Babesia gibsoni (BgHSP90) was suggested to function in the development of diminazene aceturate (DA)-resistance. Therefore, we examined the expression level of BgHSP90 in a DA-resistant B. gibsoni isolate. Transcription of the BgHSP90 gene in the DA-resistant isolate and wild-type B. gibsoni was assessed by quantitative real-time reverse transcription-polymerase chain reaction (qRT-PCR). As a result, the copy number and relative amount of BgHSP90 transcripts in the DA-resistant isolate were significantly lower than those in the wild-type. Moreover, a rabbit anti-recombinant BgHSP90 antibody was developed, and the protein synthesis of BgHSP90 in the DA-resistant isolate was compared with that in the wild-type by Western blot analysis and indirect fluorescence assay. There was significantly less BgHSP90 protein than in the wild-type. Additionally, the relative intensity of BgHSP70 in DA-resistant isolate was also lower than that in the wild-type. This suggested that the expression of BgHSP90 and BgHSP70 in the DA-resistant B. gibsoni isolate was suppressed and that the reduced amount of BgHSP90 and BgHSP70 might cause the weak proliferation of the DA-resistant isolate. Further studies are necessary to elucidate the function of BgHSP90.