Reduced transcript levels of the heat shock protein 70 gene in diminazene aceturate-resistant Babesia gibsoni variants under low concentrations of diminazene aceturate

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In our previous report, we developed a diminazene aceturate (DA)-resistant Babesiagibsoni strain that was maintained in culture with 200 ng/ml DA. While developing thisstrain, we also obtained DA-resistant B. gibsoni variants, which were maintained inculture with DA from 1 to 175 ng/ml for more than 8 weeks. Because heat shock protein 70(Hsp70) seems to play important roles in adaptation to a stress environment in protozoanparasites, in the present study, we examined the copy number of B. gibsoni Hsp70(BgHsp70) transcripts of those DA-resistant variants using quantitative real-time reversetranscription-polymerase chain reaction. We found that when wild-type B. gibsoni wasexposed to 1 ng/ml DA, the level of BgHsp70 transcripts was decreased at day 14. The copynumber of BgHsp70 transcripts in the DA-resistant variant cultured with 1 ng/ml DA wassignificantly lower than in wild-type B. gibsoni, while those in DA-resistant variantsincreased with escalating doses of DA from 1 to 75 ng/ml, although they were lower thanin wild-type B. gibsoni. However, those in DA-resistant variants cultured with ＞ 125 ng/mlDA were almost the same as wild-type B. gibsoni. These results indicated that thetranscript levels of the BgHsp70 gene might be reduced when the parasites are exposed toa low concentration of DA, and then might recover to the normal level after achievingresistance against DA. We expect that further study of the function of BgHsp70 willelucidate the mechanism of drug resistance against DA in B. gibsoni.

Reduced transcript levels of the heat shock protein 70 gene in diminazene aceturate-resistant Babesia gibsoni variants under low concentrations of diminazene aceturate

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