| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 3417836 | Parasitology International | 2013 | 4 Pages |
A cDNA encoding farnesyl pyrophosphate synthase of Babesia bovis (BbFPPS) has been isolated, cloned and characterized as molecular drug target. Sequence analysis revealed that BbFPPS contains an open reading frame of 1011 bp with predicted 336 amino acids and molecular mass of 38 kDa. Antiserum raised in mice against recombinant BbFPPS expressed in Escherichia coli specifically reacted with native protein of B. bovis parasites by Western blot analysis and indirect immunofluorescent test. Enzymatic assay using recombinant BbFPPS revealed that the Km value of the enzyme for isopentenyl pyrophosphate and dimethylallyl pyrophosphate was 2.494 ± 1.536 μM. Risedronate inhibited the activity of BbFPPS yielding IC50 value of 8.4 ± 1.2 nM. Furthermore, the in vitro growth of B. bovis was significantly inhibited in the presence of a micromolar concentration of risedronate (IC50 = 4.02 ± 0.91 μM). No regrowth of B. bovis was observed at 10 μM of risedronate in the subsequent viability test. These results demonstrate that BbFPPS is the molecular target of risedronate, which could inhibit the in vitro growth of B. bovis.
Graphical abstractInhibitory curve of risedronate on the in vitro growth of B. bovis and its effects on the morphology of the parasites.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► FPPS is active enzyme in Babesia bovis. ► FPPS a potential molecular drug target of risedronate. ► Risedronate is a possible chemotherapeutic agent against bovine babesiosis.
