Abstract
We describe a single aquaporin gene in Toxoplasma gondii which, surprisingly, has only 28% sequence similarity to the aquaglyceroporin of another apicomplexan parasite, Plasmodium falciparum. Sequence comparisons showed 47% similarity to water-specific plant aquaporins and the conservation of typical pore-forming residues. We established that the Toxoplasma aquaporin protein is a bifunctional membrane pore with intermediate water and high glycerol permeability. Furthermore, we identified hydroxyurea, an antineoplastic agent with inhibitory effects on parasite proliferation, as a permeant of this channel.
Original language | English |
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Pages (from-to) | 500-504 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 555 |
Issue number | 3 |
DOIs | |
State | Published - Dec 18 2003 |
Keywords
- Aquaglyceroporin
- Glycerol
- Hydroxyurea
- Plasmodium
- Toxoplasma
- Water