Localisation of acid phosphatase activity on the surface of bloodstream forms of Trypanosoma congolense

Experimental Parasitology
O M TosombaJ D Lonsdale-Eccles

Abstract

In vitro, living bloodstream forms of Trypanosoma congolense were shown to hydrolyse p-nitrophenyl phosphate, a substrate for phosphatases. This activity appears to be from an acid phosphatase because it was enhanced at low pH values, was inhibited by the acid phosphatase inhibitor sodium fluoride, and was not inhibited by the alkaline phosphatase inhibitor tetramisole. The activity did not appear to be secreted into the surrounding medium by the living parasites although phosphatase activity could be detected in the surrounding medium when dead or dying parasites were present. Studies at various temperatures indicated that at least some of this acid phosphatase activity may be associated with the surface of the parasites, rather than with endocytic or intracellular systems. This was supported by subcellular fractionation of radiolabelled parasites which showed some cosedimentation of acid phosphatase activity with radiolabelled iodine. Histochemical studies of the parasites also supported this conclusion. Electron microscopical examination of trypanosomes incubated with lead nitrate and p-nitrophenyl phosphate showed lead phosphate deposits on the surface of the parasites in addition to the expected localisation in the flagell...Continue Reading

Citations

May 24, 2011·Journal of Parasitology Research·Marta T GomesJosé Roberto Meyer-Fernandes
Nov 30, 2011·Molecular and Biochemical Parasitology·Richard T KangetheTheresa H T Coetzer
Mar 3, 2001·The Journal of Parasitology·S J BlackN B Murphy
Jan 22, 2011·Journal of Bioenergetics and Biomembranes·Daniela Cosentino-Gomes, José Roberto Meyer-Fernandes
Apr 3, 2003·FEMS Microbiology Letters·Eloise Cedro FernandesHiroshi Aoyama
Jan 12, 2013·FEMS Microbiology Letters·Anne C S FernandesThaïs Souto-Padrón
Jul 12, 2002·Insect Biochemistry and Molecular Biology·Eliane FialhoMário A C Silva-Neto
Jul 10, 1998·Molecular and Biochemical Parasitology·T FuruyaR Docampo

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