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Cryptosporidium parvum: identification and characterization of an acid phosphatase

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Abstract

Acid phosphatases are putative virulence factors in different pathogenic microorganisms. Acid phosphatases can also inhibit the respiratory burst of human neutrophils. In Cryptosporidium parvum, a protozoan parasitic, the study of enzymes is limited. In this paper, we report the presence of a membrane-bound acid phosphatase activity in C. parvum oocysts. The enzymatic activity was inhibited by protein tyrosine phosphatase inhibitors such as sodium orthovanadate, ammonium molybdate, and sodium tungstate and was not affected by protein serine/threonine phosphatase inhibitors such as okadaic acid and calyculin. Antibodies against the catalytic domain of human placental PTPase 1B cross-reacted with two molecules of 30 and 31 kDa present in membrane fraction of a Cryptosporidium oocyst homogenate. This is the first demonstration of acid phosphatase activity in Cryptosporidium.

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Acknowledgment

We thank Alma Escalona-Montaño and Lily Carlin for excellent technical assistance. Dr. Patricia Talamás Rohana for critically reading of the manuscript. This work was supported by grants R01 AI 41735-01, FD-R-001621, and 45052-M from CONACyT, México.

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Authors and Affiliations

  1. Department of Experimental Medicine, School of Medicine, UNAM, Dr. Balmis 148, Colonia Doctores, Mexico City, D.F., 06726, México

    María Magdalena Aguirre-García

  2. Department of Medicine, Division of Infectious Diseases, School of Public Health, The University of Texas Health Science Center in Houston, 6431 Fannin, MSB2.112, Houston, TX, 77030, USA

    Pablo C. Okhuysen

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  1. María Magdalena Aguirre-García
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  2. Pablo C. Okhuysen
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Correspondence to María Magdalena Aguirre-García.

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Aguirre-García, M.M., Okhuysen, P.C. Cryptosporidium parvum: identification and characterization of an acid phosphatase. Parasitol Res 101, 85–89 (2007). https://doi.org/10.1007/s00436-006-0457-8

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  • DOI: https://doi.org/10.1007/s00436-006-0457-8

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