Molecular dissection of the functional domains of a unique, tartrate-resistant, surface membrane acid phosphatase in the primitive human pathogen Leishmania donovani

Alison M. Shakarian, Manju B. Joshi, Elodie Ghedin, Dennis M. Dwyer

Research output: Contribution to journalArticle

Abstract

The primitive trypanosomatid pathogen of humans, Leishmania donovani, constitutively expresses a unique externally oriented, tartrate-resistant, acid phosphatase on its surface membrane. This is of interest because these organisms are obligate intracellular protozoan parasites that reside and multiply within the hydrolytic milieu of mammalian macrophage phago-lysosomes. Here we report the identification of the gene encoding this novel L. donovani enzyme. In addition, we characterized its structure, demonstrated its constitutive expression in both parasite developmental forms, and determined the cell surface membrane localization of its translated protein product. Further, we used a variety of green fluorescent protein chimeric constructs as reporters in a homologous leishmanial expression system to dissect the functional domains of this unique, tartrate-resistant, surface membrane enzyme.

Original languageEnglish (US)
Pages (from-to)17994-18001
Number of pages8
JournalJournal of Biological Chemistry
Volume277
Issue number20
DOIs
StatePublished - May 17 2002

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Leishmania donovani
Dissection
Pathogens
Acid Phosphatase
Parasites
Membranes
Enzymes
Green Fluorescent Proteins
Lysosomes
Gene encoding
Macrophages
Cell Membrane
Genes
Proteins
tartaric acid
Tartrate-Resistant Acid Phosphatase

ASJC Scopus subject areas

  • Biochemistry

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Molecular dissection of the functional domains of a unique, tartrate-resistant, surface membrane acid phosphatase in the primitive human pathogen Leishmania donovani. / Shakarian, Alison M.; Joshi, Manju B.; Ghedin, Elodie; Dwyer, Dennis M.

In: Journal of Biological Chemistry, Vol. 277, No. 20, 17.05.2002, p. 17994-18001.

Research output: Contribution to journalArticle

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