Members of a unique histidine acid phosphatase family are conserved amongst a group of primitive eukaryotic human pathogens

• Published in: Molecular and cellular biochemistry 2003-03, Vol.245 (1-2), p.31-41
• Main Authors: Shakarian, Alison M, Joshi, Manju B, Yamage, Mat, Ellis, Stephanie L, Debrabant, Alain, Dwyer, Dennis M
• Format: Article
• Language: English
• Subjects: Acid Phosphatase - chemistry; Acid Phosphatase - metabolism; Acids; Animals; Biomarkers, Tumor; Chromosomes; Crithidia; DNA, Protozoan - analysis; Enzymatic activity; Enzymes; Eukaryotic Cells - chemistry; Histidine; Humans; Isoenzymes - chemistry; Isoenzymes - metabolism; Leishmania; Leishmania donovani; Leishmania donovani - enzymology; Leishmania donovani - genetics; Leishmania donovani - metabolism; Leishmania infantum - enzymology; Leishmania infantum - genetics; Leishmania infantum - metabolism; Leishmania major - enzymology; Leishmania major - genetics; Leishmania major - metabolism; Leishmania mexicana - enzymology; Leishmania mexicana - genetics; Leishmania mexicana - metabolism; Leishmania tropica - enzymology; Leishmania tropica - genetics; Leishmania tropica - metabolism; Leptomonas seymouri; Parasites; Pathogens; Phytomonas serpens; Tartrate-Resistant Acid Phosphatase; Trypanosoma - chemistry; Trypanosoma - genetics; Trypanosoma - metabolism; Trypanosoma brucei; Trypanosoma cruzi
• ISSN: 0300-8177; 1573-4919
• DOI: 10.1023/A:1022851914014

Recently, we identified and characterized the genes encoding several distinct members of the histidine-acid phosphatase enzyme family from Leishmania donovani, a primitive protozoan pathogen of humans. These included genes encoding the heavily phosphorylated/glycosylated, tartrate-sensitive, secretory acid phosphatases (Ld SAcP-1 and Ld SAcP-2) and the unique, tartrate-resistant, externally-oriented, surface membrane-bound acid phosphatase (Ld MAcP) of this parasite. It had been previously suggested that these enzymes may play essential roles in the growth, development and survival of this organism. In this report, to further examine this hypothesis, we assessed whether members of the L. donovani histidine-acid phosphatase enzyme family were conserved amongst other pathogenic Leishmania and related trypanosomatid parasites. Such phylogenetic conservation would clearly indicate an evolutionary selection for this family of enzymes and strongly suggest and support an important functional role for acid phosphatases to the survival of these parasites. Results of pulsed field gel electrophoresis and Southern blotting showed that homologs of both the Ld SAcPs and Ld MAcP were present in each of the visceral and cutaneous Leishmania species examined (i.e. isolates of L. donovani, L. infantum, L. tropica, L. major and L. mexicana, respectively). Further, results of enzyme assays showed that all of these organisms expressed both tartrate-sensitive and tartrate-resistant acid phosphatase activities. In addition, homologs of both the Ld SAcPs and Ld MAcP genes and their corresponding enzyme activities were also identified in two Crithidia species (C. fasciculata and C. luciliae) and in Leptomonas seymouri. In contrast, Trypanosoma brucei, Trypanosoma cruzi and Phytomonas serpens had only very-low levels of such enzyme activities. Cumulatively, results of this study showed that homologs of the Ld SAcPs and Ld MAcP are conserved amongst all pathogenic Leishmania sps. suggesting that they may play significant functional roles in the growth, development and survival of all members of this important group of human pathogens.