ArticleThe Biochemical journal2015
The Leishmania donovani histidine acid ecto-phosphatase LdMAcP: insight into its structure and function.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Structural basis of secreted acid phosphatase polymerization in the Leishmania parasite.Protein science : a publication of the Protein Society · 2026Article
- Characterization of the First Secreted Sorting Nexin Identified in theInternational journal of molecular sciences · 2024Article
- Development of a multi-epitope vaccine candidate for leishmanial parasites applying immunoinformatics andFrontiers in immunology · 2023Article
- In-silico design of an immunoinformatics based multi-epitope vaccine against Leishmania donovani.BMC bioinformatics · 2022Article
- TheFrontiers in cellular and infection microbiology · 2021Article
- Involvement ofFrontiers in cellular and infection microbiology · 2021Review
- Measurement of Acid Ecto-phosphatase Activity in LiveBio-protocol · 2019Article
- Genome Plasticity in CulturedFrontiers in microbiology · 2018Article
- Characterization of the Protein Tyrosine Phosphatase LmPRL-1 Secreted by Leishmania major via the Exosome Pathway.Infection and immunity · 2017Article
- Function of Macrophage and Parasite Phosphatases in Leishmaniasis.Frontiers in immunology · 2017Review
- The genetics of Leishmania virulence.Medical microbiology and immunology · 2015Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acid ecto-phosphatase activity has been implicated in Leishmania donovani promastigote virulence. In the present study, we report data contributing to the molecular/structural and functional characterization of the L. donovani LdMAcP (L. donovani membrane acid phosphatase), member of the histidine acid phosphatase (HAcP) family. LdMAcP is membrane-anchored and shares high sequence identity with the major secreted L. donovani acid phosphatases (LdSAcPs). Sequence comparison of the LdMAcP orthologues in Leishmania sp. revealed strain polymorphism and species specificity for the L. donovani complex, responsible for visceral leishmaniasis (Khala azar), proposing thus a potential value of LdMAcP as an epidemiological or diagnostic tool. The extracellular orientation of the LdMAcP catalytic domain was confirmed in L. donovani promastigotes, wild-type (wt) and transgenic overexpressing a recombinant LdMAcP-mRFP1 (monomeric RFP1) chimera, as well as in transiently transfected mammalian cells expressing rLdMAcP-His. For the first time it is demonstrated in the present study that LdMAcP confers tartrate resistant acid ecto-phosphatase activity in live L. donovani promastigotes. The latter confirmed the long sought molecular identity of at least one enzyme contributing to this activity. Interestingly, the L. donovani rLdMAcP-mRFP1 promastigotes generated in this study, showed significantly higher infectivity and virulence indexes than control parasites in the infection of J774 mouse macrophages highlighting thereby a role for LdMAcP in the parasite's virulence.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.