ArticleEukaryotic cell2013
Role of cytosolic glyceraldehyde-3-phosphate dehydrogenase in visceral organ infection by Leishmania donovani.
Article in Eukaryotic cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Uncovering therapeutic targets in Leishmania donovani through comparative network topology analysis.Archives of microbiology · 2025Article
- Targeted protein degradation might present a novel therapeutic approach in the fight against African trypanosomiasis.European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences · 2023Article
- Metabolic Pathways ofPharmaceutics · 2022Review
- Molecular characterization of glyceraldehyde-3-phosphate dehydrogenase from Eimeria tenella.Parasitology research · 2022Article
- Profilin is involved in G1 to S phase progression and mitotic spindle orientation during Leishmania donovani cell division cycle.PloS one · 2022Article
- Repurposing bioenergetic modulators against protozoan parasites responsible for tropical diseases.International journal for parasitology. Drugs and drug resistance · 2020Article
- Iron and Heme Metabolism at the Leishmania-Host Interface.Trends in parasitology · 2020Review
- Myeloid Cell-Derived HIF-1α Promotes Control of Leishmania major.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- Trypanosoma evansi is alike to Trypanosoma brucei brucei in the subcellular localisation of glycolytic enzymes.Memorias do Instituto Oswaldo Cruz · 2015Article
- Article
- Regulation and biological function of a flagellar glucose transporter in Leishmania mexicana: a potential glucose sensor.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Evidence for loss of a partial flagellar glycolytic pathway during trypanosomatid evolution.PloS one · 2014Article
- In-silico Leishmania target selectivity of antiparasitic terpenoids.Molecules (Basel, Switzerland) · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The initial 7 steps of the glycolytic pathway from glucose to 3-phosphoglycerate are localized in the glycosomes in Leishmania, including step 6, catalyzed by the enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). In L. donovani and L. mexicana, there exists a second GAPDH enzyme present in the cytosol that is absent in L. braziliensis and that has become a pseudogene in L. major. To investigate the role of the cytosolic GAPDH (cGAPDH), an L. donovani cGAPDH-null mutant was generated, and conversely, the functional L. donovani cGAPDH was introduced into L. major and the resulting engineered parasites were characterized. The L. donovani cGAPDH-null mutant was able to proliferate at the same rate as the wild-type parasite in glucose-deficient medium. However, in the presence of glucose, the L. donovani cGAPDH-null mutant consumed less glucose and proliferated more slowly than the wild-type parasite and displayed reduced infectivity in visceral organs of experimentally infected mice. This demonstrates that cGAPDH is functional in L. donovani and is required for survival in visceral organs. Restoration of cGAPDH activity in L. major, in contrast, had an adverse effect on L. major proliferation in glucose-containing medium, providing a possible explanation of why it has evolved into a pseudogene in L. major. This study indicates that there is a difference in glucose metabolism between L. donovani and L. major, and this may represent an important factor in the ability of L. donovani to cause visceral disease.
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