ArticleParasitology research2008
Identification and enzymatic activities of four protein disulfide isomerase (PDI) isoforms of Leishmania amazonensis.
Article in Parasitology research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
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- A Calcium- and GTP-Dependent Transglutaminase inVeterinary sciences · 2023Article
- Nanomedicine-based strategies to improve treatment of cutaneous leishmaniasis.Royal Society open science · 2022Article
- Identification and Characterization of a Novel Protein Disulfide Isomerase Gene (International journal of molecular sciences · 2020Article
- Meloidogyne graminicola protein disulfide isomerase may be a nematode effector and is involved in protection against oxidative damage.Scientific reports · 2019Article
- An immunoproteomic approach to identifying immunoreactive proteins inPathogens and global health · 2019Article
- Emerging therapeutic targets for treatment of leishmaniasis.Expert opinion on therapeutic targets · 2018Review
- Identification and characterization of a putative protein disulfide isomerase (HsPDI) as an alleged effector of Heterodera schachtii.Scientific reports · 2017Article
- Molecular cloning and characterization of protein disulfide isomerase of Brugia malayi, a human lymphatic filarial parasite.EXCLI journal · 2017Article
- The protein disulfide isomerase 1 of Phytophthora parasitica (PpPDI1) is associated with the haustoria-like structures and contributes to plant infection.Frontiers in plant science · 2015Article
- Molecular cloning, expression, and immunolocalization of protein disulfide isomerase in excretory-secretory products from Clonorchis sinensis.Parasitology research · 2012Article
- Molecular characterization and immunolocalization of a protein disulfide isomerase from Angiostrongylus cantonensis.Parasitology research · 2012Article
- Leishmania major protein disulfide isomerase as a drug target: enzymatic and functional characterization.Parasitology research · 2012Article
- Identification of proteins in promastigote and amastigote-like Leishmania using an immunoproteomic approach.PLoS neglected tropical diseases · 2012Article
- Identification and characterization of genes involved in leishmania pathogenesis: the potential for drug target selection.Molecular biology international · 2011Article
- Protein disulfide isomerase and host-pathogen interaction.TheScientificWorldJournal · 2011Review
- A second protein disulfide isomerase plays a protective role against nitrosative and nutritional stresses in Schizosaccharomyces pombe.Molecular biology reports · 2010Article
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2 authors at 1 institution in 1 country.
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Abstract
Leishmania parasites primarily infect cells of macrophage lineage and can cause leishmaniasis in the skin, mucosal, and visceral organs, depending on both host- and parasite-derived factors. The protein disulfide isomerases (PDIs) are thiol-disulfide oxidoreductases that catalyze the formation, reduction, and isomerization of disulfide bonds of proteins in cells. Although four Leishmania PDI genes are functionally inferred from homology in the genome sequences, only two of them have been expressed as active proteins to date. The functional relationship among various PDI enzymes remains largely unclear. In this study, we expressed and partially characterized all four L. amazonensis PDIs encoding 52-, 47-, 40-, and 15-kDa proteins. Homology analysis showed that the sequence identity between L. amazonensis (New World) PDIs and their counterpart PDI sequences from L. major (Old World) ranged from 76% to 99%. Kinetic characterization indicated that while the 15-, 40-, and 47- kDa PDI proteins displayed both insulin isomerase and reductase activities, the 52-kDa protein had only isomerase activity with no detectable reductase activity. All four PDI proteins were recognized by sera from L. amazonensis-infected mice and were sensitive to inhibition by standard PDI inhibitors. This study describes the enzymatic activities of recombinant L. amazonensis PDIs and suggests a role for these proteins in parasite development.
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