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Catalase impairs Leishmania mexicana development and virulence
J. Sádlová, L. Podešvová, T. Bečvář, C. Bianchi, ES. Gerasimov, A. Saura, K. Glanzová, T. Leštinová, NS. Matveeva, Ľ. Chmelová, D. Mlacovská, T. Spitzová, B. Vojtková, P. Volf, V. Yurchenko, N. Kraeva
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
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- MeSH
- Virulence Factors genetics metabolism MeSH
- Catalase genetics metabolism MeSH
- Cells, Cultured MeSH
- Leishmania mexicana genetics growth & development pathogenicity MeSH
- Mice, Inbred BALB C MeSH
- Mice MeSH
- Protozoan Proteins genetics MeSH
- Psychodidae parasitology MeSH
- Life Cycle Stages genetics MeSH
- Teschovirus genetics MeSH
- Virulence MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Catalase is one of the most abundant enzymes on Earth. It decomposes hydrogen peroxide, thus protecting cells from dangerous reactive oxygen species. The catalase-encoding gene is conspicuously absent from the genome of most representatives of the family Trypanosomatidae. Here, we expressed this protein from the Leishmania mexicana Β-TUBULIN locus using a novel bicistronic expression system, which relies on the 2A peptide of Teschovirus A. We demonstrated that catalase-expressing parasites are severely compromised in their ability to develop in insects, to be transmitted and to infect mice, and to cause clinical manifestation in their mammalian host. Taken together, our data support the hypothesis that the presence of catalase is not compatible with the dixenous life cycle of Leishmania, resulting in loss of this gene from the genome during the evolution of these parasites.
Department of Parasitology Faculty of Science Charles University Prague Czech Republic
Faculty of Biology M 5 Lomonosov Moscow State University Moscow Russia
Life Science Research Centre Faculty of Science University of Ostrava Ostrava Czech Republic
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