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Characterization and role of the 3-methylglutaconyl coenzyme A hidratase in Trypanosoma brucei. | LitMetric

Characterization and role of the 3-methylglutaconyl coenzyme A hidratase in Trypanosoma brucei.

Mol Biochem Parasitol

Departamento de Microbiologia, Imunologia e Parasitologia, Universidade Federal de São Paulo, São Paulo, SP, Brazil. Electronic address:

Published: June 2017

AI Article Synopsis

  • Trypanosoma brucei is a protozoan parasite responsible for African Trypanosomiasis that relies on nutrients from hosts and is not fully understood in its amino acid breakdown.
  • The study focuses on the enzyme 3-methylglutaconyl-CoA hydratase (3-MGCoA-H), involved in leucine catabolism, which impacts the parasite's growth in the presence of leucine.
  • Findings indicate that while the enzyme's depletion doesn’t greatly affect parasite proliferation, excess leucine causes growth issues that can be remedied by mevalonate, highlighting its role in steroid biosynthesis necessary for T. brucei survival.

Article Abstract

Trypanosoma brucei, the agent of African Trypanosomiasis, is a flagellated protozoan parasite that develops in tsetse flies and in the blood of various mammals. The parasite acquires nutrients such as sugars, lipids and amino acids from their hosts. Amino acids are used to generate energy and for protein and lipid synthesis. However, it is still unknown how T. brucei catabolizes most of the acquired amino acids. Here we explored the role of an enzyme of the leucine catabolism, the 3-methylglutaconyl-Coenzyme A hydratase (3-MGCoA-H). It catalyzes the hydration of 3-methylglutaconyl-Coenzyme A (3-MGCoA) into 3-hydroxymethylglutaryl-Coenzyme A (3-HMGCoA). We found that 3-MGCoA-H localizes in the mitochondrial matrix and is expressed in both insect and mammalian bloodstream forms of the parasite. The depletion of 3-MGCoA-H by RNA interference affected minimally the proliferation of both forms. However, an excess of leucine in the culture medium caused growth defects in cells depleted of 3-MGCoA-H, which could be reestablished by mevalonate, a precursor of isoprenoids and steroids. Indeed, procyclics depleted of the 3-MGCoA-H presented reduced levels of synthesized steroids relative to cholesterol that is scavenged by the parasite, and these levels were also reestablished by mevalonate. These results suggest that accumulation of leucine catabolites could affect the level of mevalonate and consequently inhibit the sterol biosynthesis, required for T. brucei growth.

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Source
http://dx.doi.org/10.1016/j.molbiopara.2017.03.007DOI Listing

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