Characterization of a Key Enzyme in Trypanosoma cruzi
Author Information
Author(s): Cadavid-Restrepo Gloria, Gastardelo Thiago S, Faudry Eric, de Almeida Hugo, Bastos Izabela MD, Negreiros Raquel S, Lima Meire M, Assumpção Teresa C, Almeida Keyla C, Ragno Michel, Ebel Christine, Ribeiro Bergmann M, Felix Carlos R, Santana Jaime M
Primary Institution: Department of Cell Biology, The University of Brasília, Brasília, Brazil
Hypothesis
The study aims to identify and characterize the major leucyl aminopeptidase in Trypanosoma cruzi.
Conclusion
LAPTc is a 330-kDa homohexameric metalloaminopeptidase that plays a crucial role in the nutritional supply of T. cruzi.
Supporting Evidence
- LAPTc was identified as a 330-kDa homohexameric protein.
- The enzyme is expressed by all forms of T. cruzi.
- LAPTc retains its oligomeric structure even after losing enzymatic activity.
Takeaway
Researchers found an important enzyme in a parasite that causes Chagas disease, which helps the parasite get nutrients it can't make on its own.
Methodology
The enzyme was isolated using a two-step chromatographic procedure and characterized through molecular and enzymatic analysis.
Limitations
The study does not explore the enzyme's activity in all T. cruzi forms or under all conditions.
Digital Object Identifier (DOI)
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