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Trypanosoma cruzi Trans-sialidase: structural features and biological implications
Isadora A Oliveira1, Leonardo Freire-de-Lima, Luciana L Penha
1Laboratório de Glicobiologia Estrutural e Funcional, Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Avenida Carlos Chagas Filho, 373, Centro de Ciências da Saúde-Bloco D-3, 21941-902, Cidade Universitária, Rio de Janeiro, Brazil.
Sub-Cellular Biochemistry
|November 23, 2013
Summary
Trypanosoma cruzi trans-sialidase (TcTS) efficiently transfers sialic acid, independent of host sialyltransferases. Structural studies reveal TcTS
Area of Science:
- Biochemistry
- Parasitology
- Structural Biology
Background:
- Trypanosoma cruzi trans-sialidase (TcTS) is unique for incorporating sialic acid independently of host sialyltransferases.
- TcTS plays critical roles in parasite biology and the pathology of Chagas' disease.
Purpose of the Study:
- To review the diverse biological functions of TcTS.
- To summarize structural investigations elucidating TcTS mechanism.
Main Methods:
- Intermediate trapping with fluorosugars.
- Peptide mapping.
- X-ray crystallography, molecular modeling, and magnetic nuclear resonance (NMR) spectroscopy.
Main Results:
- Structural studies have provided a 3D understanding of TcTS.
- Evidence suggests TcTS possesses efficient sugar transfer activity, not just hydrolysis.
Conclusions:
- TcTS is a key enzyme in T. cruzi with significant implications for Chagas' disease.
- Ongoing structural research is uncovering the enzyme's sugar transfer mechanisms.
