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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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IMPACT FACTOR 2015: 2.710
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1437-4315
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Volume 384, Issue 8 (Aug 2003)

Issues

Trans-Sialidase-Like Sequences from Trypanosoma congolense Conserve Most of the Critical Active Site Residues Found in Other Trans-Sialidases

E. Tiralongo / I. Martensen / J. Grötzinger / J. Tiralongo / R. Schauer
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2003.133

Abstract

Trypanosoma congolense is the agent of Nagana, the trypanosomiasis in African ruminants. Trypanosomes express an enzyme called trans-sialidase, which is believed to play an important role in maintaining pathogenicity of the parasites. Thus far, only two complete trans-sialidase sequences have been characterised, one from the American trypanosome T. cruzi and one from the African trypanosome T. brucei brucei. Although the crystal structure of T. cruzi trans-sialidase has recently been published [Buschiazzo et al., Mol. Cell 10 (2002), pp. 757 768], a number of questions concerning the exact transfer mechanism remain unanswered. The availability of further trans-sialidase sequences will ensure a better understanding of how transfer activity can be achieved and will provide the opportunity to develop highly specific, structure-based trans-sialidase inhibitors. Utilising a PCR-based approach two different trans-sialidase gene copies from T. congolense were identified, which share only 50% identity with each other, but show significant similarity with known viral, bacterial and trypanosomal sialidases and trans-sialidases. In both partial sequences most of the critical active site residues common to other trypanosomal sialidases and trans-sialidases are conserved. This is further illustrated by modelling the active site of the longer of the two partial gene sequences.

About the article

Published Online: 2005-06-01

Published in Print: 2003-08-20


Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2003.133. Export Citation

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