caa a22 4500 378853112 CHVBK 20180305123328.0 cr unu---uuuuu 161128e20030820xx s 000 0 eng 10.1515/BC.2003.133 doi (NATIONALLICENCE)gruyter-10.1515/BC.2003.133 Trans-Sialidase-Like Sequences from Trypanosoma congolense Conserve Most of the Critical Active Site Residues Found in Other Trans-Sialidases [Elektronische Daten] [E. Tiralongo, I. Martensen, J. Grötzinger, J. Tiralongo, R. Schauer] 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. Copyright © 2003 by Walter de Gruyter GmbH & Co. KG Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence Tiralongo E. aut Martensen I. aut Grötzinger J. aut Tiralongo J. aut Schauer R. aut Biological Chemistry Walter de Gruyter 384/8(2003-08-20), 1203-1213 1431-6730 384:8<1203 2003 384 bchm https://doi.org/10.1515/BC.2003.133 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2003.133 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Tiralongo E. aut NATIONALLICENCE 700 1- Martensen I. aut NATIONALLICENCE 700 1- Grötzinger J. aut NATIONALLICENCE 700 1- Tiralongo J. aut NATIONALLICENCE 700 1- Schauer R. aut NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 384/8(2003-08-20), 1203-1213 1431-6730 384:8<1203 2003 384 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter