Trans-Sialidase-Like Sequences from Trypanosoma congolense Conserve Most of the Critical Active Site Residues Found in Other Trans-Sialidases
-
E. Tiralongo
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.
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
Articles in the same Issue
- Molecular and Functional Interdependence of the Urokinase-Type Plasminogen Activator System with Integrins
- Differential Haemoglobin Gene Expression in the Crustacean Daphnia magna Exposed to Different Oxygen Partial Pressures
- Cloning and Characterization of the Promoter Region of the Mouse Frizzled-Related Protein 4 Gene
- The Bloom's Syndrome Helicase Interacts Directly with the Human DNA Mismatch Repair Protein hMSH6
- Assignment of Disulphide Bridges in Par j 2.0101, a Major Allergen of Parietaria judaica Pollen
- Determination of the NMR Structure of Gln25-Ribonuclease T1
- The Molecular Chaperone, α-Crystallin, Protects against Loss of Antigenicity and Activity of Esterase Caused by Sugars, Sugar Phosphate and a Steroid
- The Activator-Binding Site of Onchocerca volvulus S-Adenosylmethionine Decarboxylase, a Potential Drug Target
- Trans-Sialidase-Like Sequences from Trypanosoma congolense Conserve Most of the Critical Active Site Residues Found in Other Trans-Sialidases
- EGFR and FGFR Signaling through FRS2 Is Subject to Negative Feedback Control by ERK1/2
- The N’-Terminal Domain of Glyceraldehyde-3-Phosphate Dehydrogenase of the Apicomplexan Plasmodium falciparum Mediates GTPase Rab2-Dependent Recruitment to Membranes
- Novel Cell-Permeable Acyloxymethylketone Inhibitors of Asparaginyl Endopeptidase
- Clinical Relevance of Matrix Metalloproteinase-13 Determined with a New Highly Specific and Sensitive ELISA in Ascitic Fluid of Advanced Ovarian Carcinoma Patients
Articles in the same Issue
- Molecular and Functional Interdependence of the Urokinase-Type Plasminogen Activator System with Integrins
- Differential Haemoglobin Gene Expression in the Crustacean Daphnia magna Exposed to Different Oxygen Partial Pressures
- Cloning and Characterization of the Promoter Region of the Mouse Frizzled-Related Protein 4 Gene
- The Bloom's Syndrome Helicase Interacts Directly with the Human DNA Mismatch Repair Protein hMSH6
- Assignment of Disulphide Bridges in Par j 2.0101, a Major Allergen of Parietaria judaica Pollen
- Determination of the NMR Structure of Gln25-Ribonuclease T1
- The Molecular Chaperone, α-Crystallin, Protects against Loss of Antigenicity and Activity of Esterase Caused by Sugars, Sugar Phosphate and a Steroid
- The Activator-Binding Site of Onchocerca volvulus S-Adenosylmethionine Decarboxylase, a Potential Drug Target
- Trans-Sialidase-Like Sequences from Trypanosoma congolense Conserve Most of the Critical Active Site Residues Found in Other Trans-Sialidases
- EGFR and FGFR Signaling through FRS2 Is Subject to Negative Feedback Control by ERK1/2
- The N’-Terminal Domain of Glyceraldehyde-3-Phosphate Dehydrogenase of the Apicomplexan Plasmodium falciparum Mediates GTPase Rab2-Dependent Recruitment to Membranes
- Novel Cell-Permeable Acyloxymethylketone Inhibitors of Asparaginyl Endopeptidase
- Clinical Relevance of Matrix Metalloproteinase-13 Determined with a New Highly Specific and Sensitive ELISA in Ascitic Fluid of Advanced Ovarian Carcinoma Patients