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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : The EMBO journal

Structural basis of sialyltransferase activity in trypanosomal sialidases

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The EMBO journal - 01 Jan 2000

Buschiazzo A, Tavares GA, Campetella O, Spinelli S, Cremona ML, París G, Amaya MF, Frasch AC, Alzari PM

Link to Pubmed [PMID] – 10619840

EMBO J. 2000 Jan;19(1):16-24

The intracellular parasite Trypanosoma cruzi, the etiological agent of Chagas disease, sheds a developmentally regulated surface trans-sialidase, which is involved in key aspects of parasite-host cell interactions. Although it shares a common active site architecture with bacterial neuraminidases, the T.cruzi enzyme behaves as a highly efficient sialyltransferase. Here we report the crystal structure of the closely related Trypanosoma rangeli sialidase and its complex with inhibitor. The enzyme folds into two distinct domains: a catalytic beta-propeller fold tightly associated with a lectin-like domain. Comparison with the modeled structure of T.cruzi trans-sialidase and mutagenesis experiments allowed the identification of amino acid substitutions within the active site cleft that modulate sialyltransferase activity and suggest the presence of a distinct binding site for the acceptor carbohydrate. The structures of the Trypanosoma enzymes illustrate how a glycosidase scaffold can achieve efficient glycosyltransferase activity and provide a framework for structure-based drug design.

http://www.ncbi.nlm.nih.gov/pubmed/10619840