Endothelial cell signalling induced by trans-sialidase from Trypanosoma cruzi
Authors:
- Wagner B. DiasWDWagner B. Dias
- Leonardo Freire-De-LimaLeonardo Freire-De-Lima
- Fabiana VieiraFVFabiana Vieira
- Murielle F. GirardMGMurielle F. Girard
- Bernard BouteilleBBBernard Bouteille
- José O. PreviatoJPJosé O. Previato
- Lucia Mendonça-PreviatoLMLucia Mendonça-Previato
- Adriane R. TodeschiniATAdriane R. Todeschini
Open Access
- 2 August 2007
- journal article
- Published by Hindawi Limited in Cellular Microbiology
- Vol. 10 (1) , 88-99
Abstract
International audienceThe protozoan responsible for Chagas' disease, Trypanosoma cruzi, expresses on its surface an unusual trans-sialidase enzyme thought to play an important role in host-parasite interactions. Trans-sialidase is the product of a multigene family encoding both active and inactive proteins. We have demonstrated that despite lacking enzymatic activity due to a single mutation, Tyr342-His, inactive trans-sialidase displays sialic acid binding activity, with identical specificity to that of its active analogue. In this work we demonstrate that binding of a recombinant inactive trans-sialidase to molecules containing alpha2,3-linked sialic acid on endothelial cell surface triggers NF-kappaB activation, expression of adhesion molecules and upregulation of parasite entry into host cells. Furthermore, inactive recombinant trans-sialidase blocks endothelial cell apoptosis induced by growth factor deprivation. These results suggest that inactive members of the trans-sialidase family play a role in endothelial cell responses to T. cruzi infectionKeywords
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