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Endothelial cell signalling induced by trans-sialidase from Trypanosoma cruzi.
- Source :
-
Cellular microbiology [Cell Microbiol] 2008 Jan; Vol. 10 (1), pp. 88-99. Date of Electronic Publication: 2007 Aug 02. - Publication Year :
- 2008
-
Abstract
- The 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 infection.
- Subjects :
- Amino Acid Substitution genetics
Animals
Apoptosis immunology
Cell Adhesion Molecules biosynthesis
Cell Line
Glycoproteins genetics
Glycoproteins immunology
Humans
Mutant Proteins genetics
Mutant Proteins immunology
Mutant Proteins metabolism
Mutation, Missense
N-Acetylneuraminic Acid metabolism
NF-kappa B metabolism
Neuraminidase genetics
Neuraminidase immunology
Point Mutation
Protein Binding
Protozoan Proteins genetics
Protozoan Proteins immunology
Recombinant Proteins genetics
Recombinant Proteins immunology
Recombinant Proteins metabolism
Trypanosoma cruzi genetics
Endothelial Cells parasitology
Glycoproteins metabolism
Neuraminidase metabolism
Protozoan Proteins metabolism
Trypanosoma cruzi enzymology
Trypanosoma cruzi physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1462-5822
- Volume :
- 10
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Cellular microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 17672865
- Full Text :
- https://doi.org/10.1111/j.1462-5822.2007.01017.x