The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis (Q27639917)

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author name string

María F Amaya

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María L Cremona

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Alberto C Frasch

Heterologous expression of Trypanosoma cruzi trans-sialidase in Leishmania major enhances virulence

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language of work or name

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October 2002

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published in

Molecular Cell

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volume

10

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issue

4

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page(s)

757-68

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cites work

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Trypanosoma rangeli sialidase: cloning, expression and similarity to T. cruzi trans-sialidase

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Structural basis of sialyltransferase activity in trypanosomal sialidases

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Probing the sialic acid binding site of the hemagglutinin-neuraminidase of Newcastle disease virus: identification of key amino acids involved in cell binding, catalysis, and fusion.

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Immunization with a plasmid DNA containing the gene of trans-sialidase reduces Trypanosoma cruzi infection in mice

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A single tyrosine differentiates active and inactive Trypanosoma cruzi trans-sialidases.

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Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain

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Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase

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Siglecs, sialic acids and innate immunity

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A simple purification of procyclic acidic repetitive protein and demonstration of a sialylated glycosyl-phosphatidylinositol membrane anchor.

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Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi

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Regulation of cell adhesion by polysialic acid. Effects on cadherin, immunoglobulin cell adhesion molecule, and integrin function and independence from neural cell adhesion molecule binding or signaling activity

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Improved methods for building protein models in electron density maps and the location of errors in these models

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STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS

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Selectins: interpreters of cell-specific carbohydrate information during inflammation

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Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI

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The 1.8 A structures of leech intramolecular trans-sialidase complexes: evidence of its enzymatic mechanism

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The trans-sialidase from the african trypanosome Trypanosoma brucei

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Thymocyte depletion in Trypanosoma cruzi infection is mediated by trans-sialidase-induced apoptosis on nurse cells complex

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Probing molecular function of trypanosomal sialidases: single point mutations can change substrate specificity and increase hydrolytic activity

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Comparison of antibody and protective immune responses against Trypanosoma cruzi infection elicited by immunization with a parasite antigen delivered as naked DNA or recombinant protein

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Sialic acids as important molecules in the regulation of the immune system: pathophysiological implications of sialidases in immunity

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Characterization of a novel trans-sialidase of Trypanosoma brucei procyclic trypomastigotes and identification of procyclin as the main sialic acid acceptor

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Incorporation of sialic acid into Trypanosoma cruzi macromolecules. A proposal for a new metabolic route

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Temperature differences for trans-glycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi trans-sialidase

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The Occurrence ofN-Acetyl- andN-Glycoloylneuraminic Acid inTrypanosoma cruzi

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A novel cell surface trans-sialidase of trypanosoma cruzi generates a stage-specific epitope required for invasion of mammalian cells

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Structural and functional properties of Trypanosoma trans-sialidase

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Directed mutagenesis of the Trypanosoma cruzi trans-sialidase enzyme identifies two domains involved in its sialyltransferase activity

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Sialidases: structures, biological significance and therapeutic potential

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Trans-sialidase from Trypanosoma cruzi catalyzes sialoside hydrolysis with retention of configuration

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Substrate specificity of the Trypanosoma cruzi trans-sialidase

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Sialic acids as ligands in recognition phenomena.

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Fab' fragments of a mAb to a member of family 2 of trans-sialidases of Trypanosoma cruzi block trypanosome invasion of host cells and neutralize infection by passive immunization

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