Trans-sialidase and sialidase activities discriminate between morphologically indistinguishable trypanosomatids.

@article{MedinaAcosta1994TranssialidaseAS,
  title={Trans-sialidase and sialidase activities discriminate between morphologically indistinguishable trypanosomatids.},
  author={Enrique Medina-Acosta and Ana Mar{\'i}a Franco and Ana Maria Jansen and Macarena Cerrudo Sampol and Nuno Neves and Lain Pontes-de-carvalho and G Grimaldi j{\'u}nior and Victor Nussenzweig},
  journal={European journal of biochemistry},
  year={1994},
  volume={225 1},
  pages={
          333-9
        }
}
The expression of trans-sialidase and sialidase activities in the kinetoplastid protozoa was explored as a potential marker to discriminate between the morphologically indistinguishable flagellates isolated from human, insects and vertebrate reservoir hosts. By virtue of the differences observed in the ratios of these enzyme activities, a collection of 52 species and strains comprising the major taxa of these parasites could be separated into four expression types. Type-I parasites express… Expand
Trypanosoma rangeli sialidase: kinetics of release and antigenic characterization.
TLDR
The epimastigote stage of Trypanosoma rangeli release a sialidase with a high sialic acid hydrolysis capacity, which is demonstrated to be an active process that is reduced at low temperatures and in the presence of sodium azide, suggesting a self-regulating mechanism and a biological role for the secreted T. rangelingi sialdase. Expand
The Chemistry and Biology of Trypanosomal trans‐Sialidases: Virulence Factors in Chagas Disease and Sleeping Sickness
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Trans‐Sialidase activity with varying linkage specificity has also been found in a few bacteria species and in human serum, and is of increasing practical importance for the chemo‐enzymatic synthesis of sialylated glycans. Expand
Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi.
  • A. Frasch
  • Biology, Medicine
  • Parasitology today
  • 2000
TLDR
The structure and possible function of the proteins making up these families of trypanosomes and cruzi are reviewed, with a focus on the trans-sialidase-like proteins. Expand
Directed mutagenesis of the Trypanosoma cruzi trans-sialidase enzyme identifies two domains involved in its sialyltransferase activity.
Of the increasing number of sialidases found to be made by microorganisms, the trypanosome trans-sialidase is unique in its added ability to efficiently carry out a sialyltransferase reaction usingExpand
Insights into the Activity and Specificity of Trypanosoma cruzi trans-Sialidase from Molecular Dynamics Simulations
TLDR
Computational simulations of TcTS following its sialylation by the substrate suggest that protein flexibility has a role in the transferase/sialidase activity of T cTS, and have the potential to aid in the design of anti-Chagas inhibitors effective against this neglected tropical disease. Expand
Structural basis of sialyltransferase activity in trypanosomal sialidases.
TLDR
The crystal structure of the closely related Trypanosoma rangeli sialidase and its complex with inhibitor is reported, illustrating how a glycosidase scaffold can achieve efficient glycosyltransferase activity and provide a framework for structure-based drug design. Expand
Structural basis of sialyltransferase activity in trypanosomal sialidases
TLDR
The crystal structure of the closely related Trypanosoma rangeli sialidase and its complex with inhibitor is reported, illustrating how a glycosidase scaffold can achieve efficient glycosyltransferase activity and provide a framework for structure‐based drug design. Expand
NMR spectroscopic and molecular modeling investigations of the trans-sialidase from Trypanosoma cruzi.
TLDR
It is demonstrated here that NMR spectroscopy is a powerful tool to monitor the trans-sialidase enzyme reaction for a variety of donor and acceptor molecules and that lactose in the absence of other coligands does not bind to the TcTS active site or other binding domains. Expand
Use of proteolytic enzymes as an additional tool for trypanosomatid identification
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Findings strongly suggest that the association of cellular and secretory proteinase pattern could represent a useful marker to help trypanosomatid identification. Expand
Transformation of monomorphic Trypanosoma brucei bloodstream form trypomastigotes into procyclic forms at 37 degrees C by removing glucose from the culture medium.
TLDR
It is shown that strain 427 monomorphic bloodstream forms of Trypanosoma brucei grown in axenic culture at 37 degrees C can be transformed to procyclic forms by simply replacing the glucose carbon source in the culture medium with glycerol. Expand
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The presence of a trans-sialidase on the surface of Trypanosoma brucei culture-derived procyclic trypomastigotes is reported, and it appears that the only sialylated surface molecule is procyclin. Expand
Structural and functional properties of Trypanosoma trans-sialidase.
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Several lines of evidence suggest that trans-sialidase and sialic acid acceptors on the surface of T. cruzi participate in host-parasite interactions and mediate the initial stages of the trypanosomes' invasion of host cells. Expand
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It is shown that Endotrypanum promastigotes possess sialid enzyme and trans-sialidase activities, which are absent from Leishmania, and which are not closely related to the previously described trypanosomal sialIDase/trans-sIALidase enzyme. Expand
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Although parasite sialic acid promotes C3b cleavage into iC3b, this mechanism alone does not account for the robust resistance of these parasites to complement lysis, and a novel fluorescence-based, trypomastigote lysis assay is used to evaluate the role of sIALic acid on the parasite's plasma membrane in providing protection against the complement cascade. Expand
Trypanosoma rangeli sialidase lacks trans-sialidase activity.
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Extracts and tissue culture supernatants of axenic forms of T. rangeli and the T. cruzi enzymes differ antigenically and in their pH optimum for hydrolase activity, and these enzymes contain a sialidase that hydrolyzes sialyl(alpha 2-3)lactose, and much less efficiently sialic acid, but not poly( alpha 2-8)N-acetylneuraminic acid. Expand
Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes
TLDR
It is concluded that a single enzyme can catalyze the transfer or the hydrolysis of macromolecular-bound sialic acid and the predominant direction of the reaction will depend on the availability of appropriate oligosaccharide acceptors of sIALic acid. Expand
A novel cell surface trans-sialidase of trypanosoma cruzi generates a stage-specific epitope required for invasion of mammalian cells
TLDR
Monoclonal antibodies that recognize sialic acid residues of SSP-3 inhibit attachment of trypomastigotes to host cells, suggesting that the unusual trans-sialidase provides Ssp-3 with structural features required for target cell recognition. Expand
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It has been proposed that sialylation of the parasite surface catalyzed by trans‐sialidase is necessary for successful invasion of the host cell, but the evidence available is still indirect, so another function could be a protection from lysis by the alternative pathway of complement while the parasite is circulating in the acute phase of the disease. Expand
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TLDR
The expression of trans-sialidase and the acquisition of sialic acid by T. cruzi may be relevant to the interaction of the parasite with the host, and consequently may influence the pathobiology of Chagas disease. Expand
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