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Journal ArticleDOI

A sialidase activity in the midgut of the insect Triatoma infestans is responsible for the low levels of sialic acid in Trypanosoma cruzi growing in the insect vector

TLDR
It is shown that parasite forms growing in the vector Triatoma infestans express trans-sialidase in the hindgut portions of the insect, and this novel activity could have a nutritional role in the gut of haematophagous insects and indicates that acquisition of sialic acid is not required for parasite development in the Gut of T.infestans.
Abstract
Trypanosoma cruzi expresses a unique trans-sialidase that is responsible for the transfer of sialic acid from host glycoproteins and glycolipids to mucin-like glycoprotein acceptors on the parasite surface. The enzyme and the sialic acid acceptors are present in the mammalian forms of the parasite and in the parasite forms that grow in axenic cultures, which correspond to the developmental stages found in the insect vectors. Here we show that parasite forms growing in the vector Triatoma infestans express trans-sialidase in the hindgut portions of the insect. However, the sialic acid acceptors are poorly sialylated due to the low concentration of sialic acid donors in the gut lumen of T.infestans, which feeds exclusively on blood that is rich in sialic acid donors. These low levels of sialic acid donors are due to a novel sialidase activity present mainly in the anterior midgut with high specificity for alpha-2,3-sialyllactose, but not for alpha-2,6-sialyllactose. The activity is present in starved insects or insects fed with culture medium, indicating that it did not originate from the blood meal. Enzyme activity does not decrease in insects fed with antibiotics, is present in the salivary glands, and the few bacteria isolated from the gut and faeces of T.infestans did not display sialidase activity, indicating that the enzyme is not derived from a commensal organism. This novel activity could have a nutritional role in the gut of haematophagous insects and indicates that acquisition of sialic acid is not required for parasite development in the gut of T.infestans.

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Citations
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Journal ArticleDOI

The mucin-like glycoprotein super-family of Trypanosoma cruzi: structure and biological roles.

TL;DR: The T. cruzi mucins (TcMUC), a group of highly glycosylated GPI-anchored proteins rich in Thr, Ser, and Pro residues, are expressed in high copy numbers in both insect and mammalian stages of the parasite.
Journal ArticleDOI

Comparative enzymology, biochemistry and pathophysiology of human exo-α-sialidases (neuraminidases)

TL;DR: This review summarizes the current research on human exo -α-sialidase (sIALidase, neuraminidase).
Journal ArticleDOI

Trans-sialidase and mucins of Trypanosoma cruzi: an important interplay for the parasite.

TL;DR: The characteristics of the interplay between the trans-sialidase and the mucins of T. cruzi are focused on and the known carbohydrate structures of the muc Ins are summarized, which are characteristic of each differentiation stage.
Journal ArticleDOI

New Insights on the Sialidase Protein Family Revealed by a Phylogenetic Analysis in Metazoa

TL;DR: The evolution of the sialidase protein family is reconstructed from the ancestral sIALidase NEU1 and a new form of the enzyme is identified, representing an intermediate step in the evolution leading to the modern NEU3, NEU4 and NEU2.
References
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Journal ArticleDOI

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

TL;DR: 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.
Journal ArticleDOI

Stage-specific surface antigens expressed during the morphogenesis of vertebrate forms of Trypanosoma cruzi.

TL;DR: It is concluded that trypomastigotes are programmed to develop into amastigote whether or not they enter cells, and that the differentiation can occur in the blood of the vertebrate host.
Journal ArticleDOI

Lytic anti-α-galactosyl antibodies from patients with chronic Chagas' disease recognize novel O-linked oligosaccharides on mucin-like glycosyl-phosphatidylinositol-anchored glycoproteins of Trypanosoma cruzi

TL;DR: These novel T. cruzi O-linked oligosaccharides are highly immunogenic under the conditions of natural infection and are the targets for lytic Ch anti-Gal.
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