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Abstract:

Trypanosoma cruzi, the etiologic agent of Chagas disease, is covered by a dense glycocalix mainly composed by glycoproteins called mucins which are also the acceptors of sialic acid in a reaction catalyzed by a trans-sialidase (TcTS). Sialylation of trypomastigote mucins protects the parasite from lysis by the anti α-Galp antibodies from serum. The TcTS is essential for the infection process since T. cruzi is unable to biosynthesize sialic acid. The enzyme specifically transfers it from a terminal β-D-Galp unit in the host glycoconjugate to terminal β-D-Galp units in the parasite mucins to construct the D-NeuNAc(α2→3)β-D-Galp motif. On the other hand, although galactose is the most abundant sugar in mucins of both, the infective trypomastigotes and the insect stage epimastigotes, α-D-Galp is only present in the infective stage whereas β-D-Galf is characteristic of the epimastigote stage of the less virulent strains. Neither α-D-Galp nor D-Galf is acceptor of sialic acid. In the mucins, some of the oligosaccharides are branched with terminal β-D-Galp units to be able to accept sialic acid in the TcTS reaction. Based on previous reports showing that anti α-Galp antibodies only partially colocalize with sialic acid, we have undertaken the synthesis of the trisaccharide α-D-Galp(1→3)-[β-D-Galp(1→6)]-D-Galp, the smallest structure containing both, the antigenic D-Galp(α1→3)-D-Galp unit and the sialic acid-acceptor β-D-Galp unit. The trisaccharide was obtained as the 6-aminohexyl glycoside to facilitate further conjugation for biochemical studies. The synthetic approach involved the α-galactosylation at O-4 of a suitable precursor of the reducing end, followed by β-galactosylation at O-6 of the same precursor and introduction of the 6-aminohexyl aglycone. The fully deprotected trisaccharide was successfully sialylated by TcTS using either 3′-sialyllactose or fetuin as donors. The product, 6-aminohexyl α-D-NeuNAc(2→3)-β-D-Galp(1→6)-[α-D-Galp(1→3)]-β-D-Galp, was purified and characterized. © 2017 Elsevier Ltd

Registro:

Documento: Artículo
Título:Synthesis of a model trisaccharide for studying the interplay between the anti α-Gal antibody and the trans-sialidase reactions in Trypanosoma cruzi
Autor:Giorgi, M.E.; Lopez, R.; Agusti, R.; Marino, C.; de Lederkremer, R.M.
Filiación:Universidad de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas, Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR), Facultad de Ciencias Exactas y Naturales, Departamento de Química Orgánica, Buenos Aires, Argentina
Palabras clave:Anti α-gal; Trans-sialidase; Trypanosoma cruzi; Carboxylic acids; Biochemical studies; Etiologic agents; Infection process; Reaction catalyzed; Synthetic approach; Trans-sialidases; Trypanosoma cruzi; Virulent strains; Antibodies; 6 aminohexyl glycoside; glycoside; sialidase; trisaccharide; unclassified drug; antibody; calcium binding protein; galactose-binding protein; glucose transporter; glycoprotein; periplasmic binding protein; sialidase; trans-sialidase; trisaccharide; Article; biochemical analysis; carbohydrate synthesis; conjugation; nonhuman; priority journal; sialylation; Trypanosoma cruzi; carbohydrate analysis; chemistry; immunology; metabolism; synthesis; Trypanosoma cruzi; Antibodies; Calcium-Binding Proteins; Carbohydrate Sequence; Chemistry Techniques, Synthetic; Glycoproteins; Monosaccharide Transport Proteins; Neuraminidase; Periplasmic Binding Proteins; Trisaccharides; Trypanosoma cruzi
Año:2017
Volumen:450
Página de inicio:30
Página de fin:37
DOI: http://dx.doi.org/10.1016/j.carres.2017.08.007
Título revista:Carbohydrate Research
Título revista abreviado:Carbohydr. Res.
ISSN:00086215
CODEN:CRBRA
CAS:sialidase, 9001-67-6; Antibodies; Calcium-Binding Proteins; galactose-binding protein; Glycoproteins; Monosaccharide Transport Proteins; Neuraminidase; Periplasmic Binding Proteins; trans-sialidase; Trisaccharides
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00086215_v450_n_p30_Giorgi

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Citas:

---------- APA ----------
Giorgi, M.E., Lopez, R., Agusti, R., Marino, C. & de Lederkremer, R.M. (2017) . Synthesis of a model trisaccharide for studying the interplay between the anti α-Gal antibody and the trans-sialidase reactions in Trypanosoma cruzi. Carbohydrate Research, 450, 30-37.
http://dx.doi.org/10.1016/j.carres.2017.08.007
---------- CHICAGO ----------
Giorgi, M.E., Lopez, R., Agusti, R., Marino, C., de Lederkremer, R.M. "Synthesis of a model trisaccharide for studying the interplay between the anti α-Gal antibody and the trans-sialidase reactions in Trypanosoma cruzi" . Carbohydrate Research 450 (2017) : 30-37.
http://dx.doi.org/10.1016/j.carres.2017.08.007
---------- MLA ----------
Giorgi, M.E., Lopez, R., Agusti, R., Marino, C., de Lederkremer, R.M. "Synthesis of a model trisaccharide for studying the interplay between the anti α-Gal antibody and the trans-sialidase reactions in Trypanosoma cruzi" . Carbohydrate Research, vol. 450, 2017, pp. 30-37.
http://dx.doi.org/10.1016/j.carres.2017.08.007
---------- VANCOUVER ----------
Giorgi, M.E., Lopez, R., Agusti, R., Marino, C., de Lederkremer, R.M. Synthesis of a model trisaccharide for studying the interplay between the anti α-Gal antibody and the trans-sialidase reactions in Trypanosoma cruzi. Carbohydr. Res. 2017;450:30-37.
http://dx.doi.org/10.1016/j.carres.2017.08.007