Trans-sialidases

F. Vandekerckhove, S. Schenkman, L. Pontes de Carvalho, S. Tomlinson, M. Kiso, M. Yoshida, A. Hasegawa, and V. Nussenzweig, Substrate specificity of the Trypanosoma cruzi trans-sialidase, Glycobiology 2 541 (1992). 

Lewisx (SLex, 26).76 The enzyme trans-sialidase transfers sialic acid to 0-3 of the galactose unit.77 Thus, the 3 -deoxy derivatives of the disaccharides would be useful for studying biological recognition processes. 

A. C. C. Frash, Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi, Parasitol. Today, 16 (2000) 282-286. 

Another multifunctional bacterial enzyme that has been reported recently is Pasteurella multocida sialyltransferase (PmSTl or tPm0188Ph) (67, 68). It has four different activities, including an a2,3SiaT, a2,6SiaT, a2,3-sialidase, and trans-sialidase activities. PmSTl is a highly active sialyltransferase with broad donor and acceptor substrate specificity therefore it is a powerful tool... 

Lee S, Kim B. trans-Sialidase catalyzed sialylation of P-galacto- 29. syldisaccharide with an introduction of P-galactosidase. Enzyme Microb. Technol. 2001 28 161-167. 

T. cruzi small mucin-like gene family TcTS, Trypanosoma cruzi trans-sialidase THF, tetrahydrofuran TMSOTf, trimethylsilyl trifluoromethanesulfonate TRR, Thr-rich region TSSA, trypomastigote small surface antigen UDP, uridine diphosphate VSG, variant surface glycoprotein. 

The gp85 glycoproteins are included in the trans-sialidase superfamily, although some members are enzymatically inactive.36 The Tc-85 glycoprotein is specific for the trypomastigote forms37 and is anchored by a GPI with l-<9-hexadecylglycerol.38,39... 

SCHEME 11. Mechanism of action of T. cruzi trans-sialidase (Ref. 149). 

SCHEME 12. Selective sialylation of 2,3-di-0-(/i-D-galactopyranosyl)-i)-galactose catalyzed by Trypanosoma cruzi trans-sialidase. 

SCHEME 14. Sialylation of a-D-Galp-(l—>6)-/ -D-Galp-OMe by the trans-sialidase of T. cruzi. 

Scheme 16. Trans-sialylation of lactose and modified derivatives employing trans-sialidase.

SCHEME 17. Trans-sialylations of /JGal-(l—>3)-Gal-R derivatives employing trans-sialidase. 

SCHEME 20. /Y-(il ycoIyIncuraminic acid transfer by Trypanosoma cruzi trans-sialidase from donors 107 and 108 to lactitol. 

T. cruzi is an exceptional system for glycobiology studies and the most unusual structures have been identified. From the medical point of view, the mucin and trans-sialidase families, which constitute 15% of all predicted genes, are involved in the infection process. 

M. J. M. Alves and W. Colli, Role of the gp85/trans-sialidase superfamily of glycoproteins in the interaction of Trypanosoma cruzi with host structures, in B. A. Burleigh and D. Soldati-Favre, (Eds.), Molecular Mechanisms of Parasite Invasion, 47 pp. 58-96. 

S. Schenkman, M. A. J. Ferguson, N. Heise, M. L. de Almeida, R. A. Mortara, andN. Yoshida, Mucinlike glycoproteins linked to the membrane by glycosylphosphatidylinositol anchor are the major acceptors of sialic acid in a reaction catalyzed by trans-sialidase in metacyclic forms of Trypanosoma cruzi, Mol. Biochem. Parasitol., 59 (1993) 293-303. 

C. A. Buscaglia, V. A. Campo, A. C. C. Frasch, and J. M. Di Noia, Trypanosoma cruzi surface mucins host-dependent coat diversity, Nat. Rev. Microbiol, 4 (2006) 229-236 A. C. C. Frasch, Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi, Parasitol. Today, 16 (2000) 282-286. 

S. Schenkman and M. Jiang, G.W. Hart and V. Nussenzweig. A novel cell surface trans-sialidase of Trypanosoma cruzi generates a stage-specific epitope required for invasion of mammalian cells, Cell, 65 (1991) 1117-1125. 

M. Chuenkova and M. E. S. Pereira, Trypanosoma cruzi trans-sialidase enhancement of virulence in a murine model of Chagas disease, J. Exp. Med., 181 (1995) 1693-1703. 

S. Schenkman, D. Eichinger, M. E. S. Pereira, and V. Nussenzweig, Structural and functional properties of Trypanosoma trans-sialidase, Annu. Rev. Microbiol., 48 (1994) 499-523. 

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