Trypanosoma cruzi trans-sialidase

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). 

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. 

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

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

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. 

O. E. Campetella, A. K. Uttaro, A. J. Parodi, and A. C. C. Frasch, A recombinant Trypanosoma cruzi trans-sialidase lacking the amino acid repeats retains the enzymatic activity, Mol. Biochem. Parasitol., 64 (1994) 337-340. 

M. F. Amaya, A. G. Watts, I. Damager, A. Wehenkel, T. Nguyen, A. Buschiazzo, G. Paris, A. C. C. Frasch, S. G. Withers, and P. M. Alzari, Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase, Structure, 12 (2004) 775-784. 

S. Buchini, A. Buschiazzo, and S. G. Withers, A new generation of specific Trypanosoma cruzi trans-sialidase inhibitors, Angew. Chem. Ini. Ed., 47 (2008) 2700-2703. 

M. L. Cremona, D. O. Sanchez, A. C. C. Frasch, and O. Campetella, A single tyrosine differentiates active and inactive Trypanosoma cruzi trans-sialidases, Gene, 160 (1995) 123-128. 

R. Agusti, V. M. Mendoza, C. Gallo-Rodriguez, and R. M. de Lederkremer, Selective sialylation of 2,3-di-0-( j -D-galactopyranosyl)-D-galactose catalyzed by Trypanosoma cruzi trans-sialidase, Tetrahedron Asymmetry, 16 (2005) 541-551. 

M. Ribeirao, V. L. Pereira-Chioccola, D. Eichinger, M. M. Rodrigues, and S. Schenkman, Temperature differences for frans-glycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi trans-sialidase, Glycobiology, 1 (1997) 1237-1246. 

J. A. Harrison, K. P. Kartha, W. B. Turnbull, S. L. Scheuerl, J. H. Naismith, S. Schenkman, and R. A. Field, Hydrolase and sialyltransferase activities of trypanosoma cruzi trans-sialidase towards NeuAc-alpha-2,3-gal-Gal-beta-0-PNP, Bioorg. Med. Chem. Lett., 11 (2001) 141-144. 

K. B. Lee and Y. C. Lee, Transfer of modified sialic acids by Trypanosoma cruzi trans-sialidase for attachment of functional groups to oligosaccharide, Anal. Biochem., 216 (1994) 358—364. 

R. Agusti, G. Paris, L. Ratier, A. C. C. Frasch, and R. M. de Lederkremer, Lactose derivatives are inhibitors of Trypanosoma cruzi trans-sialidase activity toward conventional substrates in vitro and in vivo, Glycobiology, 14 (2004) 659-670. 

L. Ratier, M. Unutia, G. Paris, L. Zarebski, A. C. Fiaseh, and F. A. Goldbaum, Relevance of die diversity among members of die Trypanosoma cruzi trans-sialidase femily analyzed widi eamehds single-domain antibodies, PLoS ONE, 3 (2008) e3524. 

W. Gao, H. H. Words, and M. A. Pereira, The Trypanosoma cruzi trans-sialidase is a T cell-independent B cell mitogen and an inducer of non-speeifie Ig secretion, Int. Immunol, 14 (2002) 299-308. 

Schenkman, S, Eichinger, D, Pereira, ME A. and Nussenzweig, V (1994) Structural and functional properties of Trypanosoma cruzi trans-sialidase. Armu Rev Microbiol 48 499-523. 

Buschiazzo, A., Cremona, M. L., Campetella, O., Frasch, A.C.C., and Sanchez, D. O., 1993, Sequence of a Trypanosoma ranged gene closely related to Trypanosoma cruzi trans-sialidase. Mol. Biochem. Parasitol. 62 115-116. 

Schenkman, S., and Eichinger, D., 1993, Trypanosoma cruzi trans-sialidase and cell invasion, Parasitol. Today 9 218-222. 

Schenkman, S., de Varvalho, L. P., and Nussenzweig, V., 1992, Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzyme, J. Exp. Med. 175 567-575. 

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