T. A. Jones, J. Y. Zou, S. W. Cowan, M. Kjeldgaard, M. Belen-carrillo et al., Heterologous expression of Trymaps and the location of errors in these models, Acta Crystallogr. A, vol.47, pp.110-119, 1991.

, panosoma cruzi trans-sialidase in Leishmania major enhances virulence, Infect. Immun, vol.68, pp.2728-2734

D. E. Koshland and . Jr, Stereochemistry and the mechanism of enzymatic reactions, Biol. Rev, vol.28, pp.416-436, 1953.

P. Borst and S. Ulbert, Control of VSG gene expression sites, Mol. Biochem. Parasitol, vol.114, pp.17-27, 2001.

V. S. Lamzin and K. S. Wilson, Automated refinement of protein molecules, Acta Crystallogr. D, vol.49, pp.129-149, 1993.

A. T. Brü-nger, Free R value: a novel statistical quantity for assessing the accuracy of crystal structures, Nature, vol.355, pp.472-474, 1992.

R. A. Laskowski, M. W. Macarthur, D. S. Moss, J. M. Thornton, P. D. Adams et al., PROCHECK: a program to check the stereochemical quality Brü nger, J. Appl. Crystallogr, vol.26, pp.283-291, 1993.

R. W. Grosse-kunstleve, J. S. Jiang, J. Kuszewski, M. Nilges, and N. S. Pannu, Selectins: interpreters of cell-specific carbohysoftware suite for macromolecular structure determination. Acta drate information during inflammation, Crystallography & NMR system: a new Lasky, vol.258, pp.905-921, 1992.

K. L. Longenecker, S. M. Garrard, P. J. Sheffield, . Derewenda, C. A. Buscaglia et al., , 1999.

Z. S. , Protein crystallization by rational mutagenesis of surface Tandem amino acid repeats from Trypanosoma cruzi shed antigens residues: Lys to Ala mutations promote crystallization of RhoGDI. increase the half-life of proteins in blood, Acta Crystallogr. D, vol.93, pp.679-688, 2001.

A. Buschiazzo, O. Campetella, A. C. Frasch, Y. Trypano-luo, S. C. Li et al., The 1.8 Å structures soma rangeli sialidase: cloning, expression and similarity to T. cruzi of leech intramolecular trans-sialidase complexes: evidence of its trans-sialidase, J. Mol. Biol, vol.7, pp.323-332, 1997.
URL : https://hal.archives-ouvertes.fr/pasteur-00847149

A. Buschiazzo, G. A. Tavares, O. Campetella, S. Spinelli, . Cremona et al., , 1998.

M. L. Paris, G. Amaya, M. F. Frasch, A. C. , A. et al., The role of sialic acid in opsonin-dependent and opsonin-indepen-Structural basis of sialyltransferase activity in trypanosomal sialident adhesion of Listeria monocytogenes to murine peritoneal macdases, rophages. Infect. Immun, vol.19, pp.620-626, 2000.

G. The-ccp4-montagna, M. L. Cremona, G. Paris, M. F. Amaya, P. M. Alzari et al., The trans-sialidase from 760-763. the African trypanosome Trypanosoma brucei, CCP4 (Collaborative Computational Project 4), vol.50, pp.2941-2950, 1994.

H. Connaris, T. Takimoto, R. Russell, S. Crennell, I. Moustafa et al., Thymocyte depletion in Trypanosoma site of the hemagglutinin-neuraminidase of Newcastle disease virus: identification of key amino acids involved in cell binding, catalysis, cruzi infection is mediated by trans-sialidase-induced apoptosis on nurse cells complex, Proc. Natl. Acad. Sci. USA, vol.99, pp.1816-1824, 2002.

J. O. Previato, A. F. Andrade, M. C. Pessolani, and L. Mendonca-previato, Incorporation of sialic acid into Trypanosoma cruzi macromolecules. A proposal for a new metabolic route, Mol. Biochem. Parasitol, vol.16, pp.85-96, 1985.

M. Ribeirao, V. L. Pereira-chioccola, D. Eichinger, M. M. Rodrigues, and S. Schenkman, Temperature differences for transglycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi trans-sialidase, Glycobiology, vol.7, pp.1237-1246, 1997.

U. Rutishauser, Polysialic acid and the regulation of cell interactions, Curr. Opin. Struct. Biol, vol.8, pp.679-684, 1996.

U. Rutishauser and L. Landmesser, Polysialic acid in the vertebrate nervous system: a promoter of plasticity in cell-cell interactions, Trends Neurosci, vol.19, pp.422-427, 1996.

R. Schauer, Achievements and challengs of sialic acid research, Glycoconj. J, vol.17, pp.485-499, 2000.

R. Schauer, G. Reuter, H. Muhlpfordt, A. F. Andrade, and M. E. Pereira, The occurrence of N-acetyl and N-glycoloylneuraminic acid in Trypanosoma cruzi, Hoppe-Seyler's Z. Physiol. Chem, vol.364, pp.1053-1057, 1983.

S. Schenkman and D. Eichinger, Trypanosoma cruzi transsialidase and cell invasion, Parasitol. Today, vol.9, pp.218-225, 1993.

S. Schenkman, M. S. Jiang, G. W. Hart, and V. Nussenzweig, , 1991.

, A novel cell surface trans-sialidase of Trypanosoma cruzi generates a stage-specific epitope required for invasion of mammalian cells, Cell, vol.65, pp.1117-1125

R. P. Schenkman, F. Vandekerckhove, and S. Schenkman, , 1993.

, Mammalian cell sialic acid enhances invasion by Trypanosoma cruzi, Infect. Immun, vol.61, pp.898-902

S. Schenkman, D. Eichinger, M. E. Pereira, and V. Nussenzweig, Structural and functional properties of Trypanosoma transsialidase, Annu. Rev. Microbiol, vol.48, pp.499-523, 1994.

P. Scudder, J. P. Doom, M. Chuenkova, I. D. Manger, and M. E. Pereira, Enzymatic characterization of beta-D-galactoside alpha 2,3-trans-sialidase from Trypanosoma cruzi, J. Biol. Chem, vol.268, pp.9886-9891, 1993.

L. E. Smith and D. Eichinger, Directed mutagenesis of the Trypanosoma cruzi trans-sialidase enzyme identifies two domains involved in its sialyltransferase activity, Glycobiology, vol.7, pp.445-451, 1997.

G. Taylor, Sialidases: structures, biological significance and therapeutic potential, Curr. Opin. Struct. Biol, vol.6, pp.830-837, 1996.

A. R. Todeschini, L. Mendonç-a-previato, J. O. Previato, and A. Varki,