A nonradioactive 96-well plate assay for screening of trans-sialidase activity

Analytical Biochemistry

Volumn 322, Issue 2, 2003, Pages 139-147

  Schrader, Silke ^a   Tiralongo, Evelin ^a   Paris, Gastón ^b   Yoshino, Teruo ^c   Schauer, Roland ^a  

^a UNIVERSITY OF KIEL   (Germany)

^b INSTITUTO DE INVESTIGACIONES BIOTECNOLÓGICAS   (Argentina)

^c INTERNATIONAL CHRISTIAN UNIVERSITY   (Japan)

Author keywords

96 well plates; Nonradioactive screening assay; Trans sialidase; Trypanosoma congolense; Trypanosoma cruzi

Indexed keywords

ENZYMES; MONOCLONAL ANTIBODIES;

96-WELL PLATE; SCREENING ASSAYS; TRANS-SIALIDASES; TRYPANOSOMA CONGOLENSE; TRYPANOSOMA CRUZI;

SUBSTRATES;

4 METHYLUMBELLIFERYL BETA DEXTRO GALACTOSIDE; GALACTOSIDE; SIALIC ACID DERIVATIVE; SIALIDASE; SIALYLLACTOSE; UNCLASSIFIED DRUG;

ACCURACY; ANALYTIC METHOD; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SUBSTRATE; FLUORESCENCE; FLUOROMETRY; NONHUMAN; PRIORITY JOURNAL; RELIABILITY; REPRODUCIBILITY; TRYPANOSOMA CONGOLENSE; TRYPANOSOMA CRUZI;

TRYPANOSOMA; TRYPANOSOMA CONGOLENSE; TRYPANOSOMA CRUZI;

EID: 0142164917     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2003.07.016     Document Type: Article

References (38)

1. de Souza W. Cell biology of Trypanosoma cruzi. Int. Rev. Cytol. 86:1984;197-283.
2. Schenkman S., Jiang M.S., Hart G.W., Nussenzweig V. 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.
3. Engstler M., Schauer R., Brun R. Distribution of developmentally regulated trans-sialidases in the Kinetoplastida and characterization of a shed trans-sialidase activity from procyclic Trypanosoma congolense. Acta Trop. 59:1995;117-129.
4. Kemp S.J., Teale A.J. Genetic basis of trypanotolerance in cattle and mice. Parasitol. Today. 14:1998;450-454.
5. Pontes de Carvalho L.C., Tomlinson S., Vandekerckhove F., Bienen E.J., Clarkson A.B., Jiang M.S., Hart G.W., Nussenzweig V. Characterization of a novel trans-sialidase of Trypanosoma brucei procyclic trypomastigotes and identification of procyclin as the main sialic acid acceptor. J. Exp. Med. 177:1993;465-474.
6. Schauer R., Reuter G., Mühlpfordt H., Andrade A.F., Pereira M.E. The occurrence of N-acetyl- and N-glycoloylneuraminic acid in Trypanosoma cruzi. Hoppe-Seylers Z. Physiol. Chem. 364:1983;1053-1057.
7. Schenkman S., Ferguson M.A., Heise N., de Almeida M.L., Mortara R.A., Yoshida N. Mucin-like 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;293-304.
8. Pereira-Chioccola V.L., Schenkman S. Biological role of Trypanosoma cruzi trans-sialidase. Biochem. Soc. Trans. 27:1999;516-518.
9. Engstler M., Schauer R. Trans-sialidases in the insect vector stages of African and American trypanosomes: Reply. Parasitol. Today. 10:1994;180.
10. Medina-Acosta E., Paul S., Tomlinson S., Pontes-de-Carvalho L.C. Combined occurrence of trypanosomal sialidase/trans-sialidase activities and leishmanial metalloproteinase gene homologues in Endotrypanum sp. Mol. Biochem. Parasitol. 64:1994;273-282.
11. Mattos-Guaraldi A.L., Formiga L.C., Andrade A.F. Trans-sialidase activity for sialic acid incorporation on Corynebacterium diphtheriae. FEMS Microbiol. Lett. 168:1998;167-172.
12. Tertov V.V., Kaplun V.V., Sobenin I.A., Boytsova E.Y., Bovin N.V., Orekhov A.N. Human plasma trans-sialidase causes atherogenic modification of low density lipoprotein. Atherosclerosis. 159:2001;103-115.
13. Vandekerckhove F., Schenkman S., Pontes de Carvalho L., Tomlinson S., Kiso M., Yoshida M., Hasegawa A., Nussenzweig V. Substrate specificity of the Trypanosoma cruzi trans-sialidase. Glycobiology. 2:1992;541-548.
14. Parodi A.J., Pollevick G.D., Mautner M., Buschiazzo A., Sanchez D.O., Frasch A.C. Identification of the gene(s) coding for the trans-sialidase of Trypanosoma cruzi. EMBO J. 11:1992;1705-1710.
15. Engstler M., Reuter G., Schauer R. The developmentally regulated trans-sialidase from Trypanosoma brucei sialylates the procyclic acidic repetitive protein. Mol. Biochem. Parasitol. 61:1993;1-14.
16. Scudder P., Doom J.P., Chuenkova M., Manger I.D., Pereira M.E. Enzymatic characterisation of β-D-galactoside α2,3-trans-sialidase from Trypanosoma cruzi. J. Biol. Chem. 268:1993;9886-9891.
17. Buschiazzo A., Tavares G.A., Campetella O., Spinelli S., Cremona M.L., Paris G., Amaya M.F., Frasch A.C., Alzari P.M. Structural basis of sialyltransferase activity in trypanosomal sialidases. EMBO J. 19:2000;16-24.
18. Paris G., Cremona M.L., Amaya M.F., Buschiazzo A., Giambiagi S., Frasch A.C., Alzari P.M. Probing molecular function of trypanosomal sialidases: single point mutations can change substrate specificity and increase hydrolytic activity. Glycobiology. 11:2001;305-311.
19. Lee K.B., Lee Y.C. Transfer of modified sialic acids by Trypanosoma cruzi trans-sialidase for attachment of functional groups to oligosaccharide. Anal. Biochem. 216:1994;358-364.
20. Takahashi N., Lee K.B., Nakagawa H., Tsukamoto Y., Kawamura Y., Li Y.T., Lee Y.L. Enzymatic sialylation of N-linked oligosaccharides using an α-(2,3)-specific trans-sialidase from Trypanosoma cruzi: structural identification using a three-dimensional elution mapping technique. Anal. Biochem. 230:1995;333-342.
21. Buschiazzo A., Amaya M.F., Cremona M.L., Frasch A.C., Alzari P.M. The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis. Mol. Cell. 10:2002;757-768.
22. Schenkmann S., Pontes de Carvalho L., Nussenzweig V. Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes. J. Exp. Med. 175:1992;567-575.
23. Lee S.G., Kim B.G. Development of spectrophotometric method for monitoring trans-sialidase reaction and its application. Biotechnol. Lett. 22:2000;819-823.
24. Harrison J.A., Kartha K.P., Turnbull W.B., Scheuerl S.L., Naismith J.H., Schenkman S., Field R.A. Hydrolase and sialyltransferase activities of Trypanosoma cruzi trans-sialidase towards NeuAc-α-2,3-Gal-β-O-PNP. Bioorg. Med. Chem. Lett. 11:2001;141-144.
25. Wang L.X., Pavlova N.V., Li S.C., Li Y.T., Lee Y.C. A fluorometric assay of ceramide glycanase with 4-methylumbelliferyl beta-D-lactoside derivatives. Glycoconj. J. 13:1996;359-365.
26. Veh R.W., Michalski J.C., Corfield A.P., Sander-Wewer M., Gies D., Schauer R. New chromatographic system for the rapid analysis and preparation of colostrum sialyloligosaccharides. J. Chromatogr. 212:1981;313-322.
27. Brun R., Schönberger M. Cultivation and in vitro cloning of procyclic culture forms of Trypanosoma brucei in a semi-defined medium. Acta Trop. 36:1979;289-292.
28. Schauer R. Analysis of sialic acids. Methods Enzymol. 138:1987;132-161.
29. Hara S., Yamaguchi M., Takemori Y., Furuhata K., Ogura H., Nakamura M. Determination of mono-O-acetylated N-acetylneuraminic acids in human and rat sera by fluorometric high-performance liquid chromatography. Anal. Biochem. 179:1989;162-166.
30. Todeschini A.R., Mendonca-Previato L., Previato J.O., Varki A., Halbeek H. Trans-sialidase from Trypanosoma cruzi catalyzes sialoside hydrolysis with retention of configuration. Glycobiology. 10:2000;213-221.
31. Buschiazzo A., Frasch A.C., Campetella O. Medium scale production and purification to homogeneity of a recombinant trans-sialidase from Trypanosoma cruzi. Cell Mol. Biol. 42:1996;703-710.
32. Tiralongo E., Schrader S., Lange H., Lemke H., Tiralongo J., Schauer R. Two Trans-sialidase forms with different sialic acid transfer and sialidase activities from Trypanosoma congolense. J. Biol. Chem. 278:2003;23301-23310.
33. ′ -sialyl-N-acetyllactosamine by regioselective transglycosylation FEBS Lett. 399:1996;203-206.
34. ′ -sialyl-lacto-N-biose I (NeuAcalpha2-3Galbeta1-3GlcNAc) Eur. J. Biochem. 267:2000;942-949.
35. Ribeirao M., Pereira-Chioccola V.L., Eichinger D., Rodrigues M.M., Schenkman S. Temperature differences for trans-glycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi trans-sialidase. Glycobiology. 7:1997;1237-1246.
36. Lee S.G., Shin D.H., Kim B.G. Production of sialyloligosaccharides by trans-sialidase catalysed reaction using fetuin as a sialic acid donor. Enzyme Microb. Technol. 31:2002;742-746.
37. Leguizamon M.L., Russomando G., Luquetti A., Rassi A., Almiron M., Gonzalez- Cappa S., Frasch A.C., Campetella O. Long-lasting antibodies detected by a trans-sialidase inhibition assay in parasite free/serologically cured chagasic patients. J. Infect. Dis. 175:1997;1272-1275.
38. Leguizamon M.S., Russomando G., Rojas de Arias A., Saudio M., Cabral M., Gonzales-Cappa S.M., Frasch A.C.C., Campetella O. Use of trans-sialidase inhibition assay in a population serologically negative for Trypanosoma cruzi but at a high risk of infection. Clin. Diagn. Lab. Immunol. 5:1998;254-255.