메뉴 건너뛰기




Volumn 19, Issue 1, 2000, Pages 16-24

Structural basis of sialyltransferase activity in trypanosomal sialidases

Author keywords

Inhibitor complex; Sialidase; Sialyltransferase; Trypanosoma cruzi; X ray structure

Indexed keywords

CARBOHYDRATE; SIALIDASE; SIALYLTRANSFERASE;

EID: 0034602830     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.1.16     Document Type: Article
Times cited : (125)

References (51)
  • 1
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992) Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 4
    • 0031473756 scopus 로고    scopus 로고
    • Trypanosoma rangeli sialidase: Cloning, expression and similarity to T. cruzi transsialidase
    • Buschiazzo, A., Campetella, O. and Frasch, A.C.C. (1997) Trypanosoma rangeli sialidase: cloning, expression and similarity to T. cruzi transsialidase. Glycobiology, 7, 1167-1173.
    • (1997) Glycobiology , vol.7 , pp. 1167-1173
    • Buschiazzo, A.1    Campetella, O.2    Frasch, A.C.C.3
  • 5
    • 0028225173 scopus 로고
    • A recombinant Trypanosoma cruzi trans-sialidase lacking the amino acid repeats retains the enzymatic activity
    • Campetella, O., Uttaro, A., Parodi, A.J. and Frasch, A.C.C. (1994) A recombinant Trypanosoma cruzi trans-sialidase lacking the amino acid repeats retains the enzymatic activity. Mol. Biochem. Parasitol., 64, 337-340.
    • (1994) Mol. Biochem. Parasitol. , vol.64 , pp. 337-340
    • Campetella, O.1    Uttaro, A.2    Parodi, A.J.3    Frasch, A.C.C.4
  • 6
    • 0026755388 scopus 로고
    • Evidence for a sialosyl cation transition-state complex in the reaction of sialidase from influenza virus
    • Chong, A.K.J., Pegg, M.S., Taylor, N.R. and von Itzstein, M. (1992) Evidence for a sialosyl cation transition-state complex in the reaction of sialidase from influenza virus. Eur. J. Biochem., 207, 335-343.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 335-343
    • Chong, A.K.J.1    Pegg, M.S.2    Taylor, N.R.3    Von Itzstein, M.4
  • 7
    • 0033610089 scopus 로고    scopus 로고
    • Trans-sialidase of Trypanosoma cruzi: Location of galactose-binding site(s)
    • Chuenkova, M., Pereira, M.E. and Taylor, G. (1999) Trans-sialidase of Trypanosoma cruzi: location of galactose-binding site(s). Biochem. Biophys. Res. Commun., 262, 549-556.
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 549-556
    • Chuenkova, M.1    Pereira, M.E.2    Taylor, G.3
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D, 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 9
    • 0029044435 scopus 로고
    • A single tyrosine differentiates active and inactive Trypanosoma cruzi trans-sialidases
    • Cremona, M.L., Sánchez, D.O., Frasch, A.C.C. and Campetella, O. (1995) A single tyrosine differentiates active and inactive Trypanosoma cruzi trans-sialidases. Gene, 160, 123-128.
    • (1995) Gene , vol.160 , pp. 123-128
    • Cremona, M.L.1    Sánchez, D.O.2    Frasch, A.C.C.3    Campetella, O.4
  • 10
    • 0032971645 scopus 로고    scopus 로고
    • Enzymically inactive members of the trans-sialidase family from Trypanosoma cruzi display β-galactose binding activity
    • Cremona, M.L., Campetella, O., Sánchez, D.O. and Frasch, A.C.C. (1999) Enzymically inactive members of the trans-sialidase family from Trypanosoma cruzi display β-galactose binding activity. Glycobiology, 9, 581-587.
    • (1999) Glycobiology , vol.9 , pp. 581-587
    • Cremona, M.L.1    Campetella, O.2    Sánchez, D.O.3    Frasch, A.C.C.4
  • 11
    • 0027364312 scopus 로고
    • Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase
    • Crennell, S.J., Garman, E.F., Graeme Laver, W., Vimr, E.R. and Taylor, G.A. (1993) Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase. Proc. Natl Acad. Sci. USA, 90, 9852-9856.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9852-9856
    • Crennell, S.J.1    Garman, E.F.2    Graeme Laver, W.3    Vimr, E.R.4    Taylor, G.A.5
  • 12
    • 0028773635 scopus 로고
    • Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain
    • Crennell, S.J., Garman, E., Graeme Laver, W., Vimr, E. and Taylor, G. (1994) Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. Structure, 2, 535-544.
    • (1994) Structure , vol.2 , pp. 535-544
    • Crennell, S.J.1    Garman, E.2    Graeme Laver, W.3    Vimr, E.4    Taylor, G.5
  • 13
    • 0029937503 scopus 로고    scopus 로고
    • The structures of Salmonella typhimurium LT2 neuraminidase and its complexes with three inhibitors at high resolution
    • Crennell, S.J., Garman, E.F., Philippon, C., Vasella, A., Graeme Laver, W., Vimr, E.R. and Taylor, G.A. (1996) The structures of Salmonella typhimurium LT2 neuraminidase and its complexes with three inhibitors at high resolution. J. Mol. Biol., 259, 264-280.
    • (1996) J. Mol. Biol. , vol.259 , pp. 264-280
    • Crennell, S.J.1    Garman, E.F.2    Philippon, C.3    Vasella, A.4    Graeme Laver, W.5    Vimr, E.R.6    Taylor, G.A.7
  • 14
    • 84941082197 scopus 로고
    • Trypanosoma rangeli
    • Kreier, J.P. and Baker, J.R. (eds), Academic Press, San Diego, CA
    • D'Alessandro-Bacigalupo, A. and Gore Saravia, N. (1992) Trypanosoma rangeli. In Kreier, J.P. and Baker, J.R. (eds), Parasitic Protozoa. Academic Press, San Diego, CA, Vol. 2, pp. 1-54.
    • (1992) Parasitic Protozoa , vol.2 , pp. 1-54
    • D'Alessandro-Bacigalupo, A.1    Gore Saravia, N.2
  • 15
    • 0030973773 scopus 로고    scopus 로고
    • Sterol biosynthesis inhibitors: Potential chemotherapeutics against Chagas disease
    • Docampo, R. and Schmunis, G.A. (1997) Sterol biosynthesis inhibitors: potential chemotherapeutics against Chagas disease. Parasitol. Today, 13, 129-130.
    • (1997) Parasitol. Today , vol.13 , pp. 129-130
    • Docampo, R.1    Schmunis, G.A.2
  • 16
    • 0029006744 scopus 로고
    • Distribution of developmentally regulated trans-sialidases in the Kinetoplastida and characterization of a shed trans-sialidase activity from procyclic Trypanosoma congolense
    • Engstler, M., Schauer, R. and Brun, R. (1995) Distribution of developmentally regulated trans-sialidases in the Kinetoplastida and characterization of a shed trans-sialidase activity from procyclic Trypanosoma congolense. Acta Trop., 59, 117-129.
    • (1995) Acta Trop. , vol.59 , pp. 117-129
    • Engstler, M.1    Schauer, R.2    Brun, R.3
  • 18
    • 0028087655 scopus 로고
    • Trans-sialidase, SAPA amino acid repeats and the relationship between Trypanosoma cruzi and the mammalian host
    • Frasch, A.C.C. (1994) Trans-sialidase, SAPA amino acid repeats and the relationship between Trypanosoma cruzi and the mammalian host. Parasitology, 108, S37-44.
    • (1994) Parasitology , vol.108
    • Frasch, A.C.C.1
  • 19
    • 0032198656 scopus 로고    scopus 로고
    • Neuraminidase inhibitors take bite out of influenza
    • Glaser, V. (1998) Neuraminidase inhibitors take bite out of influenza. Nature Biotechnol., 16, 1002.
    • (1998) Nature Biotechnol. , vol.16 , pp. 1002
    • Glaser, V.1
  • 20
    • 0032059448 scopus 로고    scopus 로고
    • Glycosidase families
    • Henrissat, B. (1998) Glycosidase families. Biochem. Soc. Trans., 26, 153-156.
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 153-156
    • Henrissat, B.1
  • 21
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and Bairoch, A. (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293, 781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 22
    • 0028232955 scopus 로고
    • Searching protein structure databases has come of age
    • Holm, L. and Sander, C. (1994) Searching protein structure databases has come of age. Proteins, 19, 165-173.
    • (1994) Proteins , vol.19 , pp. 165-173
    • Holm, L.1    Sander, C.2
  • 23
    • 0026603555 scopus 로고
    • Cloning, sequencing and distribution of the Salmonella typhimurium LT2 sialidase gene. nanH, provides evidence for interspecies gene transfer
    • Hoyer, L.L., Hamilton, A.C., Steenbergen, S.M. and Vimr, E.R. (1992) Cloning, sequencing and distribution of the Salmonella typhimurium LT2 sialidase gene. nanH, provides evidence for interspecies gene transfer. Mol. Microbiol., 6, 873-884.
    • (1992) Mol. Microbiol. , vol.6 , pp. 873-884
    • Hoyer, L.L.1    Hamilton, A.C.2    Steenbergen, S.M.3    Vimr, E.R.4
  • 24
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 25
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • Koshland, D.E. (1953) Stereochemistry and the mechanism of enzymatic reactions. Biol. Rev., 28, 416-436.
    • (1953) Biol. Rev. , vol.28 , pp. 416-436
    • Koshland, D.E.1
  • 26
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0032522642 scopus 로고    scopus 로고
    • The crystal structure of an intramolecular trans-sialidase with a Neuacα2→3Gal specificity
    • Luo, Y., Li, S.C., Chou, M.Y., Li, Y.T. and Luo, M. (1998) The crystal structure of an intramolecular trans-sialidase with a NeuAcα2→3Gal specificity. Structure, 15, 521-530.
    • (1998) Structure , vol.15 , pp. 521-530
    • Luo, Y.1    Li, S.C.2    Chou, M.Y.3    Li, Y.T.4    Luo, M.5
  • 29
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr. A, 50, 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 307-325.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-325
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0024431691 scopus 로고
    • Glycosyltranferases. Structure, localization and control of cell type-specific glycosylation
    • Paulson, J.C. and Colley, K.J. (1989) Glycosyltranferases. Structure, localization and control of cell type-specific glycosylation. J. Biol. Chem., 264, 17615-17618.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17615-17618
    • Paulson, J.C.1    Colley, K.J.2
  • 33
    • 0025763222 scopus 로고
    • The Trypanosoma cruzi neuraminidase contains sequences similar to bacterial neuraminidases. YWTD repeats of the low density lipoprotein receptor and type III modules of fibronectin
    • Pereira, M.E.A., Mejia, S., Ortega-Barria, E., Matzilevich, D. and Prioli, R.P. (1991) The Trypanosoma cruzi neuraminidase contains sequences similar to bacterial neuraminidases. YWTD repeats of the low density lipoprotein receptor and type III modules of fibronectin. J. Exp. Med., 174, 179-191.
    • (1991) J. Exp. Med. , vol.174 , pp. 179-191
    • Pereira, M.E.A.1    Mejia, S.2    Ortega-Barria, E.3    Matzilevich, D.4    Prioli, R.P.5
  • 35
    • 0027412004 scopus 로고
    • Characterization of a novel trans-sialidase of Trypanosoma brucei procyclic trypomastigotes and identification of procyclin as the main sialic acid acceptor
    • Pontes de Carvalho, L.C., Tomlinson, S., Vandekerckhove, F., Jay Bienen, E., Clarkson, A.B., Jiang, M.S., Hart, G.W. and Nussenzweig, V. (1993a) 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, 465-474.
    • (1993) J. Exp. Med. , vol.177 , pp. 465-474
    • Pontes De Carvalho, L.C.1    Tomlinson, S.2    Vandekerckhove, F.3    Bienen, E.4    Clarkson, A.B.5    Jiang, M.S.6    Hart, G.W.7    Nussenzweig, V.8
  • 37
    • 0021842684 scopus 로고
    • Incorporation of sialic acid into Trypanosoma cruzi macromolecules. A proposal for a new metabolic route
    • Previato, J.O., Andrade, A.F., Pessolani, M.C. and Mendonca Previato, L. (1985) Incorporation of sialic acid into Trypanosoma cruzi macromolecules. A proposal for a new metabolic route. Mol. Biochem. Parasitol., 16, 85-96.
    • (1985) Mol. Biochem. Parasitol. , vol.16 , pp. 85-96
    • Previato, J.O.1    Andrade, A.F.2    Pessolani, M.C.3    Mendonca Previato, L.4
  • 38
    • 0031440882 scopus 로고    scopus 로고
    • Temperature differences for trans-glycosylation and hydrolysis reactions reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi trans-sialidase
    • Ribeirao, M., Pereira-Chioccola, V.L., Eichinger, D., Rodrigues, M.M. and Schenkman, S. (1997) Temperature differences for trans-glycosylation and hydrolysis reactions reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi trans-sialidase. Glycobiology, 7, 1237-1246.
    • (1997) Glycobiology , vol.7 , pp. 1237-1246
    • Ribeirao, M.1    Pereira-Chioccola, V.L.2    Eichinger, D.3    Rodrigues, M.M.4    Schenkman, S.5
  • 39
    • 0027185635 scopus 로고
    • The sialidase superfamily and its spread by horizontal gene transfer
    • Roggentin, P., Schauer, R., Hoyer, L.L. and Vimr, E.R. (1993) The sialidase superfamily and its spread by horizontal gene transfer. Mol. Microbiol., 9, 915-921.
    • (1993) Mol. Microbiol. , vol.9 , pp. 915-921
    • Roggentin, P.1    Schauer, R.2    Hoyer, L.L.3    Vimr, E.R.4
  • 40
    • 0025769326 scopus 로고
    • A novel cell surface trans-sialidase of Trypanosoma cruzi generates a stage-specific epitope required for invasion in mammalian cells
    • Schenkman, S., Man-Shiow, J., Hart, G.H. and Nussenzweig, V. (1991) A novel cell surface trans-sialidase of Trypanosoma cruzi generates a stage-specific epitope required for invasion in mammalian cells. Cell, 65, 1117-1125.
    • (1991) Cell , vol.65 , pp. 1117-1125
    • Schenkman, S.1    Man-Shiow, J.2    Hart, G.H.3    Nussenzweig, V.4
  • 42
    • 0030902705 scopus 로고    scopus 로고
    • Directed mutagenesis of the Trypanosoma cruzi trans-sialidase enzyme identifies two domains involved in its sialyltransferase activity
    • Smith, L.E. and Eichinger, D. (1997) Directed mutagenesis of the Trypanosoma cruzi trans-sialidase enzyme identifies two domains involved in its sialyltransferase activity. Glycobiology, 7, 445-451.
    • (1997) Glycobiology , vol.7 , pp. 445-451
    • Smith, L.E.1    Eichinger, D.2
  • 43
    • 0030200034 scopus 로고    scopus 로고
    • Isolation and expression of an open reading frame encoding sialidase from Trypanosoma rangeli
    • Smith, L.E., Uemura, H. and Eichinger, D. (1996) Isolation and expression of an open reading frame encoding sialidase from Trypanosoma rangeli. Mol. Biochem. Parasitol., 79, 21-33.
    • (1996) Mol. Biochem. Parasitol , vol.79 , pp. 21-33
    • Smith, L.E.1    Uemura, H.2    Eichinger, D.3
  • 44
    • 0030444832 scopus 로고    scopus 로고
    • Sialidases: Structures, biological significance and therapeutic potential
    • Taylor, G. (1996) Sialidases: structures, biological significance and therapeutic potential. Curr. Opin. Struct. Biol., 6, 830-837.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 830-837
    • Taylor, G.1
  • 45
    • 0032171720 scopus 로고    scopus 로고
    • Natural immunity to trypanosomes
    • Tomlinson, S. and Raper, J. (1998) Natural immunity to trypanosomes. Parasitol. Today, 14, 354-359.
    • (1998) Parasitol. Today , vol.14 , pp. 354-359
    • Tomlinson, S.1    Raper, J.2
  • 46
    • 0026744786 scopus 로고
    • Only some members of a gene family in Trypanosoma cruzi encode proteins that express both trans-sialidase and neuraminidase activities
    • Uemura, H., Schenkman, S., Nussensweig, V. and Eichinger, D. (1992) Only some members of a gene family in Trypanosoma cruzi encode proteins that express both trans-sialidase and neuraminidase activities. EMBO J., 11, 3837-3844.
    • (1992) EMBO J. , vol.11 , pp. 3837-3844
    • Uemura, H.1    Schenkman, S.2    Nussensweig, V.3    Eichinger, D.4
  • 48
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
    • Varghese, J.N., Laver, W.G. and Colman, P.M. (1983) Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature, 303, 35-40.
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 49
    • 0027993630 scopus 로고
    • Microbial sialidases: Does bigger always mean better?
    • Vimr, E.R. (1994) Microbial sialidases: does bigger always mean better? Trends Microbiol., 2, 271-277.
    • (1994) Trends Microbiol. , vol.2 , pp. 271-277
    • Vimr, E.R.1
  • 50
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • Von Itztein, M. et al. (1993) Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature, 363, 418-423.
    • (1993) Nature , vol.363 , pp. 418-423
    • Von Itztein, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.