Abstract
Sialidases (EC 3.2.1.18; N-acylneuraminosyl glycohydrolase) are a family of exoglycosidases that catalyze the cleavage of nonreducing sialic acid residues ketosidically linked to mono-or oligosaccharide chains of glycoconjugates. They are widely distributed in viruses, bacteria, fungi, mycoplasma, and protozoa as well as avian and mammalian species (Rosenberg and Schengrund, 1976; Corfield et al., 1981a; Corfield and Schauer, 1982; Conzelmann and Sandhoff, 1987; Corfield, 1992). Among the various sialidase species, viral and bacterial enzymes have been studied extensively; a number of them have been purified to homogeneity and characterized for their properties and structures. Mammalian sialidases are more labile and often are bound tightly to membranes, hindering successful purification of these enzymes. Much attention, however, has been directed toward these enzymes as interest in the metabolism and biological function of sialoglycoconjugates in mammalian cells has grown in recent years (Schauer, 1982, 1985, 1991; Ledeen, 1989; Schengrund, 1990; Varki, 1992). The term “sialidase” was first proposed by Heimer and Meyer (1956), and “neuraminidase” was introduced a year later (Gottschalk, 1957). Both names have been used interchangeably in the literature. Since the enzyme does not usually apply to neuraminic acid itself, but to its derivatives, sialic acid, the term “sialidase” is deemed more appropriate (Rosenberg and Schengrund, 1976).
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References
Air, G. M., and Laver, W. G., 1989, The neuraminidase of influenza virus, Proteins 6: 341–356.
Air, G. M., Ritchie, L. R., Laver, W. G., and Colman, P. M., 1985, Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity, Virology 145: 117–122.
Air, G. M., Laver, W. G., Luo, M., Stray, S. J., Legrone, G., and Webster, R. G., 1990, Antigenic, sequence, and crystal variation in influenza B neuraminidase, Virology 177: 578–587.
Aisaka, K., Igarashi, A., and Uwajima, T., 1991, Purification crystallization and characterization of neuraminidase from Micromonospora viridifaciens, Agric. Biol. Chem. 55: 997–1004.
Aminoff, D., 1961, Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids, Biochem. J. 81: 384–392.
Ando, S., Tanaka, Y., and Kon, K., 1986, Membrane aging of the brain synaptosomes with special reference to gangliosides, in: Gangliosides and Neuroplasticity, ( G. Tettamanti, R. W. Ledeen, K. Sandhoff, Y. Nagai, and G. Taffano, eds.), Liviana Press, Podova, pp. 105–112.
Ando, S., Yu, R. K., Scarsdale, J. N., Kusunoki, S., and Prestegard, J. H., 1989, High-resolution proton NMR studies of gangliosides. Structures of two types of GD3 lactones and their reactivities with monoclonal antibody R24, J. Biol. Chem. 264: 3478–3483.
Aronson, N.N., and de Duve, C., 1968, Digestive activity of lysosomes. II. The digestion of macromolecular carbohydrates by extracts of rat liver lysosomes, J. Biol. Chem. 243: 4564–4573.
Bach, G., Zeigler, M., Shaap, T., and Kohn, G., 1979, Mucolipidosis: Ganglioside sialidase deficiency, Biochem. Biophys. Res. Commun. 90: 1341–1347.
Bachmayer, H., 1972, Effect of tryptophan modification on the activity of bacterial and viral neuraminidases, FEBS Lett. 23: 217–219.
Baker, N. J., and Gandhi, S. S., 1976, Effect of Ca2+ on the stability of influenza virus neuraminidase, Arch. Virol. 52: 7–18.
Baker, A. T., Varghese, J. N., Laver, W. G., Air, G. M., and Colman, P. M., 1987, Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus, Proteins 2: 111–117.
Barton, N. W., Lipovac, V., and Rosenberg, A., 1975, Effects of strong electrolyte upon the activity of Clostridium perfringens sialidase towards sialyllactose and sialoglycolipids, J. Biol. Chem. 250: 8462–8466.
Baum, L. G., and Paulson, J. C., 1991, The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity, Virology 180: 1015.
Beau, J. M., and Schauer, R., 1980, Metabolism of 4-O-methyl-N-acetylneuraminic acid a synthetic sialic acid, Eur. J. Biochem. 106: 531–540.
Beauregard, G., and Potier, M., 1982, Radiation inactivation of enzymes at low dose rates: Identical molecular weights of rat liver cytosolic and lysosomal neuraminidases, Anal. Biochem. 122: 379–384.
Ben-Yoseph, Y., Momoi, T., Hahn, L. C., and Nadler, H. L., 1982, Catalytically defective ganglioside neuraminidase in mucolipidosis IV, Clin. Genet. 21: 374–381.
Ben-Yoseph, Y., Mitchell, D. A., Yager, R. M., and Pretzlaff, R. K., 1991, Stimulation of GM3 ganglioside activity by an activator protein in patient with mucolipidosis IV and controls, Enzyme 45: 23–29.
Berg, J. O., Lindqvist, L., Andersson, G., and Nord, C. E., 1983, Neuraminidase in Bacteroides fragilis, Appl. Environ. Microhiol. 46: 75–80.
Berg, W., Gutschker-Gdaniec, G., and Schauer, R., 1985, Fluorescent staining of sialidases in polyacrylamide gel electrophoresis and ultrathin-layer isoelectric focusing, Anal. Biochem. 145: 339–342.
Bernacki, R. J., and Bosmann, H. B., 1973, Rat-liver-sialidase activity utilizing a tritium-labeled sialic acid derivative of glycoprotein substrates, Eur. J. Biochem. 34: 425–433.
Berry, A. M., Paton, J. C., Glare, E. M., Hansman, D., and Catcheside, D.E.A., 1988, Cloning and expression of the pneumococcal neuraminidase gene in Escherichia coli, Gene 71: 299–305.
Bhavanandan, V. P., Yeh, A. K., and Carubelli, R., 1975, Neuraminidase assay utilizing sialyl- oligosaccharide substrates with tritium-labeled aglycone, Anal. Biochem. 69: 385–394.
Blok, J., and Air, G. M., 1982, Sequence variation at the 3’ end of the neuraminidase gene from 39 influenza type A viruses, Virology 121: 211–229.
Blok, J., Air, G. M., Laver, W. G., Ward, C. W., Lilley, G. G., Woods, E. F., Roxburgh, C. M., and Inglis, A. S., 1982, Studies on the size, chemical composition, and partial sequence of the neuraminidase (NA) from type A influenza viruses show that the N-terminal region of the NA is not processed and serves to anchor the NA in the viral membrane, Virology 119: 109–121.
Blumberg, W. P., Giorgi, C., Roux, L., Raju, R., Dowling, P., Chollet, A., and Kolakofsky, D., 1985, Sequence determination of the Sendai virus HN gene and its comparison to the influenza virus glycoproteins, Cell 41: 269–278.
Bos, T. J., Davis, A. R., and Nayak, D. P., 1984, NHz terminal hydrophobic region of influenza virus neuraminidase provides the signal function in translocation, Proc. Natl. Acad. Sei. USA 81: 2327–2331.
Bossart, P., Babu, Y. S., Cook, W. J., Air, G. M., and Laver, W. G., 1988, Crystallization and preliminary X-ray analyses of two neuraminidases from influenza B virus B/Hong Kong/8/73 and B/Lee/40, J. Biol. Chem. 263: 6421–6423.
Brossmer, R., and Nebelin, E., 1969, Synthesis of N-formyl-and N-succinyl-D-neuraminic acid on the specificity of neuraminidase, FEBS Lett. 4: 335–336.
Burmeister, W. P., Daniels, R. S., Dayan, S., Gagnon, J., Cusack, S., and Ruigrok, R.W.H., 1991, Sequence and crystallization of influenza virus B/Beijing/ I /87 neuraminidase, Virology 180: 266–272.
Burmeister, W. P., Ruigrok, R.W.H., and Cusack, S., 1992, The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid, EMBO J. 11: 49–56.
Burmeister, W. P., Baudin, F., Cusack, S., and Ruigrok, W. H., 1993, Comparison of structure and sequence of influenza B/Yamagata and B/Beijing neuraminidases shows a conserved “head” but much greater variability in the “stalk” and NB protein, Virology 192: 683–686.
Burnet, F. M., and Stone, J. D., 1947, The receptor-destroying enzyme of V. cholerae, Aust. J. Exp. Biol. Med. 25: 227–233.
Cabezas, J. A., Milicua, M., Bernal, C. S., Villar, E., Pres, N., and Hannoun, C., 1989, Kinetic studies on the sialidase of three influenza B and three influenza A virus strains, Glycoconj. J. 6: 219–227.
Cacalano, G., Kays, M., Saiman, L., and Prince, A., 1992, Production of the Pseudomonas aeruginosa neuraminidase is increased under hyperosmolar conditions and is regulated by genes involved in alginate expression, J. Clin. Invest. 89: 1866–1874.
Camara, M., Mitchell, T. J., Andrew, P. W., and Boulnois, G. J., 1991, Streptococcus pneumoniae produces at least two distinct enzymes with neuraminidase activity: Cloning and expression of a second neuraminidase gene in Escherichia coli, Infect. Immun. 59: 2856–2858.
Carroll, S. M., and Paulson, J. C., 1982, Complete metal ion requirement of influenza virus Ni neuraminidases, Arch. Virol. 71: 273–277.
Carubelli, E., 1962, Neuraminidase activity in mammalian organs, Biochim. Biophys. Acta 60: 196–197.
Carubelli, E., and Tulsiani, D.R.P., 1971, Neuraminidase activity in brain and liver of rats during development, Biochim. Biophys. Acta 237: 78–87.
Cassidy, J. T., Jourdian, G. W., and Roseman, S., 1965, The sialic acid. VI. Purification and properties of sialidase from Clostridium perfringens, J. Biol. Chem. 240: 3501–3506.
Castrucci, M. R., and Kawaoka, Y., 1993, Biologic importance of neuraminidase stalk length in influenza A virus, J. Virol. 67: 759–764.
Cavallesco, R., and Pereira, M.E.A., 1988, Antibody to Trypanosoma cruzi neuraminidase enhances infection in vitro and identifies a subpopulation of trypomastigotes, J. Immunol. 140: 617–625.
Chabas, A., Guardiola, A., and Burguera, J. M., 1987, An activator protein of oligosaccharide sialidase, Biochem. Int. 15: 449–457.
Chiarini, A., Fiorilli, A., Siniscalco, C., Tettamanti, G., and Venerando, V., 1990, Solubilization of the membrane-bound sialidase from pig brain by treatment with bacterial phosphatidylinositol phospholipase C, J. Neurochem. 55: 1576–1584.
Chiarini, A., Fiorilli, A., di Francesco, L., Venerando, B., and Tettamanti, G., 1993, Human erythrocyte sialidase is linked to the plasma membrane by a glycosylphosphatidylinositol anchor and partly located on the outer surface, Glycoconj. J. 10: 64–71.
Chigorno, V., Cardace, G., Pitto, M., Sonnino, S., Ghidoni, R., and Tettamanti, G., 1986, A radiometric assay for ganglioside sialidase to the determination of the enzyme subcellular location in cultured human fibriblasts, Anal. Biochem. 153: 283–294.
Chong, A.K.J., Pegg, M. S., and von Itzstein, M., 1991, Influenza virus sialidase: Effect of calcium on steady-state kinetic parameters, Biochim. Biophys. Acta 1077: 65–71.
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.
Chou, M.-Y., Li, Y.-T., and Li, S.-C., 1992, a2–3 specific sialidase, sialidase L, Glycobiology 5: 495.
Chuang, N.-N., and Yang, B. C., 1990, A sialidase from hepatopancreas of the shrimp Penaeus japonicus (Crustacea: Decapoda): Reversible binding with the acidic ß-galactosidase, Comp. Biochem. Physiol. 97C: 353–356.
Colman, P. M., 1989, Neuraminidase: Enzyme and antigen, in: The Influenza viruses, ( R. M. Krug, ed.), Plenum Press, New York, pp. 175–210.
Colman, P. M., Varghese, J. N., and Laver, W. G., 1983, Structure of the catalytic and antigenic sites in influenza virus neuraminidase, Nature 303: 41–44.
Colman, P. M., Laver, W. G., Varghese, J. N., Baker, A. T., Tulloch, P. A., Air, G. M., and Webster, R. G., 1987, Three-dimensional structure of a complex of antibody with influenza virus neuraminidse, Nature 326: 358–363.
Colman, P. M., Hoyne, P. A., and Lawrence, M. C., 1993, Sequence and structure alignment of paramyxovirus hemagglutinin-neuraminidase with influenza virus neuraminidase, J. Virol. 67: 2972–2980.
Conzelmann, E., and Sandhoff, K., 1987, Glycolipid and glycoprotein degradation, Adv. Enzymol. 60: 89–216.
Corfield, A. P., and Schauer, R., 1982, Metabolism of sialic acid, in: Sialic Acids—Chemistry, Metabolism, and Function, ( R. Schauer, ed.), Springer-Verlag, Berlin, pp. 195–261.
Corfield, A. P., Michalski, J. C., and Schauer, R., 1981a, The substrate specificity of sialidases from microorganisms and mammals, in: Perspectives in Inherited Metabolic Diseases, (G. Tettamanti, P. Durand, and S. di Donate, eds.), Vol. 4, Edi Ermes, Milan, Italy, pp. 3–70.
Corfield, A. P., Veh, R. W., Wember, M., Michalski, J. C., and Schauer, R., 1981b, The release of N-acetyl and N-glycolyl-neuraminic acid from soluble complex carbohydrates and erythrocytes by bacterial, viral and mammalian sialidases, Biochem. J. 197: 293–299.
Corfield, A. P., 1992, Bacterial sialidases—Roles in pathogenesis and nutrition, Glycobiology 2: 509–521.
Corfield, A. P., Wember, M., Schauer, R., and Rott, R., 1982, The specificity of viral sialidases: The use of oligosaccharide substrates to probe enzyme characteristics and strain-specific differences, Eur. J. Biochem. 124: 521–525.
Corfield, A. P., Higa, H., Paulson, J. C., and Schauer, R., 1983, The specificity of viral and bacterial sialidases for a(2–3)- and a(2–6)-linked sialic acids in glycoproteins, Biochim. Biophys. Acta 744: 121–126.
Corfield, A. P., Sander-Wewer, M., Veh, R. W., Wember, M., and Schauer, R., 1986, The action of sialidases on substrates containing 0-acetylsialic acids, Biol. Chem. Hoppe-Seyler 367: 433–439.
Corfield, A. P., Wagner, S. A., Clamp, J. R., Kriaris, M. S., and Hoskins, L. C., 1992, Mucin degradation in the human colon: Production of sialidase, sialate O-acetylesterase, N-acetylneuraminate lyase, arylesterase, and glycosulfatase activities by strains of fecal bacteria, Infect. Immun. 60: 3971–3978.
Cross, A. S., and Wright, D. G., 1991, Mobilization of sialidase from intracellular stores to the surface of human neutrophils and its role in stimulated adhesion responses of these cells, J. Clin. Invest. 88: 2067–2076.
Cruz, T. F., and Gurd, J. W., 1978, Reaction of synaptic plasma membrane sialoglycoproteins with intrinsic sialidase and wheat germ agglutinin, J. Biol. Chem. 253: 7314–7318.
Cruz, T. F., and Gurd, J. W., 1981, The effects of development on activity, specificity and endogenous substrates of synaptic membrane sialidase, Biochim. Biophys. Acta 675: 201–208.
Cruz, T. F., and Gurd, J. W., 1983, Identification of intrinsic and sialoglycoprotein substrates in rat brain synaptic junctions, J. Neurochem. 40: 1599–1604.
Czarniecki, M. F., and Thornton, E. R., 1977, Carbon-13 NMR spin lattice relaxation in the N-acetylneuraminic acids, J. Am. Chem. Soc. 99: 8273–8279.
Dairaku, K., Miyagi, T., Wakui, A., and Tsuiki, S., 1986, Cytosolic sialidases of rat tissues with special reference to skeletal muscle enzyme, Biochem. Int. 13: 741–748.
Dale, B., Brown, R., Miller, J., White, R. T., Air, G. M., and Cordell, B., 1986, Nucleotide and deduced amino acid sequence of the influenza neuraminidase genes of two equine serotypes, Virology 155: 460–468.
Davis, L., Baig, M. M., and Atoub, E. M., 1979, Properties of extracellular neuraminidase produced by group A streptococcus, Infect. Immun. 24: 780–786.
d’Azzo, A., Hoogeveen, A. T., Reuser, A.J.J., Robinson, D., and Galjaard, H., 1982, Molecular defect in combined 3-galactosidase and neuraminidase deficiency in man, Proc. Natl. Acad. Sci. USA 79: 4535–4539.
Dimmock, N. J., 1971, Dependence of the activity of an influenza virus neuraminidase upon Ca2+, J. Gen. Virol. 13: 481–483.
Domingues, R. M., Cavalcanti, S. M., Andrale, A. F., and Ferreira, M. C., 1992, Sialic acid as receptor of Bacteroides fragilis lectin-like adhesion, Int. J. Microbiol. Virol. Parasitol. 277: 340–344.
Drzeniek, R., 1972, Viral and bacterial neuraminidases, Curr. Top. Microbiol. Immunol. 59: 35–74.
Drzeniek, R., 1973, Substrate specificity of neuraminidase, Histochem. J. 5: 271–290.
Drzeniek, R., Seto, J. T., and Rott, R., 1966, Characterization of neuraminidases from myxoviruses, Biochim. Biophys. Acta 128: 547–558.
Eisen, D., and Franson, R. C., 1987, Acid-active neuraminidases in growth media from cultures of pathogenic Naegleria fowleri and in sonicates of rabbit alveolar macrophages, Biochim. Biophys. Acta 924: 369–372.
Els, M. C., Air, G. M., Murti, K. G., Webster, R. G., and Laver, W. G., 1985, An 18-amino acid deletion in an influenza neuraminidase, Virology 142: 241–247.
Engstler, M., Reuter, G., and Schauer, R., 1992, Purification and characterization of a novel sialidase found in procyclic culture forms of Trypanosoma brucei, Mol. Biochem. Parasitol. 54: 21–30.
Esievo, K.A.N., 1983, Trypanosoma vivax, stock V953: Inhibitory effect of type A influenza virus anti-HAV8 serum on in vitro neuraminidase (sialidase) activity, J. Parasitol. 69: 491–495.
Ferrero-Garcia, M. A., Trombetta, S. E., Sanchez, D. O., Reglero, A., Frasch, A. C., and Parodi, A. J., 1993, The action of Trypanosoma cruzi trans-sialidase on glycolipids and glycoproteins, Eur. J. Biochem. 213: 765–771.
Fields, S., Winter, G., and Brownlee, G. G., 1981, Structure of the neuraminidase gene in human influenza virus A/PR/8/34, Nature 290: 213–217.
Fingerhut, R., van der Horst, G.T.J., Verheijen, F. W., and Conzelmann, E., 1992, Degradation of gangliosides by the lysosomal sialidase requires an activator protein, Eur. J. Biochem. 208: 623–629.
Fiorilli, A., Venerando, B., Siniscalco, C., Monti, E., Bresciani, R., Caimi, L., Preti, A., and Tettamanti, G., 1989, Occurrence in brain lysosomes of a sialidase active on ganglioside, J. Neurochem. 53: 672–680.
Fiorilli, A., Siniscalco, C., Chiarini, A., di Francesco, L., Venerando, B., and Tettamanti, G., 1991, Occurrence of sialidase activity in two distinct and highly homogeneous populations of lysosomes prepared from the brain of developing mouse, FEBS Leu. 282: 235–238.
Fischer, C., Kelm, S., Ruch, B., and Schauer, R., 1991, Reversible binding of sialidase-treated rat lymphocytes by homologous peritoneal macrophages, Carbohydr. Res. 213: 263–273.
Fraser, A. G., and Brown, R., 1981, Neuraminidase production by Bacteroidacea, J. Med. Microbiol. 14: 63–73.
Frevert, U., Schenkman, S. D., and Nussenzweig, V., 1992, Stage-specific expression and intracellular shedding of the cell surface trans-sialidase of Trypanosoma cruzi, Infect. Immun. 60: 2349–2360.
Friebolin, H., Brossmer, R., Keilich, G., Ziegler, D., and Supp, M., 1980, H-NMR-Spektroskopischer Nachweis der N-Acetyl-a-D-Neuraminsaure als primares Spaltprodukt der Neuraminidasen, Hoppe-Seyler’s Z. Physiol. Chem. 361: 697–702.
Galen, J. E., Ketley, J. M., Fasano, A., Richardson, S. H., Wasserman, S. S., and Kaper, J. B., 1992, Role of Vibrio cholerae neuraminidase in the function of cholera toxin, Infect. Immun. 60: 406–415.
Galjart, N., Gillemans, N., Harris, A., van der Horst, G.T.J., Verheijen, F. W., Galjaard, H., and d’Azzo, A., 1988, Expression of cDNA encoding the human protective protein associated with lysosomal ß-galactosidase and neuraminidase: Homology to yeast proteases, Cell 54: 755–764.
Garcia-Sastre, A., Cobaleda, C., Cabezas, J. A., and Villar, E., 1991, On the inhibition mechanism of the sialidase activity from Newcastle disease virus, Biol. Chem. Hoppe-Seyler 372: 923–927.
Ghidoni, R., Sonnino, S., Masserini, M., Orlando, P., and Tettamanti, G., 1981, Specific tritium labeling of gangliosides at the 3-position of sphingosine, J. Lipid Res. 22: 1286–1295.
Gorman, W. L., Takahashi, T., Scroggs, R. A., and Fortner, A., 1991, Identification of amino acid positions associated with neuraminidase activity of the hemagglutinin-neuraminidase glycoprotein of Sendai virus, Virology 180: 803–806.
Gottschalk, A., 1957, Neuraminidase: The specific enzyme of influenza virus and Vibrio cholerae, Biochim. Biophys. Acta 23: 645–646.
Guzman, C. A., Plate, M., and Pruzzo, C., 1990, Role of neuraminidase-dependent adherence in Bacterioides fragilis attachment to human epithelial cells, FEMS Microbiol. Lett. 59: 187–192.
Haddad, E. B., and Gies, J. P., 1992, Neuraminidase reduced the number of super-high-affinity (3H)oxotremorin-M binding sites in lung, Eur. J. Pharmacol. 211: 273–276.
Hall, F. B., Webster, P., Ma, A. K., Joiner, K. A., and Andrews, N. W., 1992, Desialylation of lysosomal membrane glycoproteins by Trypanosoma cruzi: A role for the surface neuraminidase in facilitating parasite entry into the host cell cytoplasm, J. Exp. Med. 176: 313–325.
Hechler, V., Mersel, M., Dreyfus, H., and Maitre, M., 1990, Effects of phospholipases, proteases and neuraminidase on gamma-hydroxybutyrate binding sites, Mol. Cell. Biochem. 93: 87–94.
Heijlman, J., and Roukema, P. A., 1972, The action of calf brain sialidase on gangliosides, sialoglycoproteins and sialoglycopeptides, J. Neurochem. 19: 2567–2575.
Heimer, R., and Meyer, K., 1956, Studies on sialic acid of submaxillary mucoid, Proc. Natl. Acad. Sci. USA 42: 728–734.
Henningsen, M., Roggentin, P., and Schauer, R., 1991, Cloning, sequencing, expression of the sialidase gene from Actinomyces viscosus DSM 43798, Biol. Chem. Hoppe-Seyler 372: 1065 1072.
Henrickson, K. J., and Savatski, L. L., 1992, Genetic variation and evolution of human parainfluenza virus type I hemagglutinin neuraminidase: Analysis of 12 clinical isolates, J. Infect. Dis. 166: 995–1005.
Heuermann, D., Roggentin, P., Kleineidam, R., and Schauer, R., 1991, Purification and characterization of a sialidase from Clostridium chauvoei NC08596, Glycoconj. J. 8: 95–101.
Hiebert, S. W., Peterson, R. G., and Lamb, R. A., 1985, Hemagglutinin-neuraminidase protein of the paramyxovirus simian virus 5: Nucleotide sequence of the mRNA predicts an N-terminal membrane anchor, J. Virol. 54: 1–6.
Hirabayashi, Y., Hyogo, A., Nakao, T., Tsuchiya, K., Suzuki, Y., Matsumoto, M., Kon, K., and Ando, S., 1990, Isolation and characterization of extremely minor gangliosides, GM lb and GD la, in adult bovine brains as developmentally regulated antigens, J. Biol. Chem. 265: 8144–8151.
Hiraiwa, M., Uda, Y., Nishizawa, M., and Miyatake, T., 1987, Human placental sialidase partial purification and characterization, J. Biochem. 101: 1273–1279.
Hiraiwa, M., Nishizawa, M., Uda, Y., Nakajima, T., and Miyatake, T., 1988, Human placental sialidase: Further purification and characterization, J. Biochem. 103: 86–90.
Hiraiwa, M., Uda, Y., Tsuji, S., Miyatake, T., Martin, B. M., Tayama, M., O’Brien, J. S., and Kishimoto, Y., 1991, Human placental sialidase complex: Characterization of the 60 KDA protein that cross-reacts with anti-saposin antibodies, Biochem. Biophys. Res. Commun. 177: 1211–1216.
Hiti, A. L., and Nayak, D. P., 1982, Complete nucleotide sequence of the neuraminidase gene of human influenza virus A/WSN/33, J. Virol. 41: 730–734.
Hogue, B. G., and Nayak, D. P., 1992, Synthesis and processing of the influenza virus neuraminidase, a type II transmembrane glycoprotein, Virology 188: 510–517.
Hong, V. N., Beauregard, G., Potier, M., Belisle, M., Mameli, L., Gatti, R., and Durand, P., 1980, Studies on the properties of human leucocyte neuraminidases, Biochim. Biophys. Acta 616: 259270.
Hoogeveen, A. T., d’Azzo, A., Brossmer, R., and Galjaard, H., 1981, Correction of combined 13-galactosidase/neuraminidase deficiency in human fibroblasts, Biochem. Biophys. Res. Commun. 103: 292–300.
Hoogeveen, A. T., Verheijen, F. W., and Galjaard, H., 1983, The relation between human lysosomal 13-galactosidase and its protective protein, J. Biol. Chem. 258: 12143–12146.
Horvat, A., and Touster, O., 1968, On the lysosomal occurrence and the properties of the neuraminidase of rat liver and of the neuraminidase of rat liver and of Ehrlich ascites tumor cells, J. Biol. Chem. 243: 4380–4390.
Hoskins, L. C., Boulding, E. T., Gerken, T. A., Harouny, V. R., and Krisris, M. S., 1992, Mucin glycoprotein degradation by mucin-oligosaccharide-degrading strains of human fecal bacteria, Microbiol. Ecol. Health Dis. 5: 193–207.
Houde, M., and Arora, D. J., 1990, Stimulation of tumor necrosis factor secretion by purified influenza virus neuraminidase, Cell. Immunol. 129: 104–111.
Royer, L. L., Roggentin, P., Schauer, R., and Vimr, E. R., 1991, Purification and properties of cloned Salmonella typhimurium LT2 sialidase with virus-typical kinetic preference for sialyl a2–3 linkages, J. Biochem. 110: 462–467.
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.
Huang, R.T.C., and Orlich, M., 1972, Substrate specificities of the neuraminidases of Newcastle disease and fowl plague viruses, Hoppe-Seyler’s Z. Physiol. Chem. 353: 318–322.
Huang, R. T., Rott, R., Wahn, K., Klenk, H. D., and Kohama, T., 1980, The function of the neuraminidase in membrane fusion induced by myxoviruses, Virology 107: 313–319.
Huang, R. T. C., Dietsch, E., and Rott, R., 1985, Further studies on the role of neuraminidase and the mechanism of low pH dependence in influenza virus-induced membrane fusion, J. Gen. Virol. 66: 295–301.
Igarashi, M., and Bando, Y., 1990, Enhanced efficiency of cell hybridization by neuraminidase treatment, J. Immunol. Methods 135: 91–93.
Iorio, R. M., and Glickman, R. L., 1992, Fusion mutants of Newcastle disease virus selected with monoclonal antibodies to the hemagglutinin-neuraminidase, J. Virol. 66: 6626–6633.
Jorgensen, E. D., Collins, P. L., and Iomedico, P. T., 1987, Cloning and nucleotide sequence of Newcastle disease virus hemagglutinin-neuraminidase mRNA: Identification of a putative sialic acid binding site, Virology 156: 12–24.
Kabayo, J. P., and Hutchinson, D. W., 1975, Studies on a neuraminidase from Streptomyces griseus, FEBS Lett. 78: 221–224.
Karasuno, T., Kanayama, Y., Nishiura, T., Nakao, H., Yonezawa, T., and Tarui, S., 1992, Glycosidase inhibitors (castanospermine and swainsonine) and neuraminidase inhibit pokeweed mitogen-induced B cell maturation, Eur. J. Immunol. 22: 2003–2008.
Kessler, J., Heck, J., Tannenbaum, S. W., and Flashner, M., 1982, Substrate and product specificity of Arthrobacter sialophilus neuraminidase, J. Biol. Chem. 257: 5056–5060.
Kessler, N., Bardeletti, G., and Aymard, M., 1977, The neuraminidase of human parainfluenza 1 virus (HA2 virus), J. Gen. Virol. 37: 547–556.
Khorlin, A. Y., Privalova, I. M., Zakstelskaya, L. Y., Molibog, E. V., and Evstigneeva, N. A., 1970, Synthetic inhibitors of Vibrio cholerae neuraminidase and neuraminidases of some influenza virus strains, FEBS Lett. 8: 17–19.
Kishore, G. S., Tulsiani, D.R.P., Bhavanandan, V. P., and Carubelli, R., 1975, Membrane-bound neuraminidase of rat liver: Neuraminidase activity in Golgi apparatus, J. Biol. Chem. 250: 2655–2659.
Kleineidam, R. G., Furuhata, K., Ogura, H., and Schauer, R., 1990, 4-Methylumbelliferyl-aglycosides of partially O-acetylated N-acetylneuraminic acids as substrates of bacterial and viral sialidases, Biol. Chem. Hoppe-Seyler 371: 715–719.
Kodama, H., Baum, L. G., and Paulson, J. C., 1991, Synthesis of linkage-specific sialoside substrates for colorimetric analysis of neuraminidases, Carbohydr. Res. 218: 111–119.
Koerner, T.A.W., Prestegard, J. H., Demou, P. C., and Yu, R. K., 1983, High-resolution proton NMR studies of gangliosides. Use of homonuclear two-dimensional spin—echo J-correlated spectroscopy for determination of residue composition and anomeric configuration, Biochemistry 22: 2676–2687.
Kuratowska, Z., and Kubicka, T., 1967, Purification and some properties of the neuraminidae from rabbit kidney, Acta Biochim. Pol. 14: 255–259.
Lambre, C. R., Greffard, A., Gattegno, L., and Saffar, L., 1989/1990, Modification of sialidase activity during the monocyte—macrophage differentiation in vitro, Immunol. Lett. 23: 179–182.
Lambre, C. R., Terzidis, H., Greffard, A., and Webster, R. G., 1991, An enzyme-linked lectin assay for sialidase, Clin. Chim. Acta 198: 183–194.
Landolfi, N. F., Leone, J., Womack, J. E., and Cook, R. G., 1985, Activation ofT lymphocytes results in an increase in H2 encoded neuraminidase, Immunogenetics 22: 159–167.
Laver, W. G., 1978, Crystallization and peptide maps of neuraminidase “heads” from H2N2 and H3N3 influenza virus strains, Virology 86: 78–87.
Laver, W. G., Air, G., Webster, R. G., and Markoff, L. J., 1982, Amino acid sequence changes in antigenic variants of type A influenza virus 2 neuraminidase, Virology 122: 450–460.
Laver, W. G., Colman, P. M., Webster, R. G., Hinsha, V. S., and Air, G. M., 1984, Influenza virus neuraminidase with hemagglutinin activity, Virology 137: 314–323.
Laver, W. G., Webster, R. G., and Colman, P. M., 1987, Crystals of antibodies complexcd with influenza virus neuraminidase show isosteric binding of antibody to wild-type and variant antigens, Virology 156: 181–184.
Laver, W. G., Thompson, S. D., Murti, K. G., and Portner, A., 1989, Crystallization of Sendai virus HN protein complexed with monoclonal antibody Fab fragments, Virology 171: 291–293.
Ledeen, R. W., 1989, Biosynthesis, metabolism, and biological effects of gangliosides, in: Neurobiology of Glycoconjugates, ( R. U. Margolis and R. K. Margolis, eds.), Plenum Press, New York, pp. 43–83.
Ledeen, R., and Salsman, K., 1965, Structure of Tay-Sachs ganglioside, Biochemistry 4: 2225–2232.
Leibovitz, Z., and Gatt, S., 1968, Enzymatic hydrolysis of sphingolipids. VII. Hydrolysis of gangliosides by a neuraminidase from calf brain, Biochim. Biophys. Acta 152: 136–143.
Lentz, M. R., Air, G. M., Laver, W. G., and Webster, R. G., 1984, Sequence of the neuraminidase gene of influenza virus A/Tokyo/3/67 and previously uncharacterized monoclonal variants, Virology 135: 257–265.
Lentz, M. R., Webster, R. T., and Air, G. M., 1987, Site-directed mutation of the active site of influenza neuraminidase and implications for the catalytic mechanism, Biochemistry 26: 5351–5358.
Li, Y. T., Nakagawa, H., Ross, S. A., Hansson, G. C., and Li, S. C., 1990, A novel sialidase which releases 2,7-anhydro-a-N-acetylneuraminic acid from sialoglycoconjugates, J. Biol. Chem. 265: 21629–21633.
Libby, P., Alroy, J., and Pereira, M.E.A., 1986, A neuraminidase from Trypanosoma cruzi removes sialic acid from the surface of mammalian myocardial and endothelial cells, J. Clin. Invest. 77: 127–135.
Lieser, M., Harms, E., Kern, H., Bach, G., and Cantz, M., 1989, Ganglioside GM3 sialidase activity in fibroblasts of normal individuals and of patients with sialidosis and mucolipidosis IV, Biochem. J. 260: 69–74.
Lipovac, V., Barton, N., and Rosenberg, A., 1973, Control of the action of Vibrio cholerae sialidase on mammalian brain gangliosides by ionic strength, Biochemistry 12: 1858–1861.
Lock, R. A., Paton, J. C., and Hansman, D., 1988, Purification and immunological characterization of neuraminidase produced by Streptococcus pneumoniae, Microbiol. Pathog. 4: 33–43.
Mahadevan, S., Nduaguba, J. C., and Tappet, A. L., 1967, Sialidase of rat liver and kidney, J. Biol. Chem. 242: 4409–4413.
Malby, R. L., Caldwell, J. B., Gruen, L. C., Harley, V. R., Ivancic, N., Kortt, A. A., Lilley, G. G., Power, B. E., Webster, R. G., and Colman, P. M., 1993, Recombinant antineuraminidase single chain antibody: Expression, characterization, and crystallization in complex with antigen, Proteins 16: 57–73.
Martinez, C., Del Rio, L., Portela, A., Domingo, E., and Ortin, J., 1983, Evolution of the influenza virus neuraminidase gene during drift of the N2 subtype, Virology 130: 539–545.
Mattingly, S. J., Milligan, T. W., Pierpont, A. A., and Straus, D. C., 1980, Extracellular neuraminidase production by clinical isolates of group B streptococci from infected neonates, J. Clin. Microbiol. 12: 633–635.
Merz, D. C., and Wolinsky, J. S., 1983, Conversion of nonfusing mumps virus infections to fusing infections by selective proteolysis of the HN glycoprotein, Virology 131: 328–340.
Meyer, D. M., Lemonnier, M., and Bourrillon, R., 1981, Human liver neuraminidase, Biochem. Biophys. Res. Commun. 130: 1302–1309.
Michalski, J. C., Corfield, A. P., and Schauer, R., 1982, Solubilization and affinity chromatography of a sialidase from human liver, Hoppe-Seyler’s Z. Physiol. Chem. 363: 1097–1102.
Michalski, J. C., Corfield, A. P., and Schauer, R., 1986, Properties of human liver lysosomal sialidase, Hoppe-Seyler’s Z. Physiol. Chem. 367: 715–722.
Miura, N., Nakatani, Y., Ishiura, M., Uchida, T., and Okada, Y., 1985, Molecular cloning of a full-length cDNA encoding the hemagglutinin-neuraminidase glycoprotein of Sendai virus, FEBS Lett. 188: 112–116.
Miyagi, T., and Tsuiki, S., 1984, Rat-liver lysosomal sialidase. Solubilization, substrate specificity and comparison with the cytosolic sialidase, Eur. J. Biochem. 141: 75–81.
Miyagi, T., and Tsuiki, S., 1985, Purification and characterization of cytosolic sialidase from rat liver, J. Biol. Chem. 260: 6710–6716.
Miyagi, T., and Tsuiki, S., 1986, Evidence for sialidase hydrolyzing gangliosides GM2 and GM I in rat liver plasma membrane, FEBS Lett. 206: 223–228.
Miyagi, T., Goto, T., and Tsuiki, S., 1984, Sialidase of rat hepatomas: Quantitative and qualitative comparison with rat liver sialidase, Gann 75: 1076–1082.
Miyagi, T., Sagawa, J., Konno, K., Handa, S., and Tsuiki, S., 1990a, Biochemical and immunological studies on two distinct ganglioside-hydrolyzing sialidases from the particulate fraction of rat brain, J. Biochem. 107: 787–793.
Miyagi, T., Sagawa, J., Konno, K., Handa, S., and Tsuiki, S., 1990b, Immunological discrimination of intralysosomal, cytosolic, and two membrane sialidases present in rat tissues, J. Biochem. 107: 794–798.
Miyagi, T., Konno, K., Sagawa, J., and Tsuiki, S., 1990c, Neoplastic alteration of a membrane-associated sialidase of rat liver, Jpn. J. Cancer Res. 81: 915–919.
Miyagi, T., Sagawa, J., Kuroki, T., Matsuya, Y., and Tsuiki, S., 1990d, Tumor-promoting phorbol ester induced alterations of sialidases and sialyltransferase activities of JB6 cells, Jpn. J. Cancer Res. 81: 1286–1292.
Miyagi, T., Konno, K., Emori, Y., Kawasaki, H., Suzuki, K., Yasui, A., and Tsuiki, S., 1993, Molecular cloning and expression of cDNA encoding rat skeletal muscle cytosolic sialidase, J. Biol. Chem. 268: 26435–26440.
Moran, N. M., Breen, K. C., and Regan, C. M., 1986, Characterization and cellular localization of a developmentally regulated rat neural sialidase, J. Neurochem. 47: 18–22.
Müller, H. E., 1974, Neuraminidase of bacteria and protozoa and their pathogenic role, Behring Inst. Mitt. 55: 34–56.
Myers, R. W., Lee, R. T., Lee, Y. C., Thomas, G. H., Reynolds, L. W., and Uchida, Y., 1980, The synthesis of 4-methylumbelliferyl a-ketoside of N-acetylneuraminic acid and its use in a fluorometric assay for neuraminidase, Anal. Biochem. 101: 166–174.
Nagai, T., Klenk, H.-D., and Rott, R., 1976, Proteolytic cleavage of viral glycoproteins and the significance of the virulence of Newcastle disease virus, Virology 72: 494–508.
Nagy, E., Derbyshire, J. B., Dobos, P., and Krell, P. J., 1990, Cloning and expression of NDV hemagglutinin-neuraminidase cDNA in a Baculovirus expression vector system, Virology 176: 426–438.
Nakamura, M., Yoshida, T., Isobe, K. I., Iwamoto, T., Jamschedur Rahman, S. M., Zhang, Y. H., Hasegawa, T., Ichihara, M., and Nakashima, I., 1991, Modulation of the secondary antibody response of murine lymphocytes to sheep red blood cells in vitro by neuraminidase and exoglycosidases, Immunol. Leu. 29: 235–240.
Nees, S., Veh, R. W., and Schauer, R., 1975, Purification and characterization of neuraminidase from Clostridium perfringens, Hoppe-Seyler’s Z. Physiol. Chem. 356: 1027–1042.
Nerome, K., Kanegae, Y., Yoshioka, Y., Itamura, S., Ishida, M., Gojobori, T., and Oya, A., 1991, Evolutionary pathway of N2 neuraminidases of swine and human influenza A viruses: Origin of the neuraminidase genes of two reassortance (HIN2) isolated from pigs, J. Gen. Virol. 72: 693–698.
Nilsson, J., Ksiazek, T., and Thyberg, J., 1982, Effects of neuraminidase on DNA synthesis, proliferation and endocytosis of cultivated arterial smooth muscle cells, Exp. Cell Res. 142: 333–339.
Nishikawa, K., Morishita, T., Toyoda, T., Miyadai, T., Yoshida, T., and Nagai, Y., 1986, Topological and operational delineation of antigenic sites on the HN glycoprotein of Newcastle disease virus and their structural requirements, J. Virol. 60: 987–993.
Nojiri, H., Takaku, F., Tetsuka, T., and Saito, M., 1982, Stimulation of sialidase activity during cell differentiation of human promyelocytic leukemic cell line HL-60, Biochem. Biophys. Res. Commun. 104: 1239–1246.
Nuss, J. M., and Air, G. M., 1991, Transfer of the hemagglutinin activity of influenza virus neuraminidase subtype N9 into an N2 neuraminidase background, Virology 183: 496–504.
Ogura, K., and Sweeley, C. C., 1992, Mitogenic effects of bacterial neuraminidase and lactosylceramide on human cultured fibroblasts, Exp. Cell Res. 199: 169–173.
Ogura, K., Ogura, M., Anderson, R. L., and Sweeley, C. C., 1992, Peroxidase-amplified assay of sialidase activity toward gangliosides, Anal. Biochem. 200: 52–57.
Ohbayashi, T., Taka, M., and Mohri, T., 1987, Effect of neuraminidase treatment on the lipid fluidity of the intestinal brush-border membranes, Biochim. Biophys. Acta 905: 57–64.
Ohmann, R., Rosenberg, A., and Svennerholm, L., 1970, Human brain sialidase, Biochemistry 9: 3774–3782.
Orefici, G., de Stasio, A., Guarino, M., Martini, A., and Orsi, N., 1984, Group b streptococci: Extracellular Neuraminidase production and virulence in mouse, Microbiologica 7: 75–78.
O’Toole, R. D., and Stahl, W. L., 1975, Experimental pneumococcal meningitis: Effects of neuraminidase and other pneumococcal constituents on cerebrospinal fluid in the intact dog, J. Gen. Virol. 33: 159–163.
Palese, P., and Compans, R. W., 1976, Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): Mechanism of action, J. Gen. Virol. 33: 159–163.
Palese, P., Tobita, K., and Ueda, M., 1974, Characterization of temperature sensitive influenza virus mutants defective in neuraminidase, Virology 61: 397–410.
Parodi, A. J., Pollevick, G. D., Mautner, M., Buschiazzo, A., Sanchez, D. O., and Frasch, A.C.C., 1992, Identification of the gene(s) coding for the trans-sialidase of Trypanosoma cruzi, EMBO J. 11: 1705–1710.
Paton, B. C., Schmid, B., Kustermann-Kuhn, B., Poulos, A., and Harzer, K., 1992, Additional biochemical findings in a patient and fetal sibling with a genetic defect in the sphingolipid activator protein (SAP) precursor, prosaposin, Biochem. J. 285: 481–488.
Pellegrin, J. J., Ortega-Barria, E., Barza, M., Baum, J., and Pereira, M.E.A., 1991, Neuraminidase activity in Acanthamoeba species trophozoites and cysts, Invest. Ophthalmol. Vis. Sci. 32: 3061–3066.
Pereira, M.E.A., 1983, A developmentally regulated neuraminidase activity in Trypanosoma cruzi, Science 219: 1444–1446.
Pereira, M.E.A., and Hoff, R., 1986, Heterogeneous distribution of neuraminidase activity in strains and clones of Trypanosoma cruzi and its possible association with parasitic myotropism, Mot. Biochem. Parasitol. 20: 183–189.
Pereira, M.E.A., Meija, S., Ortega-Barria, E., Matzilevitch, 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. 175: 179–191.
Perillo, M., Yu, R. K., and Maggio, B., 1994, Modulation of the activity of Clostridium perfringens neuraminidase by the molecular organization of gangliosides in monolayers, Biochim. Biophys. Acta 1193: 155–164.
Pilatte, Y., Bignon, J., and Lambre, C. R., 1987, Lysosomal and cytosolic sialidases in rabbit alveolar macrophages: Demonstration of increased lysosomal activity after in vivo activation with bacillus Calmette-Guerin, Biochim. Biophys. Acta 923: 150–155.
Pitto, M., Chigomo, V., Giglioni, A., Valsecchi, M., and Tettamanti, G., 1989, Sialidase in cerebellar granule cells differentiating in culture, J. Neurochem. 53: 1464–1470.
Pitto, M., Giglioni, A., and Tettamanti, G., 1992, Dual subcellular localization of sialidase in cultured granule cells differentiated in culture, Neurochem. Int. 21: 367–374.
Portner, A., Scroggs, R. A., and Metzger, D. W., 1987, Distinct functions of antigenic sites of the HN glycoprotein of Sendai virus, Virology 158: 61–68.
Portoukalian, J., and Bouchon, B., 1986, Hydrolysis of all gangliosides, including GM1 and GM2, on thin-layer plates by Vibrio cholerae neuraminidase, J. Chromatogr. 380: 386–392.
Post, J. A., 1992, Removal of sarcolemmal sialic acid residues results in a loss of sarcolemmal functioning and integrity, Am. J. Physiol. 263: H147 - H152.
Potier, M., 1988, Structure of the lysosomal sphingolipid activator protein 1 by homology with influenza virus neuraminidase, Biochem. Biophys. Res. Commun. 155: 32–37.
Potier, M., Mameli, L., Belisle, M., Dallaire, L., and Melancon, S. B., 1979, Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-a-u-N-acetylneuraminate) substrate, Anal. Biochem. 94: 287–296.
Potier, M., Michaud, L., Tranchemontagne, J., and Thauvette, L., 1990a, Structure of the lysosomal neuraminidase—ß-galactosidase—carboxypeptidase multienzymic complex, Biochem. J. 267: 197–202.
Potier, M., Lamotagne, S., Michaud, L., and Tranchemontagne, J., I 990b, Human neuraminidase is a 60-kDa processing product of prosaposin, Biochem. Biophys. Res. Commun. 173: 449–456.
Previato, J. O., Andrade, A. F., Pessolani, M. C., and Mendoca-Previato, L., 1985, Incorporation of sialic acid into Trypanosoma cruzi macromolecules. A proposal for a new metabolic route, Mol. Biochem. Parasitol. 16: 85–96.
Priori, R. P., Mejia, J. S., and Pereira, M.E.A., 1990, Monoclonal antibodies against Trypanosoma cruzi neuraminidase reveal enzymes polymorphism, recognize a subset of trypomastigotes, and enhance infection in vitro, J. Immunol. 144: 4384–4391.
Priori, R. P., Mejia, J. S., and Pereira, M.E.A., 1991, Trypanosoma cruzi: Localization of neuraminidase on the surface of trypomastigotes, Trop. Med. Parasitol. 42: 146–150.
Puri, A., Grimaldi, S., and Blumenthal, R., 1992, Role of viral envelope sialic acid membrane fusion mediated by the vesicular stomatitis virus envelope glycoprotein, Biochemistry 31: 10108–10113.
Recio-Pinto, E., Thornhill, W. B., Duch, D. S., Levinson, S. R., and Urban, B. W., 1990, Neuraminidase treatment modifies the function of electroplax sodium channels in planar lipid bilayers, Neuron 5: 675–684.
Riboni, L., Sonnino, S., Acquotti, D., Malesci, A., Ghidoni, R., Egge, H., Mingrino, S., and Tettamanti, G., 1986, Natural occurrence of ganglioside lactones. Isolation of GD1b inner ester from adult human brain, J. Biol. Chem. 261: 8514–8519.
Riboni, L., Prinetti, A., Bassi, R., and Tettamanti, G., 1991, Cerebellar granule cells in culture exhibit a ganglioside-sialidase presumably linked to the plasma membrane, FEBS 287: 42–46.
Rogerieux, F., Belaise, M., Terzidis-Trabelsi, H., Greffard, A., Pilatte, Y., and Lambre, C. R., 1993, Determination of the sialic acid linkage specificity of sialidase using lectins in a solid phase assay, Anal. Biochem. 211: 200–204.
Roggentin, P., Berg, W., and Schauer, R., 1987, Purification and characterization of sialidase from Clostridium sordeii G12, Glycoconj. J. 4: 349–359.
Roggentin, P., Rothe, B., Lottspeich, F., and Schauer, R., 1988a, Cloning and sequencing of a Clostridium perfringens sialidase gene, FEBS Lett. 238: 31–34.
Roggentin, P., Gutschker-Gdaniec, G.H.M., Hobrecht, R., and Schauer, R., 1988b, Early diagnosis of clostridial gas gangrene using sialidase antibodies, Clin. Chim. Acta 173: 251–262.
Roggentin, P., Rothe, B., Kaper, J. B., Galen, J., Lawrisuk, L., Vimr, E. R., and Schauer, R., 1989, Conserved sequences in bacterial and viral sialidases, Glycoconj. J. 6: 349–353.
Roggentin, P., Hobrecht, R., Tirpitz, D., Rothe, B., and Schauer, R., 1991, Application of sialidase antibodies for the diagnosis of clostridia] infections, Clin. Chim. Acta 196: 97–106.
Roggentin, T., Kleineidam, R. G., Schauer, R., and Roggentin, P., 1992, Effects of site-specific mutations on the enzymatic properties of a sialidase from Clostridium perfringens, Glycoconj. J. 9: 235–240.
Roggentin, T., Kleineidam, R. G., Majewski, D. M., Tirpitz, D., Roggentin, P., and Schauer, R., 1993, An immunoassay for the rapid and specific detection of three sialidase-producing clostridia causing gas gangrene, J. Immunol. Methods 157: 125–133.
Rosenberg, A., 1981, Cell surface sialidase, in: Perspectives in Inherited Metabolic Diseases, Vol. IV, ( G. Tettamanti, P. Duran, and S. di Donato, eds.), Edi. Emeres, Milan, pp. 111–124.
Rosenberg, A., and Schengrund, C. L., 1976, Sialidases, in: Biological Roles of Sialic Acid, ( A. Rosenberg and C. L. Schengrund, eds.), Plenum Press, New York, pp. 295–359.
Rosenberg, 1. A., Prioli, R. P., Ortega-Barria, E., and Pereira, M. E. A., 1991, Stage-specific phospholipase C-mediated release of Trypanosoma cruzi neuraminidase, Mol. Biochem. Parasitol. 46: 303–306.
Rothe, B., Roggentin, P., Frank, R., Blocker, H., and Schauer, R., 1989, Cloning, sequencing and expression of a sialidase gene from Clostridium sordellii G12, J. Gen. Microbiol. 135: 3087–3096.
Rothe, B., Rothe, B., Roggentin, P., and Schauer, R., 1991, The sialidase gene from Clostridium septicum: Cloning, sequencing, expression in Escherichia coli and identification of conserved sequences in sialidase and other proteins, Mol. Gen. Genet. 226: 190–197.
Russo, T. A., Thompson, J. S., Godoy, V. G., and Malamy, M. H., 1990, Cloning and expression of the Bacteroides fragilis TAL2480 neuraminidase gene, nanH, in Escherichia coli, J. Bacteriol. 172: 2594–2600.
Sagawa, J., Miyagi, T., and Tsuiki, S., 1988, Membrane-associated sialidase of rat liver and its decrease in hepatomas, Jpn. J. Cancer Res. (Gann) 79: 69–73.
Sagawa, J., Miyagi, T., and Tsuiki, S., 1990, Characterization of the major sialidases of various types of rats blood cells: Their comparison with rat liver sialidases, J. Biochem. 107: 452–456.
Saito, M., and Yu, R. K., 1986, Further characterization of a myelin-associated neuraminidase: Properties and substrate specificity, J. Neurochem. 47: 632–641.
Saito, M., and Yu, R. K., 1992, Role of myelin-associated neuraminidase in the ganglioside metabolism of rat brain myelin, J. Neurochem. 58: 83–87.
Saito, M., and Yu, R. K., 1993, Possible role of myelin-associated neuraminidase in membrane adhesion, J. Neurosci. Res. 36: 127–132.
Saito, M., Sugano, K., and Nagai, Y., 1979, Action of Arthrobacter ureafaciens sialidase on sialoglycolipid substrates, J. Biol. Chem. 254: 7845–7854.
Saito, M., Kasai, N., and Yu, R. K., 1985, In situ immunological determination of basic carbohydrate structures of gangliosides on thin-layer plates, Anal. Biochem. 148: 54–58.
Saito, M., Sato-Bibbee, C., and Yu, R. K., 1992, Neuraminidase activities in oligodendroglia cells of the rat brain, J. Neurochem. 58: 78–82.
Saito, M., Tanaka, Y., Tang, C.-P., Yu, R. K., and Ando, S., 1995, Characterization of sialidase activity in mouse synaptic plasma membranes and its age-related changes, J. Neurosci. Res. 40: 401–406.
Saito, T., Kawaoka, Y., and Webster, R. G., 1993, Phylogenetic analysis of the N8 neuraminidase gene of influenza A viruses, Virology 193: 868–876.
Sakurada, K., Ohta, T., and Hasegawa, M., 1992, Cloning, expression, and characterization of the Micromonospora viridifaciens neuraminidase gene in Streptomyces lividans, J. Bacteriol. 174: 6896–6903.
Sandhoff, K., and Pallmann, B., 1978, Membrane-bound neuraminidae from calf brain: Regulation of oligosialoganglioside degradation by membrane fluidity and membrane components, Proc. Natl. Acad. Sci. USA 75: 122–126.
Sandhoff, K., Schraven, J., and Nowoczek, G., 1976, Effect of xenon, nitrous oxide and halothane on membrane-bound sialidase from calf brain, FEBS Lett. 62: 284–287.
Sato, A., Hiramatsu, M., Kashimata, M., Murayama, M., Minami, N., and Minami, N., 1989, Characterization of sialidase in the rat salivary glands, Enzymes 41: 200–208.
Sauto-Padron, T., Harth, G., and de Souza, W., 1990, Immunocytochemical localization of neuraminidase in Trypanosoma cruzi, Infect. Immun. 58: 586–592.
Scarsdale, J. N., Prestegard, J. H., and Yu, R. K., 1990, NMR computational studies of interactions between remote residues in gangliosides, Biochemistry 29: 9843–9855.
Schauer, R., 1982, Chemistry, metabolism, and biological functions of sialic acid, Adv. Carbohydr. Chem. Biochem. 40: 131–234.
Schauer, R., 1983, Glycosidases with special reference to the pathophysiological role of sialidase, in: Structural Carbohydrates of the Liver, (H. Popper, W. Reutter, F. Gudat, and E. Kottgen, eds. ), MTP Press, pp. 83–97.
Schauer, R., 1985, Sialic acid and their role as biological masks, Trends Biochem. Sci. 9: 357–360.
Schauer, R., 1991, Biosynthesis and function of N- and 0-substituted sialic acids, Glycobiology 1: 449–452.
Schauer, R., and Wember, M., 1984, Isolation and characterization of an oligosaccharide-and glycoprotein-specific sialidase from human leucocytes, Hoppe-Seyler’s Z. Physiol. Chem. 365: 419–426.
Schauer, R., and Wember, M., 1989, Isolation and characterization of a sialidase from the starfish Asterias rubens, Biol. Chem. Hoppe-Seyler 370: 183–190.
Schauer, R., Veh, R. W., Sander, M., Corfield, A. P., and Wiegandt, H., 1980, Neuraminidaseresistant sialic acid residues of gangliosides, Adv. Exp. Med. Biol. 125: 283–294.
Schauer, R., Fischer, C., Kluge, A., Lee, H., and Ruch, B., 1990, Mechanism of binding and uptake of sialidase-treated blood cells and glycoproteins by the galactose-specific receptor of rat peritoneal macrophages, Biomed. Biochim. Acta 49: S230 - S235.
Scheel, G., Acevedo, E., Conzelmann, E., Nehrkorn, H., and Sandhoff, K., 1982, Model for the interaction of membrane-bound substrates and enzymes: Hydrolysis of gangliosides GD1a by sialidase of neural membranes isolated from calf brain, Eur. J. Biochem. 127: 245–253.
Scheel, G., Schwarzmann, G., Hoffmann-Bleihauer, P., and Sandhoff, K., 1985, The influence of ganglioside insertion into brain membranes on the rate of ganglioside degradation by membranebound sialidase, Eur. J. Biochem. 153: 29–35.
Scheibe, R., Hein, K., and Wenzel, K. W., 1990, Lysosomal ß-galactosides from rat liver: Purification, molecular forms and association with neuraminidase, Biomed. Biochim. Acta 49: 547–556.
Scheid, A., and Choppin, P. W., 1974, Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis, and infectivity by proteolytic cleavage of an inactive precursor protein of Sendai virus, Virology 57: 475–490.
Scheid, A., Caliguiri, L. A., Compans, R. W., and Choppin, P. W., 1972, Isolation of paramyxovirus glycoprotein: Association of both hemagglutinin and neuraminidase activities with the larger SV5 glycoprotein, Virology 50: 640–652.
Schengrund, C.-L., 1990, The role(s) of gangliosides in neural differentiation and repair: A prospective, Brain Res. Bull. 24: 131–141.
Schengrund, C.-L., and Nelson, J. T., 1975, Influence of cation concentration of the sialidase activity of neuronal synaptic membranes, Biochem. Biophys. Res. Commun. 63: 217–223.
Schengrund, C.-L., and Nelson, J. T., 1976, Ganglioside sialidase activity in bovine neuronal perikarya, Neurochem. Res. 1: 171–180.
Schengrund, C.-L., and Repman, M. A., 1982, Density-dependent changes in gangliosides and sialidase activity of murine neuroblastoma cells, J. Neurochem. 39: 940–947.
Schengrund, C.-L., and Rosenberg, A., 1970, Intracellular location and properties of bovine brain sialidase, J. Biol. Chem. 245: 6196–6200.
Schengrund, C.-L., Jensen, D. S., and Rosenberg, A., 1972, localization of sialidase in the plasma membrane of rat liver cells, J. Biol. Chem. 247: 2742–2746.
Schengrund, C.-L., Lausch, R. N., and Rosenberg, A., 1973, Sialidase activity in transformed cells, J. Biol. Chem. 248: 4424–4428.
Schengrund, C.-L., Rosenberg, A., and Repman, M. A., 1976, Ecto-ganglioside-sialidase activity of herpes simpex virus transformed hamster embryo fibroblasts, J. Cell Biol. 70: 555–561.
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.
Schiller, H., Segler, K., Jeserich, G., Rosner, H., and Rahmann, H., 1979, Properties of membrane-hound neuraminidase in the developing trout brain, Life Sci. 25: 2029–2033.
Schneider-Jakob, H. R., and Cantz, M., 1991, Lysosomal and plasma membrane gangliosides GM3 sialidases of cultured human fibroblasts, Biol. Chem. Hoppe-Seyler 372: 443–450.
Schwarzmann, G., 1978, A simple and novel method for tritium labelling of gangliosides and other sphingolipids, Biochim. Biophys. Acta 529: 105–114.
Scudder, P., Doom, J. P., Chuenkova, M., Manger, I. D., and Pereira, M. E., 1993, Enzymatic characterization of 3-D-galactoside cx2,3-trans-sialidase from Trypanosoma cruzi, J. Biol. Chem. 268: 9886–9891.
Segler-Stahl, K., Rosner, H., and Rahmann, H., 1981, Membrane-bound neuraminidase in the developing mouse brain, Life Sci. 29: 1363–1367.
Shaw, M. W., Lamb, R. A., Erickson, B. W., Briedis, D. J., and Choppin, P. W., 1982, Complete nucleotide sequence of the neuraminidase gene of influenze B virus, Proc. Natl. Acad. Sci. USA 79: 6817–6821.
Sheehan, J. P., and Iorio, R. M., 1992, A single acid substitution in the hemagglutinin-neuraminidase of Newcastle disease virus results in a protein deficient in both functions, Virology 189: 778–781.
Shibata, H., Kanda, T., Hazama, A., Adachi, A., and Matsumoto, M., 1981, Parainfluenza 3 virus: Plaque-type variants lacking neuraminidase activity, Infect. Immun. 34: 262–267.
Srivastava, P. N., and Abou-issa, H., 1977, Purification and properties of rabbit spermatozoa acrosomal neuraminidase, Biochem. J. 161: 193–200.
Stenberg, P., Levin, J., Baker, G., Mok, Y., and Corash, L., 1991, Neuraminidase-induced thrombocytopenia in mice: Effects on thrombopoiesis, J. Cell. Physiol. 147: 7–16.
Straus, D. C., Unbehagen, P. J., and Purdy, C. W., 1993, Neuraminidase production by a Pasteurella haemolytica Al: Strain associated with bovine pneumonia, Infect. Immun. 61: 253–259.
Suttajit, M., and Winzler, R., 1971, Effect of modification of N-acetylneuraminic acid on the binding of glycoprotcins to influenza virus and on susceptibility to cleavage by neuraminidase, J. Biol. Chem. 246: 3398–3404.
Suzuki, K., 1993, Genetic disorders of lipid, glycoprotein, and mucopolysaccharide metabolism, in: Basic Neurochemistry, 5th ed. ( G. J. Siegel, B. W. Argaroff, R. W. Albers, and P. B. Molinoff, eds.), Raven Press, New York, pp. 793–812.
Taha, B., and Carubelli, R., 1967, Mammalian neuraminidase: Intracellular distribution and changes of enzyme activity during location, Arch. Biochem. Biophys. 119: 55–61.
Taira, S., and Nariuchi, H., 1988, Possible role of neuraminidase in activated T cells in the recognition of allogeneic Ia, J. Immunol. 141: 440–446.
Takahashi, T., Ryan, K. W., and Portner, A., 1992, Expression of cDNA encoding the Sendai virus hemagglutinin-neuraminidase gene: Characterization of wild-type mutant gene products, Virology 187: 837–840.
Taki, T., Nishiwaki, S., Ishii, K., and Handa, S., 1990, A simple and specific assay of glycosyltransferase and glycosidase activities by an enzyme linked immunosorbent assay method, and its application to assay of galactosyltransferase activity in sera from patients with cancer, J. Biochem. 107: 493–498.
Tallman, J. F., and Brady, R. O., 1973, The purification and properties of a mammalian neuraminidase (sialidase), Biochim. Biophys. Acta 293: 434–443.
Tanaka, H., Ito, F., and Iwasaki, T., 1992, Purification and characterization of sialidase from Bacteroides fragilis SBT3182, Biochem. Biophys. Res. Commun. 189: 524–529.
Tanaka, H., Ito, F., and Iwasaki, T., 1994, Two sialidases which preferentially hydrolyze sialyl a2–8 linkage from Bacteroides fragilis SBT3182, J. Biochem. 115: 318–321.
Taylor, G., Vimr, E., Garman, E., and Laver, G., 1992a, Purification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2, J. Mol. Biol. 226: 1287–1290.
Taylor, G., Dineley, L., Glowka, M., and Laver, G., 1992b, Crystallization and preliminary crystallographic study of neuraminidase from Micromonospora viridifaciens, J. Mol. Biol. 225: 1135–1136.
Taylor, G., Garman, E., Webster, R., Saito, T., and Laver, G., 1993, Crystallization and preliminary X-ray studies of influenza A virus neuraminidase of subtype N5, N6, N8, and N9, J. Mol. Biol. 230: 345–348.
Terzidis-Trabelsi, H., Pilatte, Y., Greffard, A., Bignon, J., and Lambre, C., 1991, Sialidase in the guinea pig pulmonary parenchyma: Increased activity in the cytosolic and microsomal subcellular fractions after stimulation with bacillus Calmette Guerin, Biol. Chem. Hoppe-Seyler 372: 437–442.
Tettamanti, G., and Zambotti, V., 1968, Purification of neuraminidase from pig brain and its action on different gangliosides, Enzymologia 35: 61–74.
Tettamanti, G., Preti, A., Lombardo, A., Gasparini, M., and Zambotti, V., 1972, Assay of brain particulate neuraminidase III. Preparation of the enzyme devoid of endogenous substrates, Biochim. Biophys. Acta 258: 228–237.
Tettamanti, G., Preti, A., Lombardo, A., Suman, T., and Zambotti, V., 1975, Membrane-bound neuraminidase in the brain of different animals: Behavior of the enzymes on endogenous sialo derivatives and rationale for its assay, J. Neurochem. 25: 451–456.
Teufel, M., Roggentin, P., and Schauer, R., 1989, Properties of sialidase isolated from Actinomyces viscosus DSM 43798, Biol. Chem. Hoppe-Seyler 370: 435–443.
Thomas, J. J., Folgler, E. C., Nist, D. L., Thomas, B. J., and Jones, R. H., 1978, Km values of influenza virus neuraminidases for a new fluorogenic substrate, 4-methylumbelliferone N-acetylneuraminic acid ketoside, Anal. Biochem. 88: 461–467.
True, D., Singer, M. S., Lasky, L. A., and Rosen, S. D., 1990, Requirement for sialic acid on the endothelial ligand of a lymphocyte homing receptor, J. Cell Biol. 111: 2757–2764.
Tsuji, S., Yamauchi, T., Hiraiwa, M., Isobe, T., Okuyama, T., Sakimura, K., Takahashi, Y., Nishizuka, M., Uda, Y., and Miyatake, T., 1989, Molecular cloning of a full-length cDNA for human a-N-acetylgalactosaminidase (a-galactosidase B), Biochem. Biophys. Res. Commun. 163: 1498–1504.
Tulip, W. R., Varghese, J. N., Baker, A. T., Van Donkelaar, A., Laver, W. G., Webster, R. G., and Colman, P. M., 1991, Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants, J. Mol. Biol. 221: 487–497.
Tulip, W. R., Varghese, J. N., Laver, W. G., Webster, R. G., and Colman, P. M., 1992a, Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex, J. Mol. Biol. 227: 122–148.
Tulip, W. R., Varghese, J. N., Webster, R. G., Laver, W. G., and Colman, P. M., 1992b, Crystal structures of two mutant neuraminidase—antibody complexes with amino acid substrates in the interface, J. Mol. Biol. 227: 149–159.
Tulsiani, D.R.P., and Carubelli, R., 1971, Studies on the soluble and lysosomal neuraminidase of rat mammary glands, Biochim. Biophys. Acta 227: 139–153.
Tuppy, H., and Palese, P., 1969, A chromogenic substrate for the investigation of neuraminidase, FEBS Lett. 3: 72–75.
Uchida, Y., Tsukada, Y., and Sugimori, T., 1977, Distribution of neuraminidase in Arthrobacter and its purification by affinity chromatography, J. Biochem. 82: 1425–1433.
Uchida, Y., Tsukada, Y., and Sugimori, T., 1979, Enzymatic properties of neuraminidase from Arthrobacter ureafaciens, J. Biochem. 86: 1573–1585.
Uemura, H., Schenkman, S., Nussenzweig, 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.
Usuki, S., Lyu, S.-C., and Sweeley, C. C., 1988a, Sialidase activities of cultured human fibroblasts and the metabolism of GM3 ganglioside, J. Biol. Chem. 263: 6847–6853.
Usuki, S., Hoops, P., and Sweeley, C. C., 1988b, Growth control of human foreskin fibroblasts and inhibition of extracellular sialidase activity by 2-deoxy-2,3-dehydro-N-acetylneuraminic acid, J. Biol. Chem. 263: 10595–10599.
Vaheri, A., Ruoslahti, E., and Nordling, S., 1972, Neuraminidase stimulates division and sugar uptake in density-inhibited cell cultures, Nature New Biol. 238: 211–212.
van Aswegen, C. H., Van Resburg, H.G.J., Becker, P. J., Wittliff, J. L., and Du Plessis, D. J., 1990, Influence of sialic acid on the binding activity of estrogen receptors, Clin. Physiol. Biochem. 8: 169–178.
van der Horst, G.T.J., Galjart, N. T., d’Azzo, A., Galjaard, H., and Verheijen, F. W., 1989, Identification and in vitro reconstitution of lysosomal neuraminidase from human placenta, J. Biol. Chem. 264: 1317–1322.
van der Horst, G.T.J., Mancini, G.M.S., Brossmer, R., Rose, U., and Verheijen, F. W., 1990a, Photoaffinity labeling of a bacterial sialidase with an aryl azide derivative of sialic acid, J. Biol. Chem. 265: 10801–10804.
Vandekerckhove, F., Schenkman, S., de Carvalho, P. L., Tomlinson, S., Kiso, M., Yoshida, M., Hasegawa, A., and Nussenzweig, V., 1992, Substrate specificity of the Trypanosoma cruzi transsialidase, Glycobiology 2: 541–548.
van der Horst, G.T.J., Rose, U., Brossmer, R., and Verheijen, F. W., 1990b, Photoaffinity labeling of the lysosomal neuraminidase from bovine testis, FEBS Lett. 277: 42–44.
van Dessel, G., De Wolf, M., Lagrou, A., Hilderson, H., and Dierick, W., 1984, Characterization, purification, and subcellular localization of bovine thyroid sialidases, J. Biochem. 96: 937–947.
van Lenten, L., and Ashwell, G., 1971, Studies on the chemical and enzymatic modification of glycoproteins, J. Biol. Chem. 246: 1889–1894.
Varghese, J. N., and Colman, P. M., 1991, Three-dimensional structure of the neuraminidase of minfluenza virus A/Tokyo/3/67 at 2.2 A resolution, J. Mol. Biol. 221: 473–486.
Varghese, J. N., Laver, W. G., and Colman, P. M., 1983, Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution, Nature 303: 35–40.
Varghese, J. N., McKimm-Breschkin, J. L., Caldwell, J. B., Kortt, A. A., and Colman, P. M., 1992, The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor, Proteins 14: 327–332.
Varki, A., 1992, Diversity in the sialic acids, Glycobiology 2: 25–40.
Veh, R. W., Corfield, A. P., Sander, M., and Schauer, R., 1977, Neuraminic acid-specific modification and tritium labeling of gangliosides, Biochim. Biophys. Acta 486: 145–160.
Venerando, B., Tettamanti, G., Cestaro, B., and Zambotti, V., 1975, Studies on brain cytosol neuraminidase. I. Isolation and partial characterization of two forms of the enzyme from pig brain, Biochim. Biophys. Acta 403: 461–472.
Venerando, B., Preti, A., Lombardo, A., Cestaro, B., and Tettamanti, G., 1978, Studies on brain cytosol neuraminidase. II. Extractability, solubility and intraneuronal distribution of the enzyme in pig brain, Biochim. Biophys. Acta 527: 17–30.
Venerando, B., Goi, G. C., Preti, A., Fiorilli, A., Lombardo, A., and Tettamanti, G., 1982, Cytosolic sialidase in developing rat forebrain, Neurochem. Int. 4: 313–320.
Venerando, B., Fiorilli, A., Malesci, A., Goi, G. C., Lombardo, A., Preti, A., and Tettamanti, G., 1983, Cytosolic sialidase from the nerve ending of developing rat forebrain, Neurochem. Int. 5: 619–624.
Venerando, B., Fiorilli, A., Masserini, M., Giuliani, A., and Tettamanti, G., 1985, Interaction of pig brain cytosolic sialidase with gangliosides. Formation of catalytically inactive enzymeganglioside complexes, Biochim. Biophys. Acta 833: 82–92.
Venerando, B., Fiorilli, A., Caimi, L., and Tettamanti, G., 1987, Interaction of pig brain cytosolic sialidase with gangliosides. The formation of catalytically inactive enzyme—ganglioside complexes required homogenous ganglioside micelles and is a resensible phenomenon, J. Biochem. 102: 1167–1176.
Verheijen, F., Brossmer, R., and Galjaard, H., 1982, Purification of 3-galactosidase and acid neuraminidase from bovine testis: Evidence for an enzyme complex, Biochem. Biophys. Res. Commun. 108: 868–875.
Verheijen, F. W., Janse, H. C., Van Diggelen, O. P., Bakker, H. D., Loonen, M.B.C., Durand, P., and Galjaard, H., 1983, Two genetically different MU-NANA neuraminidases in human leucocytes, Biochem. Biophys. Res. Commun. 117: 470–478.
Verheijen, F. W., Palmeri, S., Hoogeveen, T., and Galjaard, H., 1985, Human placental neuraminidase: Activation, stabilization and association with ß-galactosidase and its protective protein, Eur. J. Biochem. 149: 315–321.
Verheijen, F. W., Palmeri, S., and Galjaard, H., 1987, Purification and partial characterization of lysosomal neuraminidase from human placenta, Eur. J. Biochem. 162: 63–67.
Vimr, E. R., Lawrisuk, L., Galen, J., and Kaper, J. B., 1988, Cloning and expression of the Vibrio cholerae neuraminidase gene nanH in Escherichia coli, J. Bacteriol. 170: 1495–1504.
Visser, A., and Emmelot, P., 1973, Studies on plasma membranes, J. Membr. Biol. 14: 73–84.
von Itzstein, M., Wu, W-Y., Kok, G. B., Pegg, M. S., Dyason, J. C., Jin, B., Phan, T. V., Smythe, M. L., White, H. F., Oliver, S. W., Colman, P. M., Vargese, J. N., Ryan, D. M., Woods, J. M., Bethell, R. C., Hotham, V. J., Cameron, J. M., and Penn, C. R., 1993, Rational design of potent sialidase-based inhibitors of influenza virus replication, Science, 363: 418–423.
Ward, C. W., Elleman, T. C., and Azad, A. A., 1982, Amino acid sequence of the pronase-released heads of neuraminidase subtype N2 from the Asian strain A/Tokyo/3/67 of influenza virus, Biochem. J. 207: 91–95.
Warner, T. G., and O’Brien, J. S., 1979, Synthesis of 2’-(4-methylumbelliferyl)-a-D-N-acetylneuraminic acid and detection of skin fibroblast neuraminidase in normal humans and in sialidosis, Biochemistry 18: 2783–2786.
Warner, T. G., Louie, A., and Potier, M., 1990, Photolabeling of the a-neuraminidase/ 3-galactosidase complex from human placenta with a photoreactive neuraminidase inhibitor, Biochem. Biophys. Res. Commun. 173: 13–19.
Warner, T. G., Harris, R., McDowell, R., and Vimr, E. R., 1992, Photolabeling of Salmonella typhimurium LT2 sialidase, Biochem. J. 285: 957–964.
Warren, L., 1959, The thiobarbituric acid assay of sialic acids, J. Biol. Chem. 234: 1971–1975.
Warren, L., and Spearing, C. W., 1960, Mammalian sialidase (neuraminidase), Biochem. Biophys. Res. Commun. 3: 489–492.
Werner, G., Addick, K., Fricke, U., Klaus, W., Sarram, M., and Gielen, W., 1991, Sialic acid removal modulates the myocardial and vascular activity of calcium channel ligands, Biochem. Pharmacol. 42: S77 - S87.
Wille, W., and Trenkner, E., 1981, Changes in particulate neuraminidase activity during normal and staggerer mutant mouse development, J. Neurochem. 37: 443–446.
Wrigley, N. G., Skehel, J. J., Charlwood, P. A., and Brand, C. M., 1973, The size and shape of influenza virus neuraminidase, Virology 51: 525–529.
Wu, G., and Ledeen, R. W., 1991, Stimulation of neurite outgrowth in neuroblastoma cells by neuraminidase: Putative role of GM ganglioside in differentiation, J. Neurochem. 56: 95–103.
Xu, G., Suzuki, T., Hanagata, G., Deya, E., Kiso, M., Hasegawa, A., and Suzuki, Y., 1993, Drift of the sialyl-linkage specific recognition of the sialidase of influenza B virus isolates, J. Biochem. 113: 304–307.
Yamada, T., Tsuji, S., and Miyatake, T., 1983, Lysosomal sialidase deficiency in sialidosis with partial p-galactosidase deficiency, Biochim. Biophys. Acta 755: 106–111.
Yamamoto, Y., and Nishimura, K., 1987, Copurification and separation of ß-galactosidase and sialidase from porcine testis, Int. J. Biochem. 19: 435–442.
Yee, H. F., Kuwata, J. H., and Langer, G. A., 1991, Effects of neuraminidase on cellular calcium and contraction in cultured cardiac myocytes, J. Mol. Cell. Cardiol. 23: 175–185.
Yeung, M. K., 1993, Complete nucleotide sequence of the Actinomyces viscosus T14V sialidase gene: Presence of a conserved repeating sequencing among strain of Actinomyces spp., Infect. Immun. 61: 109–116.
Yeung, M., and Fernandez, S. R., 1991, Isolation of a neuraminidase gene from Actinomyces viscosus T14V, Appl. Environ. Microbiol. 57: 3062–3069.
Yohe, H. C., and Rosenberg, A., 1977, Action of intrinsic sialidase of rat brain synaptic membranes on membrane sialolipid and sialoprotein components in situ, J. Biol. Chem. 252: 2412–2418.
Yohe, H. C., and Rosenberg, A., 1978, Effect of neurotoxic divalent cations on the activity of the intrinsic nerve ending membrane associated sialidase of bovine brain, Neurochem. Res. 3: 101–113.
Yohe, H. C., Jacobson, R. I., Yu, R. K., 1983, Ganglioside—basic protein interaction: Protection of gangliosides against neuraminidase action, J. Neurosci. 9: 401–412.
Yohe, H. C., Saito, M., Ledeen, R. W., Kunishita, T., Sclafani, J. R., and Yu, R. K., 1986, Further evidence for an intrinsic neuraminidase in CNS myelin, J. Neurochem. 46: 623–629.
Yu, R. K., and Ledeen, R. W., 1969, Configuration of the ketosidic bond of sialic acid, J. Biol. Chem. 244: 1306–1313.
Yu, R. K., Koerner, T.A.W., Ando, S., and Prestegard, J. H., 1985, High-resolution proton NMR studies of gangliosides. 3. Elucidation of the structure of ganglioside GM3-lactone, J. Biochem. 98: 1367–1373.
Zeigler, M., and Bach, G., 1981, Cellular localization of neuraminidase in cultured human fibroblasts, Biochem. J. 198: 505–508.
Zeigler, M., Sury, V., and Bach, G., 1989, The identification of lysosomal ganglioside sialidase in human cells, Eur. J. Biochem. 183: 455–458.
Zingales, B., Carniol, R., de Lederkremer, R. M., and Col li, W., 1987, Direct sialic acid transfer from a protein donor to glycolipids of trypomastigote forms of Trypanosoma cruzi, Biochem. Parasitol. 26: 35–144.
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Saito, M., Yu, R.K. (1995). Biochemistry and Function of Sialidases. In: Rosenberg, A. (eds) Biology of the Sialic Acids. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9504-2_8
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