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Volumn , Issue , 2009, Pages 585-598

Sialic acid-specific microbial lectins

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EID: 84881706662     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374546-0.00029-8     Document Type: Chapter
Times cited : (3)

References (81)
  • 2
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related ?-keto acids: An evolutionary perspective
    • Angata T., Varki A. Chemical diversity in the sialic acids and related ?-keto acids: an evolutionary perspective. Chem. Rev. 2002, 102:439-469.
    • (2002) Chem. Rev , vol.102 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 3
    • 0036662069 scopus 로고    scopus 로고
    • Molecular biology of rotavirus cell entry
    • Arias C.F., Isa P., Guerrero C.A., et al. Molecular biology of rotavirus cell entry. Arch. Med. Res. 2002, 33:356-361.
    • (2002) Arch. Med. Res , vol.33 , pp. 356-361
    • Arias, C.F.1    Isa, P.2    Guerrero, C.A.3
  • 4
    • 33750489397 scopus 로고    scopus 로고
    • SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans
    • Aspholm M., Olfat F.O., Norden J., et al. SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. PLoS Pathog. 2006, 2:e110.
    • (2006) PLoS Pathog , vol.2 , pp. e110
    • Aspholm, M.1    Olfat, F.O.2    Norden, J.3
  • 5
    • 36249026299 scopus 로고    scopus 로고
    • Crystal structures of the staphylococcal toxin SSL5 in complex with sialyl Lewis X reveal a conserved binding site that shares common features with viral and bacterial sialic acid binding proteins
    • Baker H.M., Basu I., Chung M.C., Caradoc-Davies T., Fraser J.D., Baker E.N. Crystal structures of the staphylococcal toxin SSL5 in complex with sialyl Lewis X reveal a conserved binding site that shares common features with viral and bacterial sialic acid binding proteins. J. Mol. Biol. 2007, 374:1298-1308.
    • (2007) J. Mol. Biol , vol.374 , pp. 1298-1308
    • Baker, H.M.1    Basu, I.2    Chung, M.C.3    Caradoc-Davies, T.4    Fraser, J.D.5    Baker, E.N.6
  • 6
    • 24344459117 scopus 로고    scopus 로고
    • Identification of a new sialic acid-binding protein in Helicobacter pylori
    • Bennett H.J., Roberts I.S. Identification of a new sialic acid-binding protein in Helicobacter pylori. FEMS Immunol. Med. Microbiol. 2005, 44:163-169.
    • (2005) FEMS Immunol. Med. Microbiol , vol.44 , pp. 163-169
    • Bennett, H.J.1    Roberts, I.S.2
  • 7
    • 33847757520 scopus 로고    scopus 로고
    • Insight into host cell carbohydrate-recognition by human and porcine rotavirus from crystal structures of the virion spike associated carbohydrate-binding domain (VP8)
    • Blanchard H., Yu X., Coulson B.S., von Itzstein M. Insight into host cell carbohydrate-recognition by human and porcine rotavirus from crystal structures of the virion spike associated carbohydrate-binding domain (VP8). J. Mol. Biol. 2007, 367:1215-1226.
    • (2007) J. Mol. Biol , vol.367 , pp. 1215-1226
    • Blanchard, H.1    Yu, X.2    Coulson, B.S.3    von Itzstein, M.4
  • 9
    • 3142729320 scopus 로고    scopus 로고
    • Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites
    • Burmeister W.P., Guilligay D., Cusack S., Wadell G., Arnberg N. Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites. J. Virol. 2004, 78:7727-7736.
    • (2004) J. Virol , vol.78 , pp. 7727-7736
    • Burmeister, W.P.1    Guilligay, D.2    Cusack, S.3    Wadell, G.4    Arnberg, N.5
  • 10
    • 0023033019 scopus 로고
    • Detection of lectin from Chrysosporium keratinophilum (Frey) carmichael and Anixiopsis stercoraria (Hansen) Hansen by inhibition of haemagglutination
    • Chabasse D., Robert R. Detection of lectin from Chrysosporium keratinophilum (Frey) carmichael and Anixiopsis stercoraria (Hansen) Hansen by inhibition of haemagglutination. Ann. Inst. Pasteur Microbiol. 1986, 137B:187-193.
    • (1986) Ann. Inst. Pasteur Microbiol , vol.137 B , pp. 187-193
    • Chabasse, D.1    Robert, R.2
  • 11
    • 40549083360 scopus 로고    scopus 로고
    • In meso crystal structure and docking simulations suggest an alternative proteoglycan binding site in the OpcA outer membrane adhesin
    • Cherezov V., Liu W., Derrick J.P., et al. In meso crystal structure and docking simulations suggest an alternative proteoglycan binding site in the OpcA outer membrane adhesin. Proteins 2008, 71:24-34.
    • (2008) Proteins , vol.71 , pp. 24-34
    • Cherezov, V.1    Liu, W.2    Derrick, J.P.3
  • 12
    • 36248995861 scopus 로고    scopus 로고
    • The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition
    • Chung M.C., Wines B.D., Baker H., Langley R.J., Baker E.N., Fraser J.D. The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition. Mol. Microbiol. 2007, 66:1342-1355.
    • (2007) Mol. Microbiol , vol.66 , pp. 1342-1355
    • Chung, M.C.1    Wines, B.D.2    Baker, H.3    Langley, R.J.4    Baker, E.N.5    Fraser, J.D.6
  • 13
    • 0032921275 scopus 로고    scopus 로고
    • Human and most animal rotavirus strains do not require the presence of sialic acid on the cell surface for efficient infectivity
    • Ciarlet M., Estes M.K. Human and most animal rotavirus strains do not require the presence of sialic acid on the cell surface for efficient infectivity. J. Gen. Virol. 1999, 80:943-948.
    • (1999) J. Gen. Virol , vol.80 , pp. 943-948
    • Ciarlet, M.1    Estes, M.K.2
  • 14
    • 14644401707 scopus 로고    scopus 로고
    • Function and expression of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli
    • Condemine G., Berrier C., Plumbridge J., Ghazi A. Function and expression of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli. J. Bacteriol. 2005, 187:1959-1965.
    • (2005) J. Bacteriol , vol.187 , pp. 1959-1965
    • Condemine, G.1    Berrier, C.2    Plumbridge, J.3    Ghazi, A.4
  • 16
    • 0027426946 scopus 로고
    • The surface trans-sialidase family of Trypanosoma cruzi
    • Cross G.A., Takle G.B. The surface trans-sialidase family of Trypanosoma cruzi. Annu. Rev. Microbiol. 1993, 47:385-411.
    • (1993) Annu. Rev. Microbiol , vol.47 , pp. 385-411
    • Cross, G.A.1    Takle, G.B.2
  • 17
    • 0035128179 scopus 로고    scopus 로고
    • Glycosphingolipid binding specificities of rotavirus: Identification of a sialic acid-binding epitope
    • Delorme C., Brussow H., Sidoti J., et al. Glycosphingolipid binding specificities of rotavirus: identification of a sialic acid-binding epitope. J. Virol. 2001, 75:2276-2287.
    • (2001) J. Virol , vol.75 , pp. 2276-2287
    • Delorme, C.1    Brussow, H.2    Sidoti, J.3
  • 18
    • 0036500085 scopus 로고    scopus 로고
    • The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site
    • Dormitzer P.R., Sun Z.Y., Wagner G., Harrison S.C. The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site. EMBO J. 2002, 21:885-897.
    • (2002) EMBO J , vol.21 , pp. 885-897
    • Dormitzer, P.R.1    Sun, Z.Y.2    Wagner, G.3    Harrison, S.C.4
  • 19
    • 0016819311 scopus 로고
    • Plasmid-controlled colonization factor associated with virulence in Escherichia coli enterotoxigenic for humans
    • Evans D.G., Silver R.P., Evans D.J., Chase D.G., Gorbach S.L. Plasmid-controlled colonization factor associated with virulence in Escherichia coli enterotoxigenic for humans. Infect. Immun. 1975, 12:656-667.
    • (1975) Infect. Immun , vol.12 , pp. 656-667
    • Evans, D.G.1    Silver, R.P.2    Evans, D.J.3    Chase, D.G.4    Gorbach, S.L.5
  • 20
    • 0018764294 scopus 로고
    • Purification and characterization of the CFA/I antigen of enterotoxigenic Escherichia coli
    • Evans D.G., Evans D.J., Clegg S., Pauley J.A. Purification and characterization of the CFA/I antigen of enterotoxigenic Escherichia coli. Infect. Immun. 1979, 25:738-748.
    • (1979) Infect. Immun , vol.25 , pp. 738-748
    • Evans, D.G.1    Evans, D.J.2    Clegg, S.3    Pauley, J.A.4
  • 21
    • 0035943672 scopus 로고    scopus 로고
    • The crystal structure of tetanus toxin Hc fragment complexed with a synthetic GT1b analogue suggests cross-linking between ganglioside receptors and the toxin
    • Fotinou C., Emsley P., Black I., et al. The crystal structure of tetanus toxin Hc fragment complexed with a synthetic GT1b analogue suggests cross-linking between ganglioside receptors and the toxin. J. Biol. Chem. 2001, 276:32274-32281.
    • (2001) J. Biol. Chem , vol.276 , pp. 32274-32281
    • Fotinou, C.1    Emsley, P.2    Black, I.3
  • 22
    • 0037853264 scopus 로고    scopus 로고
    • A novel erythrocyte binding antigen-175 paralogue from Plasmodium falciparum defines a new trypsin-resistant receptor on human erythrocytes
    • Gilberger T.W., Thompson J.K., Triglia T., Good R.T., Duraisingh M.T., Cowman A.F. A novel erythrocyte binding antigen-175 paralogue from Plasmodium falciparum defines a new trypsin-resistant receptor on human erythrocytes. J. Biol. Chem. 2003, 278:14480-14486.
    • (2003) J. Biol. Chem , vol.278 , pp. 14480-14486
    • Gilberger, T.W.1    Thompson, J.K.2    Triglia, T.3    Good, R.T.4    Duraisingh, M.T.5    Cowman, A.F.6
  • 23
    • 0035949581 scopus 로고    scopus 로고
    • X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs
    • Ha Y., Stevens D.J., Skehel J.J., Wiley D.C. X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proc. Natl. Acad. Sci. USA 2001, 98:11181-11186.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11181-11186
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 24
    • 0027452657 scopus 로고
    • Cloning and characterization of the S fimbrial adhesin II complex of an Escherichia coli O18:K1 meningitis isolate
    • Hacker J., Kestler H., Hoschutzky H., Jann K., Lottspeich F., Korhonen T.K. Cloning and characterization of the S fimbrial adhesin II complex of an Escherichia coli O18:K1 meningitis isolate. Infect. Immun. 1993, 61:544-550.
    • (1993) Infect. Immun , vol.61 , pp. 544-550
    • Hacker, J.1    Kestler, H.2    Hoschutzky, H.3    Jann, K.4    Lottspeich, F.5    Korhonen, T.K.6
  • 25
    • 0023897050 scopus 로고
    • Invasion of erythrocytes by malaria parasites: Erythrocyte ligands and parasite receptors
    • Hadley T.J., Miller L.H. Invasion of erythrocytes by malaria parasites: erythrocyte ligands and parasite receptors. Prog. Allergy 1988, 41:49-71.
    • (1988) Prog. Allergy , vol.41 , pp. 49-71
    • Hadley, T.J.1    Miller, L.H.2
  • 26
    • 0027156470 scopus 로고
    • Specificity of S fimbriae on recombinant Escherichia coli: Preferential binding to gangliosides expressing NeuGc?(2-3)Gal and NeuAc?(2-8)NeuAc
    • Hanisch F.G., Hacker J., Schroten H. Specificity of S fimbriae on recombinant Escherichia coli: preferential binding to gangliosides expressing NeuGc?(2-3)Gal and NeuAc?(2-8)NeuAc. Infect. Immun. 1993, 61:2108-2115.
    • (1993) Infect. Immun , vol.61 , pp. 2108-2115
    • Hanisch, F.G.1    Hacker, J.2    Schroten, H.3
  • 27
    • 0028109949 scopus 로고
    • The interaction of Trypanosoma congolense with endothelial cells
    • Hemphill A., Frame I., Ross C.A. The interaction of Trypanosoma congolense with endothelial cells. Parasitology 1994, 109:631-641.
    • (1994) Parasitology , vol.109 , pp. 631-641
    • Hemphill, A.1    Frame, I.2    Ross, C.A.3
  • 28
    • 38149082260 scopus 로고    scopus 로고
    • Characterization of the N-acetyl-5-neuraminic acid-binding site of the extracytoplasmic solute receptor (SiaP) of nontypeable Haemophilus influenzae strain 2019
    • Johnston J.W., Coussens N.P., Allen S., et al. Characterization of the N-acetyl-5-neuraminic acid-binding site of the extracytoplasmic solute receptor (SiaP) of nontypeable Haemophilus influenzae strain 2019. J. Biol. Chem. 2008, 283:855-865.
    • (2008) J. Biol. Chem , vol.283 , pp. 855-865
    • Johnston, J.W.1    Coussens, N.P.2    Allen, S.3
  • 29
    • 0028787845 scopus 로고
    • Microbial recognition of target-cell glycoconjugates
    • Karlsson K.A. Microbial recognition of target-cell glycoconjugates. Curr. Opin. Struct. Biol. 1995, 5:622-635.
    • (1995) Curr. Opin. Struct. Biol , vol.5 , pp. 622-635
    • Karlsson, K.A.1
  • 30
    • 20444431618 scopus 로고    scopus 로고
    • Different response of the knockout mice lacking b-series gangliosides against botulinum and tetanus toxins
    • Kitamura M., Igimi S., Furukawa K. Different response of the knockout mice lacking b-series gangliosides against botulinum and tetanus toxins. Biochim. Biophys. Acta 2005, 1741:1-3.
    • (2005) Biochim. Biophys. Acta , vol.1741 , pp. 1-3
    • Kitamura, M.1    Igimi, S.2    Furukawa, K.3
  • 31
    • 0026601428 scopus 로고
    • Binding of Plasmodium falciparum 175-kilodalton erythrocyte binding antigen and invasion of murine erythrocytes requires N-acetylneuraminic acid but not its O-acetylated form
    • Klotz F.W., Orlandi P.A., Reuter G., et al. Binding of Plasmodium falciparum 175-kilodalton erythrocyte binding antigen and invasion of murine erythrocytes requires N-acetylneuraminic acid but not its O-acetylated form. Mol. Biochem. Parasitol. 1992, 51:49-54.
    • (1992) Mol. Biochem. Parasitol , vol.51 , pp. 49-54
    • Klotz, F.W.1    Orlandi, P.A.2    Reuter, G.3
  • 33
    • 33745309867 scopus 로고    scopus 로고
    • Sialic acid-specific lectins: Occurrence, specificity and function
    • Lehmann F., Tiralongo E., Tiralongo J. Sialic acid-specific lectins: occurrence, specificity and function. Cell. Mol. Life Sci. 2006, 63:1331-1354.
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 1331-1354
    • Lehmann, F.1    Tiralongo, E.2    Tiralongo, J.3
  • 34
    • 0021359430 scopus 로고
    • Coli surface antigens 1 and 3 of colonization factor antigen II-positive enterotoxigenic Escherichia coli: Morphology, purification, and immune responses in humans
    • Levine M.M., Ristaino P., Marley G., et al. Coli surface antigens 1 and 3 of colonization factor antigen II-positive enterotoxigenic Escherichia coli: morphology, purification, and immune responses in humans. Infect. Immun. 1984, 44:409-420.
    • (1984) Infect. Immun , vol.44 , pp. 409-420
    • Levine, M.M.1    Ristaino, P.2    Marley, G.3
  • 35
    • 0020494502 scopus 로고
    • Colonization factor antigen on enterotoxigenic Escherichia coli is a sialic-specific lectin
    • Lindahl M., Faris A., Wadstrom T. Colonization factor antigen on enterotoxigenic Escherichia coli is a sialic-specific lectin. Lancet 1982, 2:280.
    • (1982) Lancet , vol.2 , pp. 280
    • Lindahl, M.1    Faris, A.2    Wadstrom, T.3
  • 36
    • 0023770534 scopus 로고
    • Sialic acid and N-acetylgalactosamine specific bacterial lectins of enterotoxigenic Escherichia coli (ETEC)
    • Lindahl M., Brossmer R., Wadstrom T. Sialic acid and N-acetylgalactosamine specific bacterial lectins of enterotoxigenic Escherichia coli (ETEC). Adv. Exp. Med. Biol. 1988, 228:123-152.
    • (1988) Adv. Exp. Med. Biol , vol.228 , pp. 123-152
    • Lindahl, M.1    Brossmer, R.2    Wadstrom, T.3
  • 37
    • 0038142364 scopus 로고    scopus 로고
    • Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2
    • Lobo C.A., Rodriguez M., Reid M., Lustigman S. Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2. Blood 2003, 101:4628-4631.
    • (2003) Blood , vol.101 , pp. 4628-4631
    • Lobo, C.A.1    Rodriguez, M.2    Reid, M.3    Lustigman, S.4
  • 38
    • 2542489194 scopus 로고    scopus 로고
    • Multistep entry of rotavirus into cells: A Versaillesque dance
    • Lopez S., Arias C.F. Multistep entry of rotavirus into cells: a Versaillesque dance. Trends Microbiol. 2004, 12:271-278.
    • (2004) Trends Microbiol , vol.12 , pp. 271-278
    • Lopez, S.1    Arias, C.F.2
  • 39
    • 0028862919 scopus 로고
    • Derived structure of the putative sialic acid transporter from Escherichia coli predicts a novel sugar permease domain
    • Martinez J., Steenbergen S., Vimr E. Derived structure of the putative sialic acid transporter from Escherichia coli predicts a novel sugar permease domain. J. Bacteriol. 1995, 177:6005-6010.
    • (1995) J. Bacteriol , vol.177 , pp. 6005-6010
    • Martinez, J.1    Steenbergen, S.2    Vimr, E.3
  • 41
    • 0032500378 scopus 로고    scopus 로고
    • The 1.25Å resolution refinement of the cholera toxin B-pentamer: Evidence of peptide backbone strain at the receptor-binding site
    • Merritt E.A., Kuhn P., Sarfaty S., Erbe J.L., Holmes R.K., Hol W.G. The 1.25Å resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site. J. Mol. Biol. 1998, 282:1043-1059.
    • (1998) J. Mol. Biol , vol.282 , pp. 1043-1059
    • Merritt, E.A.1    Kuhn, P.2    Sarfaty, S.3    Erbe, J.L.4    Holmes, R.K.5    Hol, W.G.6
  • 42
    • 31144434884 scopus 로고    scopus 로고
    • High-resolution molecular and antigen structure of the VP8 core of a sialic acid-independent human rotavirus strain
    • Monnier N., Higo-Moriguchi K., Sun Z.Y., Prasad B.V., Taniguchi K., Dormitzer P.R. High-resolution molecular and antigen structure of the VP8 core of a sialic acid-independent human rotavirus strain. J. Virol. 2006, 80:1513-1523.
    • (2006) J. Virol , vol.80 , pp. 1513-1523
    • Monnier, N.1    Higo-Moriguchi, K.2    Sun, Z.Y.3    Prasad, B.V.4    Taniguchi, K.5    Dormitzer, P.R.6
  • 43
    • 24744470072 scopus 로고    scopus 로고
    • Recognition of saccharides by the OpcA, OpaD, and OpaB outer membrane proteins from Neisseria meningitidis
    • Moore J., Bailey S.E., Benmechernene Z., et al. Recognition of saccharides by the OpcA, OpaD, and OpaB outer membrane proteins from Neisseria meningitidis. J. Biol. Chem. 2005, 280:31489-31497.
    • (2005) J. Biol. Chem , vol.280 , pp. 31489-31497
    • Moore, J.1    Bailey, S.E.2    Benmechernene, Z.3
  • 44
    • 0025297756 scopus 로고
    • Functional analysis of the sialic acid-binding adhesin SfaS of pathogenic Escherichia coli by site-specific mutagenesis
    • Morschhauser J., Hoschutzky H., Jann K., Hacker J. Functional analysis of the sialic acid-binding adhesin SfaS of pathogenic Escherichia coli by site-specific mutagenesis. Infect. Immun. 1990, 58:2133-2138.
    • (1990) Infect. Immun , vol.58 , pp. 2133-2138
    • Morschhauser, J.1    Hoschutzky, H.2    Jann, K.3    Hacker, J.4
  • 45
    • 4644369299 scopus 로고    scopus 로고
    • Sialic acid recognition by Vibrio cholerae neuraminidase
    • Moustafa I., Connaris H., Taylor M., et al. Sialic acid recognition by Vibrio cholerae neuraminidase. J. Biol. Chem. 2004, 279:40819-40826.
    • (2004) J. Biol. Chem , vol.279 , pp. 40819-40826
    • Moustafa, I.1    Connaris, H.2    Taylor, M.3
  • 46
    • 33746848092 scopus 로고    scopus 로고
    • Conservation of structure and mechanism in primary and secondary transporters exemplified by SiaP, a sialic acid binding virulence factor from Haemophilus influenzae
    • Muller A., Severi E., Mulligan C., et al. Conservation of structure and mechanism in primary and secondary transporters exemplified by SiaP, a sialic acid binding virulence factor from Haemophilus influenzae. J. Biol. Chem. 2006, 281:22212-22222.
    • (2006) J. Biol. Chem , vol.281 , pp. 22212-22222
    • Muller, A.1    Severi, E.2    Mulligan, C.3
  • 47
    • 0033028556 scopus 로고    scopus 로고
    • Interactions of pathogenic Neisseria with host cells. Is it possible to assemble the puzzle?
    • Nassif X., Pujol C., Morand P., Eugene E. Interactions of pathogenic Neisseria with host cells. Is it possible to assemble the puzzle?. Mol. Microbiol. 1999, 32:1124-1132.
    • (1999) Mol. Microbiol , vol.32 , pp. 1124-1132
    • Nassif, X.1    Pujol, C.2    Morand, P.3    Eugene, E.4
  • 48
    • 0024592141 scopus 로고
    • Ganglioside epitope recognized by K99 fimbriae from enterotoxigenic Escherichia coli
    • Ono E., Abe K., Nakazawa M., Naiki M. Ganglioside epitope recognized by K99 fimbriae from enterotoxigenic Escherichia coli. Infect. Immun. 1989, 57:907-911.
    • (1989) Infect. Immun , vol.57 , pp. 907-911
    • Ono, E.1    Abe, K.2    Nakazawa, M.3    Naiki, M.4
  • 49
    • 0026601423 scopus 로고
    • A malaria invasion receptor, the 175-kilodalton erythrocyte binding antigen of Plasmodium falciparum recognizes the terminal Neu5Ac(?2-3)Gal-sequences of glycophorin A
    • Orlandi P.A., Klotz F.W., Haynes J.D. A malaria invasion receptor, the 175-kilodalton erythrocyte binding antigen of Plasmodium falciparum recognizes the terminal Neu5Ac(?2-3)Gal-sequences of glycophorin A. J. Cell Biol. 1992, 116:901-909.
    • (1992) J. Cell Biol , vol.116 , pp. 901-909
    • Orlandi, P.A.1    Klotz, F.W.2    Haynes, J.D.3
  • 50
    • 25444493368 scopus 로고    scopus 로고
    • Identification of a novel sialic acid transporter in Haemophilus ducreyi
    • Post D.M., Mungur R., Gibson B.W., Munson R.S. Identification of a novel sialic acid transporter in Haemophilus ducreyi. Infect. Immun. 2005, 73:6727-6735.
    • (2005) Infect. Immun , vol.73 , pp. 6727-6735
    • Post, D.M.1    Mungur, R.2    Gibson, B.W.3    Munson, R.S.4
  • 51
    • 0037133637 scopus 로고    scopus 로고
    • Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis
    • Prince S.M., Achtman M., Derrick J.P. Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis. Proc. Natl. Acad. Sci. USA 2002, 99:3417-3421.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3417-3421
    • Prince, S.M.1    Achtman, M.2    Derrick, J.P.3
  • 52
    • 77956696032 scopus 로고    scopus 로고
    • Chemistry, biochemistry and biology of sialic acids
    • Elsevier B.V., Amsterdam, J. Montreuil, J.F.G. Vliegenthart, H. Schachter (Eds.)
    • Schauer R., Kamerling J.P. Chemistry, biochemistry and biology of sialic acids. Glycoproteins II 1997, 243-402. Elsevier B.V., Amsterdam. J. Montreuil, J.F.G. Vliegenthart, H. Schachter (Eds.).
    • (1997) Glycoproteins II , pp. 243-402
    • Schauer, R.1    Kamerling, J.P.2
  • 53
    • 0027192912 scopus 로고
    • 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
    • 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. 1993, 59:293-303.
    • (1993) Mol. Biochem. Parasitol , vol.59 , pp. 293-303
    • Schenkman, S.1    Ferguson, M.A.2    Heise, N.3    de Almeida, M.L.4    Mortara, R.A.5    Yoshida, N.6
  • 54
    • 27944469933 scopus 로고    scopus 로고
    • Sialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP-independent periplasmic transporter
    • Severi E., Randle G., Kivlin P., et al. Sialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP-independent periplasmic transporter. Mol. Microbiol. 2005, 58:1173-1185.
    • (2005) Mol. Microbiol , vol.58 , pp. 1173-1185
    • Severi, E.1    Randle, G.2    Kivlin, P.3
  • 55
    • 34948865783 scopus 로고    scopus 로고
    • Sialic acid utilization by bacterial pathogens
    • Severi E., Hood D.W., Thomas G.H. Sialic acid utilization by bacterial pathogens. Microbiology 2007, 153:2817-2822.
    • (2007) Microbiology , vol.153 , pp. 2817-2822
    • Severi, E.1    Hood, D.W.2    Thomas, G.H.3
  • 56
    • 33646103431 scopus 로고    scopus 로고
    • Carbohydrates as future anti-adhesion drugs for infectious diseases
    • Sharon N. Carbohydrates as future anti-adhesion drugs for infectious diseases. Biochim. Biophys. Acta 2006, 1760:527-537.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 527-537
    • Sharon, N.1
  • 57
    • 0023764254 scopus 로고
    • Purification and characterization of CS2, a sialic acid-specific haemagglutinin of enterotoxigenic Escherichia coli
    • Sjoberg P.O., Lindahl M., Porath J., Wadstrom T. Purification and characterization of CS2, a sialic acid-specific haemagglutinin of enterotoxigenic Escherichia coli. Biochem. J. 1988, 255:105-111.
    • (1988) Biochem. J , vol.255 , pp. 105-111
    • Sjoberg, P.O.1    Lindahl, M.2    Porath, J.3    Wadstrom, T.4
  • 58
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel J.J., Wiley D.C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 2000, 69:531-569.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 60
    • 0030839256 scopus 로고    scopus 로고
    • High-resolution structure of a polyomavirus VP1-oligosaccharide complex: Implications for assembly and receptor binding
    • Stehle T., Harrison S.C. High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding. EMBO J. 1997, 16:5139-5148.
    • (1997) EMBO J , vol.16 , pp. 5139-5148
    • Stehle, T.1    Harrison, S.C.2
  • 61
    • 0028500699 scopus 로고
    • Structure of a pertussis toxin-sugar complex as a model for receptor binding
    • Stein P.E., Boodhoo A., Armstrong G.D., et al. Structure of a pertussis toxin-sugar complex as a model for receptor binding. Nat. Struct. Biol. 1994, 1:591-596.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 591-596
    • Stein, P.E.1    Boodhoo, A.2    Armstrong, G.D.3
  • 62
    • 33750119810 scopus 로고    scopus 로고
    • Glycan microarray technologies: Tools to survey host specificity of influenza viruses
    • Stevens J., Blixt O., Paulson J.C., Wilson I.A. Glycan microarray technologies: tools to survey host specificity of influenza viruses. Nat. Rev. Microbiol. 2006, 4:857-864.
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 857-864
    • Stevens, J.1    Blixt, O.2    Paulson, J.C.3    Wilson, I.A.4
  • 63
    • 21144441367 scopus 로고    scopus 로고
    • Sialobiology of influenza: Molecular mechanism of host range variation of influenza viruses
    • Suzuki Y. Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses. Biol. Pharm. Bull. 2005, 28:399-408.
    • (2005) Biol. Pharm. Bull , vol.28 , pp. 399-408
    • Suzuki, Y.1
  • 64
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • Swaminathan S., Eswaramoorthy S. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 2000, 7:693-699.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 65
    • 0027155656 scopus 로고
    • Calf small intestine receptors for K99 fimbriated enterotoxigenic Escherichia coli
    • Teneberg S., Willemsen P.T., de Graaf F.K., Karlsson K.A. Calf small intestine receptors for K99 fimbriated enterotoxigenic Escherichia coli. FEMS Microbiol. Lett. 1993, 109:107-112.
    • (1993) FEMS Microbiol. Lett , vol.109 , pp. 107-112
    • Teneberg, S.1    Willemsen, P.T.2    de Graaf, F.K.3    Karlsson, K.A.4
  • 66
    • 0030872415 scopus 로고    scopus 로고
    • Carbohydrate binding specificity of the neutrophil-activating protein of Helicobacter pylori
    • Teneberg S., Miller-Podraza H., Lampert H.C., et al. Carbohydrate binding specificity of the neutrophil-activating protein of Helicobacter pylori. J. Biol. Chem. 1997, 272:19067-19071.
    • (1997) J. Biol. Chem , vol.272 , pp. 19067-19071
    • Teneberg, S.1    Miller-Podraza, H.2    Lampert, H.C.3
  • 67
    • 0141738649 scopus 로고    scopus 로고
    • Trans-sialidase-like sequences from Trypanosoma congolense conserve most of the critical active site residues found in other trans-sialidases
    • Tiralongo E., Martensen I., Grotzinger J., Tiralongo J., Schauer R. Trans-sialidase-like sequences from Trypanosoma congolense conserve most of the critical active site residues found in other trans-sialidases. Biol. Chem. 2003, 384:1203-1213.
    • (2003) Biol. Chem , vol.384 , pp. 1203-1213
    • Tiralongo, E.1    Martensen, I.2    Grotzinger, J.3    Tiralongo, J.4    Schauer, R.5
  • 68
    • 0038268721 scopus 로고    scopus 로고
    • Two trans-sialidase forms with different sialic acid transfer and sialidase activities from Trypanosoma congolense
    • 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. 2003, 278:23301-23310.
    • (2003) J. Biol. Chem , vol.278 , pp. 23301-23310
    • Tiralongo, E.1    Schrader, S.2    Lange, H.3    Lemke, H.4    Tiralongo, J.5    Schauer, R.6
  • 69
    • 0037195863 scopus 로고    scopus 로고
    • Trans-sialidase from Trypanosoma cruzi binds host T-lymphocytes in a lectin manner
    • Todeschini A.R., Girard M.F., Wieruszeski J.M., et al. Trans-sialidase from Trypanosoma cruzi binds host T-lymphocytes in a lectin manner. J. Biol. Chem. 2002, 277:45962-45968.
    • (2002) J. Biol. Chem , vol.277 , pp. 45962-45968
    • Todeschini, A.R.1    Girard, M.F.2    Wieruszeski, J.M.3
  • 70
    • 22744456158 scopus 로고    scopus 로고
    • Structural basis for the EBA-175 erythrocyte invasion pathway of the malaria parasite Plasmodium falciparum
    • Tolia N.H., Enemark E.J., Sim B.K., Joshua-Tor L. Structural basis for the EBA-175 erythrocyte invasion pathway of the malaria parasite Plasmodium falciparum. Cell 2005, 122:183-193.
    • (2005) Cell , vol.122 , pp. 183-193
    • Tolia, N.H.1    Enemark, E.J.2    Sim, B.K.3    Joshua-Tor, L.4
  • 71
    • 0031025736 scopus 로고    scopus 로고
    • Expression and identification of a laminin-binding protein in Aspergillus fumigatus conidia
    • Tronchin G., Esnault K., Renier G., Filmon R., Chabasse D., Bouchara J.P. Expression and identification of a laminin-binding protein in Aspergillus fumigatus conidia. Infect. Immun. 1997, 65:9-15.
    • (1997) Infect. Immun , vol.65 , pp. 9-15
    • Tronchin, G.1    Esnault, K.2    Renier, G.3    Filmon, R.4    Chabasse, D.5    Bouchara, J.P.6
  • 72
    • 0036893689 scopus 로고    scopus 로고
    • Purification and partial characterization of a 32-kilodalton sialic acid-specific lectin from Aspergillus fumigatus
    • Tronchin G., Esnault K., Sanchez M., Larcher G., Marot-Leblond A., Bouchara J.P. Purification and partial characterization of a 32-kilodalton sialic acid-specific lectin from Aspergillus fumigatus. Infect. Immun. 2002, 70:6891-6895.
    • (2002) Infect. Immun , vol.70 , pp. 6891-6895
    • Tronchin, G.1    Esnault, K.2    Sanchez, M.3    Larcher, G.4    Marot-Leblond, A.5    Bouchara, J.P.6
  • 73
    • 34547929295 scopus 로고    scopus 로고
    • Diversity in cell surface sialic acid presentations: Implications for biology and disease
    • Varki N.M., Varki A. Diversity in cell surface sialic acid presentations: implications for biology and disease. Lab. Invest. 2007, 87:851-857.
    • (2007) Lab. Invest , vol.87 , pp. 851-857
    • Varki, N.M.1    Varki, A.2
  • 76
    • 33947253253 scopus 로고    scopus 로고
    • Structure and role of sialic acids on the surface of Aspergillus fumigatus conidiospores
    • Warwas M.L., Watson J.N., Bennet A.J., Moore M.M. Structure and role of sialic acids on the surface of Aspergillus fumigatus conidiospores. Glycobiology 2007, 17:401-410.
    • (2007) Glycobiology , vol.17 , pp. 401-410
    • Warwas, M.L.1    Watson, J.N.2    Bennet, A.J.3    Moore, M.M.4
  • 77
    • 0034034902 scopus 로고    scopus 로고
    • Adhesion of Aspergillus species to extracellular matrix proteins: Evidence for involvement of negatively charged carbohydrates on the conidial surface
    • Wasylnka J.A., Moore M.M. Adhesion of Aspergillus species to extracellular matrix proteins: evidence for involvement of negatively charged carbohydrates on the conidial surface. Infect. Immun. 2000, 68:3377-3384.
    • (2000) Infect. Immun , vol.68 , pp. 3377-3384
    • Wasylnka, J.A.1    Moore, M.M.2
  • 78
    • 0025098747 scopus 로고
    • The binding of colonization factor antigens of enterotoxigenic Escherichia coli to intestinal cell membrane proteins
    • Wenneras C., Holmgren J., Svennerholm A.M. The binding of colonization factor antigens of enterotoxigenic Escherichia coli to intestinal cell membrane proteins. FEMS Microbiol. Lett. 1990, 54:107-112.
    • (1990) FEMS Microbiol. Lett , vol.54 , pp. 107-112
    • Wenneras, C.1    Holmgren, J.2    Svennerholm, A.M.3
  • 79
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3Å resolution
    • Wilson I.A., Skehel J.J., Wiley D.C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3Å resolution. Nature 1981, 289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 80
    • 0033982809 scopus 로고    scopus 로고
    • Sialylation of the host receptor may modulate entry of demyelinating persistent Theiler's virus
    • Zhou L., Luo Y., Wu Y., Tsao J., Luo M. Sialylation of the host receptor may modulate entry of demyelinating persistent Theiler's virus. J. Virol. 2000, 74:1477-1485.
    • (2000) J. Virol , vol.74 , pp. 1477-1485
    • Zhou, L.1    Luo, Y.2    Wu, Y.3    Tsao, J.4    Luo, M.5
  • 81
    • 36549003234 scopus 로고    scopus 로고
    • Structural implications of siglec-5-mediated sialoglycan recognition
    • Zhuravleva M.A., Trandem K., Sun P.D. Structural implications of siglec-5-mediated sialoglycan recognition. J. Mol. Biol. 2008, 375:437-447.
    • (2008) J. Mol. Biol , vol.375 , pp. 437-447
    • Zhuravleva, M.A.1    Trandem, K.2    Sun, P.D.3


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