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Volumn 367, Issue , 2015, Pages 1-28

Sialic acid receptors of viruses

Author keywords

Ganglioside; Mucins; Neuraminidase; Receptor binding; Receptordestroying enzyme; Sialate O acetylesterase; Virus

Indexed keywords

ACETYLESTERASE; CELL SURFACE RECEPTOR; PROTEIN BINDING; SIALATE O-ACETYLESTERASE; SIALIC ACID DERIVATIVE; SIALIC ACID RECEPTOR; SIALIDASE; VIRUS PROTEIN; VIRUS RECEPTOR;

EID: 84938387123     PISSN: 03401022     EISSN: None     Source Type: Book Series    
DOI: 10.1007/128_2013_466     Document Type: Article
Times cited : (215)

References (205)
  • 1
    • 0002171713 scopus 로고
    • The agglutination of red cells by allantoic fluid of chick embryos infected with influenza virus
    • Hirst GK (1941) The agglutination of red cells by allantoic fluid of chick embryos infected with influenza virus. Science 94:22-23
    • (1941) Science , vol.94 , pp. 22-23
    • Hirst, G.K.1
  • 2
    • 33646274372 scopus 로고
    • The adsorption of influenza virus by red cells and a new in vitro method of measuring antibodies for influenza virus
    • McClelland L, Hare R (1941) The adsorption of influenza virus by red cells and a new in vitro method of measuring antibodies for influenza virus. Can J Public Health 32:530-538
    • (1941) Can J Public Health , vol.32 , pp. 530-538
    • McClelland, L.1    Hare, R.2
  • 3
    • 84957354540 scopus 로고
    • The receptor-destroying enzyme of V. Cholerae
    • Burnet FM, Stone JD (1947) The receptor-destroying enzyme of V. cholerae. Aust J Exp Biol Med Sci 25:227-233
    • (1947) Aust J Exp Biol Med Sci , vol.25 , pp. 227-233
    • Burnet, F.M.1    Stone, J.D.2
  • 4
    • 0346744769 scopus 로고
    • Product of interaction between influenza virus enzyme and ovomucin
    • Gottschalk A, Lind PE (1949) Product of interaction between influenza virus enzyme and ovomucin. Nature 164:232
    • (1949) Nature , vol.164 , pp. 232
    • Gottschalk, A.1    Lind, P.E.2
  • 5
    • 77049267301 scopus 로고
    • Über die enzymatische Wirkung von Influenza Virus
    • Klenk E, Faillard H, Lempfrid H (1955) Über die enzymatische Wirkung von Influenza Virus. Z physiol Chem 301:235-246
    • (1955) Z physiol Chem , vol.301 , pp. 235-246
    • Klenk, E.1    Faillard, H.2    Lempfrid, H.3
  • 6
    • 33645461049 scopus 로고    scopus 로고
    • Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses
    • de Groot RJ (2006) Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses. Glycoconj J 23:59-72
    • (2006) Glycoconj J , vol.23 , pp. 59-72
    • de Groot, R.J.1
  • 7
    • 33745309867 scopus 로고    scopus 로고
    • Sialic acid-specific lectins: Occurrence, specificity and function
    • Lehmann F, Tiralongo E, Tiralongo J (2006) Sialic acid-specific lectins: occurrence, specificity and function. Cell Mol Life Sci 63:1331-1354
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1331-1354
    • Lehmann, F.1    Tiralongo, E.2    Tiralongo, J.3
  • 8
    • 59349116159 scopus 로고    scopus 로고
    • The Polyomaviridae: Contributions of virus structure to our understanding of virus receptors and infectious entry
    • Neu U, Stehle T, Atwood WJ (2009) The Polyomaviridae: contributions of virus structure to our understanding of virus receptors and infectious entry. Virology 384:389-399
    • (2009) Virology , vol.384 , pp. 389-399
    • Neu, U.1    Stehle, T.2    Atwood, W.J.3
  • 9
    • 20344381822 scopus 로고    scopus 로고
    • Glycoconjugate glycans as viral receptors
    • Olofsson S, Bergstrom T (2005) Glycoconjugate glycans as viral receptors. Ann Med 37:154-172
    • (2005) Ann Med , vol.37 , pp. 154-172
    • Olofsson, S.1    Bergstrom, T.2
  • 10
    • 78049507903 scopus 로고    scopus 로고
    • Glycosphingolipids as receptors for non-enveloped viruses
    • Taube S, Jiang M, Wobus CE (2010) Glycosphingolipids as receptors for non-enveloped viruses. Viruses 2:1011-1049
    • (2010) Viruses , vol.2 , pp. 1011-1049
    • Taube, S.1    Jiang, M.2    Wobus, C.E.3
  • 12
    • 34447299235 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • Knipe DM, Howley PM (eds), Lippincott, Williams and Wilkins, Philadelphia
    • Palese P, Shaw ML (2007) Orthomyxoviridae: the viruses and their replication. In: Knipe DM, Howley PM (eds) Fields virology. Lippincott, Williams and Wilkins, Philadelphia, pp 1647-1689
    • (2007) Fields virology , pp. 1647-1689
    • Palese, P.1    Shaw, M.L.2
  • 15
    • 77956556232 scopus 로고    scopus 로고
    • Influenza hemagglutinin and neuraminidase membrane glycoproteins
    • Gamblin SJ, Skehel JJ (2010) Influenza hemagglutinin and neuraminidase membrane glycoproteins. J Biol Chem 285:28403-28409
    • (2010) J Biol Chem , vol.285 , pp. 28403-28409
    • Gamblin, S.J.1    Skehel, J.J.2
  • 16
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel JJ, Wiley DC (2000) Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69:531-569
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 17
    • 34147114776 scopus 로고    scopus 로고
    • Receptor specificity, host range and pathogenicity of influenza viruses
    • Kawaoka Y (ed), Caister Academic, Wymondham
    • Matrosovich MN, Klenk H-D, Kawaoka Y (2006) Receptor specificity, host range and pathogenicity of influenza viruses. In: Kawaoka Y (ed) Influenza virology: current topics. Caister Academic, Wymondham, pp 95-137
    • (2006) Influenza virology: Current topics , pp. 95-137
    • Matrosovich, M.N.1    Klenk, H.-D.2    Kawaoka, Y.3
  • 18
    • 0027988832 scopus 로고
    • Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates
    • Connor RJ, Kawaoka Y, Webster RG, Paulson JC (1994) Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 205:17-23
    • (1994) Virology , vol.205 , pp. 17-23
    • Connor, R.J.1    Kawaoka, Y.2    Webster, R.G.3    Paulson, J.C.4
  • 19
    • 0033856695 scopus 로고    scopus 로고
    • Alterations of receptor-binding properties of H1, H2 and H3 avian influenza virus hemagglutinins upon introduction into mammals
    • Matrosovich M, Tuzikov A, Bovin N, Gambarian A, Klimov A, Cox N, Castrucci M, Donatelli I, Kawaoka Y (2000) Alterations of receptor-binding properties of H1, H2 and H3 avian influenza virus hemagglutinins upon introduction into mammals. J Virol 74:8502-8512
    • (2000) J Virol , vol.74 , pp. 8502-8512
    • Matrosovich, M.1    Tuzikov, A.2    Bovin, N.3    Gambarian, A.4    Klimov, A.5    Cox, N.6    Castrucci, M.7    Donatelli, I.8    Kawaoka, Y.9
  • 20
    • 0020520729 scopus 로고
    • Receptor determinants of human and animal influenza virus isolates: Differences in receptor specificity of the H3 hemagglutinin based on species of origin
    • Rogers GN, Paulson JC (1983) Receptor determinants of human and animal influenza virus isolates: differences in receptor specificity of the H3 hemagglutinin based on species of origin. Virology 127:361-373
    • (1983) Virology , vol.127 , pp. 361-373
    • Rogers, G.N.1    Paulson, J.C.2
  • 21
    • 0025620241 scopus 로고
    • Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity
    • Baum LG, Paulson JC (1990) Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity. Acta Histochem Suppl 40:35-38
    • (1990) Acta Histochem Suppl , vol.40 , pp. 35-38
    • Baum, L.G.1    Paulson, J.C.2
  • 22
    • 0035983232 scopus 로고    scopus 로고
    • Differences between influenza virus receptors on target cells of duck and chicken
    • Gambaryan A, Webster R, Matrosovich M (2002) Differences between influenza virus receptors on target cells of duck and chicken. Arch Virol 147:1197-1208
    • (2002) Arch Virol , vol.147 , pp. 1197-1208
    • Gambaryan, A.1    Webster, R.2    Matrosovich, M.3
  • 24
    • 77049105618 scopus 로고    scopus 로고
    • Differences in influenza virus receptors in chickens and ducks: Implications for interspecies transmission
    • Kuchipudi SV, Nelli R, White GA, Bain M, Chang KC, Dunham S (2009) Differences in influenza virus receptors in chickens and ducks: implications for interspecies transmission. J Mol Genet Med 3:143-151
    • (2009) J Mol Genet Med , vol.3 , pp. 143-151
    • Kuchipudi, S.V.1    Nelli, R.2    White, G.A.3    Bain, M.4    Chang, K.C.5    Dunham, S.6
  • 25
    • 77049100507 scopus 로고    scopus 로고
    • Species and age related differences in the type and distribution of influenza virus receptors in different tissues of chickens, ducks and turkeys
    • Pillai SP, Lee CW (2010) Species and age related differences in the type and distribution of influenza virus receptors in different tissues of chickens, ducks and turkeys. Virol J 7:5
    • (2010) Virol J , vol.7 , pp. 5
    • Pillai, S.P.1    Lee, C.W.2
  • 27
    • 68149168811 scopus 로고    scopus 로고
    • Influenza receptors, polymerase and host range
    • Matrosovich M, Stech J, Klenk HD (2009) Influenza receptors, polymerase and host range. Rev Sci Tech 28:203-217
    • (2009) Rev Sci Tech , vol.28 , pp. 203-217
    • Matrosovich, M.1    Stech, J.2    Klenk, H.D.3
  • 28
    • 50549091277 scopus 로고    scopus 로고
    • Receptor specificity of influenza viruses and its alteration during interspecies transmission
    • Klenk HD, Matrosovich MN, Stech J (eds), Karger, Basel
    • Matrosovich MN, Gambarian AS, Klenk HD (2008) Receptor specificity of influenza viruses and its alteration during interspecies transmission. In: Klenk HD, Matrosovich MN, Stech J (eds) Avian Influenza. Karger, Basel, pp 134-155
    • (2008) Avian Influenza , pp. 134-155
    • Matrosovich, M.N.1    Gambarian, A.S.2    Klenk, H.D.3
  • 30
    • 0032927194 scopus 로고    scopus 로고
    • The surface glycoproteins of H5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties
    • Matrosovich M, Zhou N, Kawaoka Y, Webster R (1999) The surface glycoproteins of H5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties. J Virol 73:1146-1155
    • (1999) J Virol , vol.73 , pp. 1146-1155
    • Matrosovich, M.1    Zhou, N.2    Kawaoka, Y.3    Webster, R.4
  • 32
  • 36
    • 38549111238 scopus 로고    scopus 로고
    • Avian influenza receptor expression in H5N1- infected and noninfected human tissues
    • Yao L, Korteweg C, Hsueh W, Gu J (2007) Avian influenza receptor expression in H5N1- infected and noninfected human tissues. FASEB J. doi:10.1096/fj.1006-7880com
    • (2007) FASEB J
    • Yao, L.1    Korteweg, C.2    Hsueh, W.3    Gu, J.4
  • 38
    • 84861394598 scopus 로고    scopus 로고
    • Experimental adaptation of an influenza H5 HA confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets
    • Imai M, Watanabe T, Hatta M, Das SC, Ozawa M, Shinya K, Zhong G, Hanson A, Katsura H, Watanabe S et al. (2012) Experimental adaptation of an influenza H5 HA confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets. Nature 486:420-428
    • (2012) Nature , vol.486 , pp. 420-428
    • Imai, M.1    Watanabe, T.2    Hatta, M.3    Das, S.C.4    Ozawa, M.5    Shinya, K.6    Zhong, G.7    Hanson, A.8    Katsura, H.9    Watanabe, S.10
  • 39
    • 0001806532 scopus 로고    scopus 로고
    • Influenza in pigs and their role as the intermediate host
    • Nicholson KG, Webster RG, Hay A (eds), Blackwell Science, London
    • Scholtissek C, Hinshaw VS, Olsen CW (1998) Influenza in pigs and their role as the intermediate host. In: Nicholson KG, Webster RG, Hay A (eds) Textbook of influenza. Blackwell Science, London, pp 137-145
    • (1998) Textbook of influenza , pp. 137-145
    • Scholtissek, C.1    Hinshaw, V.S.2    Olsen, C.W.3
  • 41
    • 77749268058 scopus 로고    scopus 로고
    • Replication of avian, human and swine influenza viruses in porcine respiratory explants and association with sialic acid distribution
    • Van Poucke SG, Nicholls JM, Nauwynck HJ, Van Reeth K (2010) Replication of avian, human and swine influenza viruses in porcine respiratory explants and association with sialic acid distribution. Virol J 7:38
    • (2010) Virol J , vol.7 , pp. 38
    • Van Poucke, S.G.1    Nicholls, J.M.2    Nauwynck, H.J.3    Van Reeth, K.4
  • 45
    • 84873403163 scopus 로고    scopus 로고
    • Structure and receptor binding properties of a pandemic H1N1 virus hemagglutinin
    • Yang H, Carney P, Stevens J (2010) Structure and receptor binding properties of a pandemic H1N1 virus hemagglutinin. PLoS Curr 2. doi:10.1371/currents.RRN1152
    • (2010) PLoS Curr , pp. 2
    • Yang, H.1    Carney, P.2    Stevens, J.3
  • 47
    • 77951048371 scopus 로고    scopus 로고
    • Observed association between the HA1 mutation D222G in the 2009 pandemic influenza A(H1N1) virus and severe clinical outcome, Norway 2009-2010
    • pii=19498
    • Kilander A, Rykkvin R, Dudman SG, Hungnes O (2010) Observed association between the HA1 mutation D222G in the 2009 pandemic influenza A(H1N1) virus and severe clinical outcome, Norway 2009-2010. Euro Surveill 15(9):pii=19498
    • (2010) Euro Surveill , vol.15 , Issue.9
    • Kilander, A.1    Rykkvin, R.2    Dudman, S.G.3    Hungnes, O.4
  • 49
    • 78049516347 scopus 로고    scopus 로고
    • Altered receptor specificity and cell tropism of D222G hemagglutinin mutants isolated from fatal cases of pandemic A(H1N1) 2009 influenza virus
    • Liu Y, Childs RA, Matrosovich T, Wharton S, Palma AS, Chai W, Daniels R, Gregory V, Uhlendorff J, Kiso M et al. (2010) Altered receptor specificity and cell tropism of D222G hemagglutinin mutants isolated from fatal cases of pandemic A(H1N1) 2009 influenza virus. J Virol 84:12069-12074
    • (2010) J Virol , vol.84 , pp. 12069-12074
    • Liu, Y.1    Childs, R.A.2    Matrosovich, T.3    Wharton, S.4    Palma, A.S.5    Chai, W.6    Daniels, R.7    Gregory, V.8    Uhlendorff, J.9    Kiso, M.10
  • 51
    • 0030748536 scopus 로고    scopus 로고
    • Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site
    • Matrosovich MN, Gambaryan AS, Teneberg S, Piskarev VE, Yamnikova SS, Lvov DK, Robertson JS, Karlsson KA (1997) Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site. Virology 233:224-234
    • (1997) Virology , vol.233 , pp. 224-234
    • Matrosovich, M.N.1    Gambaryan, A.S.2    Teneberg, S.3    Piskarev, V.E.4    Yamnikova, S.S.5    Lvov, D.K.6    Robertson, J.S.7    Karlsson, K.A.8
  • 53
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution
    • Varghese JN, Laver WG, Colman PM (1983) Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature 303:35-40
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 54
    • 0020028270 scopus 로고
    • Block deletions in the neuraminidase genes from some influenza A viruses of the N1 subtype
    • Blok J, Air GM (1982) Block deletions in the neuraminidase genes from some influenza A viruses of the N1 subtype. Virology 118:229-234
    • (1982) Virology , vol.118 , pp. 229-234
    • Blok, J.1    Air, G.M.2
  • 55
    • 7644241814 scopus 로고    scopus 로고
    • Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium
    • Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk HD (2004) Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J Virol 78:12665-12667
    • (2004) J Virol , vol.78 , pp. 12665-12667
    • Matrosovich, M.N.1    Matrosovich, T.Y.2    Gray, T.3    Roberts, N.A.4    Klenk, H.D.5
  • 56
    • 0016272701 scopus 로고
    • Characterization of temperature sensitive influenza virus mutants defective in neuraminidase
    • Palese P, Tobita K, Ueda M, Compans RW (1974) Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61:397-410
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Tobita, K.2    Ueda, M.3    Compans, R.W.4
  • 57
    • 0035020424 scopus 로고    scopus 로고
    • Changes in the haemagglutinin and the neuraminidase genes prior to the emergence of highly pathogenic H7N1 avian influenza viruses in Italy
    • Banks J, Speidel ES, Moore E, Plowright L, Piccirillo A, Capua I, Cordioli P, Fioretti A, Alexander DJ (2001) Changes in the haemagglutinin and the neuraminidase genes prior to the emergence of highly pathogenic H7N1 avian influenza viruses in Italy. Arch Virol 146:963-973
    • (2001) Arch Virol , vol.146 , pp. 963-973
    • Banks, J.1    Speidel, E.S.2    Moore, E.3    Plowright, L.4    Piccirillo, A.5    Capua, I.6    Cordioli, P.7    Fioretti, A.8    Alexander, D.J.9
  • 59
  • 60
    • 0036090557 scopus 로고    scopus 로고
    • Functional balance between haemagglutinin and neuraminidase in influenza virus infections
    • Wagner R, Matrosovich M, Klenk HD (2002) Functional balance between haemagglutinin and neuraminidase in influenza virus infections. Rev Med Virol 12:159-166
    • (2002) Rev Med Virol , vol.12 , pp. 159-166
    • Wagner, R.1    Matrosovich, M.2    Klenk, H.D.3
  • 61
    • 0033934134 scopus 로고    scopus 로고
    • Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: A study by reverse genetics
    • Wagner R, Wolff T, Herwig A, Pleschka S, Klenk HD (2000) Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: a study by reverse genetics. J Virol 74:6316-6323
    • (2000) J Virol , vol.74 , pp. 6316-6323
    • Wagner, R.1    Wolff, T.2    Herwig, A.3    Pleschka, S.4    Klenk, H.D.5
  • 62
    • 0029065437 scopus 로고
    • N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity
    • Hausmann J, Kretzschmar E, Garten W, Klenk HD (1995) N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity. J Gen Virol 76(Pt 7):1719-1728
    • (1995) J Gen Virol , vol.76 , pp. 1719-1728
    • Hausmann, J.1    Kretzschmar, E.2    Garten, W.3    Klenk, H.D.4
  • 63
    • 0030796172 scopus 로고    scopus 로고
    • Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks
    • Kobasa D, Rodgers ME, Wells K, Kawaoka Y (1997) Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks. J Virol 71:6706-6713
    • (1997) J Virol , vol.71 , pp. 6706-6713
    • Kobasa, D.1    Rodgers, M.E.2    Wells, K.3    Kawaoka, Y.4
  • 66
    • 67349192219 scopus 로고    scopus 로고
    • Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses
    • Uhlendorff J, Matrosovich T, Klenk HD, Matrosovich M (2009) Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses. Arch Virol 154:945-957
    • (2009) Arch Virol , vol.154 , pp. 945-957
    • Uhlendorff, J.1    Matrosovich, T.2    Klenk, H.D.3    Matrosovich, M.4
  • 67
    • 0002044965 scopus 로고
    • Sialic acid as receptor determinant of ortho- and paramyxoviruses
    • Rosenberg A (ed), Plenum, New York
    • Herrler G, Hausmann J, Klenk HD (1995) Sialic acid as receptor determinant of ortho- and paramyxoviruses. In: Rosenberg A (ed) Biology of the Sialic acids. Plenum, New York, pp 315-336
    • (1995) Biology of the Sialic acids , pp. 315-336
    • Herrler, G.1    Hausmann, J.2    Klenk, H.D.3
  • 68
    • 0025984385 scopus 로고
    • Structure and function of the HEF glycoprotein of influenza C virus
    • Herrler G, Klenk HD (1991) Structure and function of the HEF glycoprotein of influenza C virus. Adv Virus Res 40:213-234
    • (1991) Adv Virus Res , vol.40 , pp. 213-234
    • Herrler, G.1    Klenk, H.D.2
  • 70
    • 0344036042 scopus 로고
    • The receptordestroying enzyme of influenza C virus is neuraminate-O-acetylesterase
    • Herrler G, Rott R, Klenk HD, Muller HP, Shukla AK, Schauer R (1985) The receptordestroying enzyme of influenza C virus is neuraminate-O-acetylesterase. EMBO J 4:1503-1506
    • (1985) EMBO J , vol.4 , pp. 1503-1506
    • Herrler, G.1    Rott, R.2    Klenk, H.D.3    Muller, H.P.4    Shukla, A.K.5    Schauer, R.6
  • 71
    • 0024245829 scopus 로고
    • Serine 71 of the glycoprotein HEF is located at the active site of the acetylesterase of influenza C virus
    • Herrler G, Multhaup G, Beyreuther K, Klenk HD (1988) Serine 71 of the glycoprotein HEF is located at the active site of the acetylesterase of influenza C virus. Arch Virol 102:269-274
    • (1988) Arch Virol , vol.102 , pp. 269-274
    • Herrler, G.1    Multhaup, G.2    Beyreuther, K.3    Klenk, H.D.4
  • 72
    • 0028850080 scopus 로고
    • The catalytic triad of the influenza C virus glycoprotein HEF esterase: Characterization by site-directed mutagenesis and functional analysis
    • Pleschka S, Klenk HD, Herrler G (1995) The catalytic triad of the influenza C virus glycoprotein HEF esterase: characterization by site-directed mutagenesis and functional analysis. J Gen Virol 76:2529-2537
    • (1995) J Gen Virol , vol.76 , pp. 2529-2537
    • Pleschka, S.1    Klenk, H.D.2    Herrler, G.3
  • 73
    • 0024543947 scopus 로고
    • Influenza C virus esterase: Analysis of catalytic site, inhibition, and possible function
    • Vlasak R, Muster T, Lauro AM, Powers JC, Palese P (1989) Influenza C virus esterase: analysis of catalytic site, inhibition, and possible function. J Virol 63:2056-2062
    • (1989) J Virol , vol.63 , pp. 2056-2062
    • Vlasak, R.1    Muster, T.2    Lauro, A.M.3    Powers, J.C.4    Palese, P.5
  • 74
    • 0031044164 scopus 로고    scopus 로고
    • Inactivation of inhibitors by the receptor-destroying enzyme of influenza C virus
    • Hofling K, Klenk HD, Herrler G (1997) Inactivation of inhibitors by the receptor-destroying enzyme of influenza C virus. J Gen Virol 78:567-570
    • (1997) J Gen Virol , vol.78 , pp. 567-570
    • Hofling, K.1    Klenk, H.D.2    Herrler, G.3
  • 75
    • 0343807503 scopus 로고    scopus 로고
    • Transfer of an esterase-resistant receptor analog to the surface of influenza C virions results in reduced infectivity due to aggregate formation
    • Hofling K, Brossmer R, Klenk H, Herrler G (1996) Transfer of an esterase-resistant receptor analog to the surface of influenza C virions results in reduced infectivity due to aggregate formation. Virology 218:127-133
    • (1996) Virology , vol.218 , pp. 127-133
    • Hofling, K.1    Brossmer, R.2    Klenk, H.3    Herrler, G.4
  • 76
    • 0028875020 scopus 로고
    • A synthetic sialic acid analog that is resistant to the receptor-destroying enzyme can be used by influenza C virus as a receptor determinant for infection of cells
    • Herrler G, Gross HJ, Brossmer R (1995) A synthetic sialic acid analog that is resistant to the receptor-destroying enzyme can be used by influenza C virus as a receptor determinant for infection of cells. Biochem Biophys Res Commun 216:821-827
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 821-827
    • Herrler, G.1    Gross, H.J.2    Brossmer, R.3
  • 77
    • 0026708107 scopus 로고
    • A synthetic sialic acid analogue is recognized by influenza C virus as a receptor determinant but is resistant to the receptor-destroying enzyme
    • Herrler G, Gross HJ, Imhof A, Brossmer R, Milks G, Paulson JC (1992) A synthetic sialic acid analogue is recognized by influenza C virus as a receptor determinant but is resistant to the receptor-destroying enzyme. J Biol Chem 267:12501-12505
    • (1992) J Biol Chem , vol.267 , pp. 12501-12505
    • Herrler, G.1    Gross, H.J.2    Imhof, A.3    Brossmer, R.4    Milks, G.5    Paulson, J.C.6
  • 78
    • 0023002952 scopus 로고
    • Influenza C virus uses 9-O-acetyl-Nacetylneuraminic acid as a high affinity receptor determinant for attachment to cells
    • Rogers GN, Herrler G, Paulson JC, Klenk HD (1986) Influenza C virus uses 9-O-acetyl-Nacetylneuraminic acid as a high affinity receptor determinant for attachment to cells. J Biol Chem 261:5947-5951
    • (1986) J Biol Chem , vol.261 , pp. 5947-5951
    • Rogers, G.N.1    Herrler, G.2    Paulson, J.C.3    Klenk, H.D.4
  • 79
    • 0023638370 scopus 로고
    • The surface receptor is a major determinant of the cell tropism of influenza C virus
    • Herrler G, Klenk HD (1987) The surface receptor is a major determinant of the cell tropism of influenza C virus. Virology 159:102-108
    • (1987) Virology , vol.159 , pp. 102-108
    • Herrler, G.1    Klenk, H.D.2
  • 80
    • 0029076138 scopus 로고
    • Identification of a 40-kDa cell surface sialoglycoprotein with the characteristics of a major influenza C virus receptor in a Madin-Darby canine kidney cell line
    • Zimmer G, Klenk HD, Herrler G (1995) Identification of a 40-kDa cell surface sialoglycoprotein with the characteristics of a major influenza C virus receptor in a Madin-Darby canine kidney cell line. J Biol Chem 270:17815-17822
    • (1995) J Biol Chem , vol.270 , pp. 17815-17822
    • Zimmer, G.1    Klenk, H.D.2    Herrler, G.3
  • 81
    • 0030883585 scopus 로고    scopus 로고
    • Molecular characterization of gp40, a mucin-type glycoprotein from the apical plasma membrane of Madin-Darby canine kidney cells (type I)
    • Zimmer G, Lottspeich F, Maisner A, Klenk HD, Herrler G (1997) Molecular characterization of gp40, a mucin-type glycoprotein from the apical plasma membrane of Madin-Darby canine kidney cells (type I). Biochem J 326:99-108
    • (1997) Biochem J , vol.326 , pp. 99-108
    • Zimmer, G.1    Lottspeich, F.2    Maisner, A.3    Klenk, H.D.4    Herrler, G.5
  • 82
    • 0028058925 scopus 로고
    • Persistent influenza C virus possesses distinct functional properties due to a modified HEF glycoprotein
    • Marschall M, Herrler G, Boswald C, Foerst G, Meier-Ewert H (1994) Persistent influenza C virus possesses distinct functional properties due to a modified HEF glycoprotein. J Gen Virol 75:2189-2196
    • (1994) J Gen Virol , vol.75 , pp. 2189-2196
    • Marschall, M.1    Herrler, G.2    Boswald, C.3    Foerst, G.4    Meier-Ewert, H.5
  • 84
    • 0026776666 scopus 로고
    • A single point mutation of the influenza C virus glycoprotein (HEF) changes the viral receptor-binding activity
    • Szepanski S, Gross HJ, Brossmer R, Klenk HD, Herrler G (1992) A single point mutation of the influenza C virus glycoprotein (HEF) changes the viral receptor-binding activity. Virology 188:85-92
    • (1992) Virology , vol.188 , pp. 85-92
    • Szepanski, S.1    Gross, H.J.2    Brossmer, R.3    Klenk, H.D.4    Herrler, G.5
  • 86
    • 0030778595 scopus 로고    scopus 로고
    • Characterization of infectious salmon anemia virus, an orthomyxo-like virus isolated from Atlantic salmon (Salmo salar L.)
    • Falk K, Namork E, Rimstad E, Mjaaland S, Dannevig BH (1997) Characterization of infectious salmon anemia virus, an orthomyxo-like virus isolated from Atlantic salmon (Salmo salar L.). J Virol 71:9016-9023
    • (1997) J Virol , vol.71 , pp. 9016-9023
    • Falk, K.1    Namork, E.2    Rimstad, E.3    Mjaaland, S.4    Dannevig, B.H.5
  • 87
    • 0036844206 scopus 로고    scopus 로고
    • Characterization of the receptordestroying enzyme activity from infectious salmon anaemia virus
    • Kristiansen M, Froystad MK, Rishovd AL, Gjoen T (2002) Characterization of the receptordestroying enzyme activity from infectious salmon anaemia virus. J Gen Virol 83:2693-2697
    • (2002) J Gen Virol , vol.83 , pp. 2693-2697
    • Kristiansen, M.1    Froystad, M.K.2    Rishovd, A.L.3    Gjoen, T.4
  • 88
    • 1542377444 scopus 로고    scopus 로고
    • Infectious salmon anemia virus specifically binds to and hydrolyzes 4-O-acetylated sialic acids
    • Hellebo A, Vilas U, Falk K, Vlasak R (2004) Infectious salmon anemia virus specifically binds to and hydrolyzes 4-O-acetylated sialic acids. J Virol 78:3055-3062
    • (2004) J Virol , vol.78 , pp. 3055-3062
    • Hellebo, A.1    Vilas, U.2    Falk, K.3    Vlasak, R.4
  • 89
    • 1542317650 scopus 로고    scopus 로고
    • Identification and characterization of viral structural proteins of infectious salmon anemia virus
    • Falk K, Aspehaug V, Vlasak R, Endresen C (2004) Identification and characterization of viral structural proteins of infectious salmon anemia virus. J Virol 78:3063-3071
    • (2004) J Virol , vol.78 , pp. 3063-3071
    • Falk, K.1    Aspehaug, V.2    Vlasak, R.3    Endresen, C.4
  • 91
    • 0035037385 scopus 로고    scopus 로고
    • Characterization of the infectious salmon anemia virus genomic segment that encodes the putative hemagglutinin
    • Rimstad E, Mjaaland S, Snow M, Mikalsen AB, Cunningham CO (2001) Characterization of the infectious salmon anemia virus genomic segment that encodes the putative hemagglutinin. J Virol 75:5352-5356
    • (2001) J Virol , vol.75 , pp. 5352-5356
    • Rimstad, E.1    Mjaaland, S.2    Snow, M.3    Mikalsen, A.B.4    Cunningham, C.O.5
  • 92
    • 0001515909 scopus 로고
    • Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses
    • Vlasak R, Luytjes W, Spaan W, Palese P (1988) Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses. Proc Natl Acad Sci U S A 85:4526-4529
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 4526-4529
    • Vlasak, R.1    Luytjes, W.2    Spaan, W.3    Palese, P.4
  • 93
    • 0026023775 scopus 로고
    • Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity
    • Schultze B, Wahn K, Klenk HD, Herrler G (1991) Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity. Virology 180:221-228
    • (1991) Virology , vol.180 , pp. 221-228
    • Schultze, B.1    Wahn, K.2    Klenk, H.D.3    Herrler, G.4
  • 94
    • 0024268308 scopus 로고
    • The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity
    • Vlasak R, Luytjes W, Leider J, Spaan W, Palese P (1988) The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity. J Virol 62:4686-4690
    • (1988) J Virol , vol.62 , pp. 4686-4690
    • Vlasak, R.1    Luytjes, W.2    Leider, J.3    Spaan, W.4    Palese, P.5
  • 95
    • 0024827047 scopus 로고
    • Biosynthesis, structure, and biological activities of envelope protein gp65 of murine coronavirus
    • Yokomori K, La Monica N, Makino S, Shieh CK, Lai MM (1989) Biosynthesis, structure, and biological activities of envelope protein gp65 of murine coronavirus. Virology 173:683-691
    • (1989) Virology , vol.173 , pp. 683-691
    • Yokomori, K.1    La Monica, N.2    Makino, S.3    Shieh, C.K.4    Lai, M.M.5
  • 96
    • 48249140239 scopus 로고    scopus 로고
    • Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution
    • Zeng Q, Langereis MA, van Vliet AL, Huizinga EG, de Groot RJ (2008) Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution. Proc Natl Acad Sci U S A 105:9065-9069
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9065-9069
    • Zeng, Q.1    Langereis, M.A.2    van Vliet, A.L.3    Huizinga, E.G.4    de Groot, R.J.5
  • 97
    • 0031668026 scopus 로고    scopus 로고
    • Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice)
    • Sugiyama K, Kasai M, Kato S, Kasai H, Hatakeyama K (1998) Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice). Arch Virol 143:1523-1534
    • (1998) Arch Virol , vol.143 , pp. 1523-1534
    • Sugiyama, K.1    Kasai, M.2    Kato, S.3    Kasai, H.4    Hatakeyama, K.5
  • 98
    • 0032901056 scopus 로고    scopus 로고
    • Identification of a coronavirus hemagglutinin-esterase with a substrate specificity different from those of influenza C virus and bovine coronavirus
    • Klausegger A, Strobl B, Regl G, Kaser A, Luytjes W, Vlasak R (1999) Identification of a coronavirus hemagglutinin-esterase with a substrate specificity different from those of influenza C virus and bovine coronavirus. J Virol 73:3737-3743
    • (1999) J Virol , vol.73 , pp. 3737-3743
    • Klausegger, A.1    Strobl, B.2    Regl, G.3    Kaser, A.4    Luytjes, W.5    Vlasak, R.6
  • 100
  • 101
    • 0026479482 scopus 로고
    • Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains
    • Storz J, Zhang XM, Rott R (1992) Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains. Arch Virol 125:193-204
    • (1992) Arch Virol , vol.125 , pp. 193-204
    • Storz, J.1    Zhang, X.M.2    Rott, R.3
  • 102
    • 0026505695 scopus 로고
    • Bovine coronavirus uses N-acetyl-9-O-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells
    • Schultze B, Herrler G (1992) Bovine coronavirus uses N-acetyl-9-O-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells. J Gen Virol 73:901-906
    • (1992) J Gen Virol , vol.73 , pp. 901-906
    • Schultze, B.1    Herrler, G.2
  • 103
    • 0031253694 scopus 로고    scopus 로고
    • Infection of polarized epithelial cells with enteric and respiratory tract bovine coronaviruses and release of virus progeny
    • Lin X, O'Reilly KL, Storz J (1997) Infection of polarized epithelial cells with enteric and respiratory tract bovine coronaviruses and release of virus progeny. Am J Vet Res 58:1120-1124
    • (1997) Am J Vet Res , vol.58 , pp. 1120-1124
    • Lin, X.1    O'Reilly, K.L.2    Storz, J.3
  • 104
    • 0030004116 scopus 로고    scopus 로고
    • Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-glycolylneuraminic acid) binding activity
    • Schultze B, Krempl C, Ballesteros ML, Shaw L, Schauer R, Enjuanes L, Herrler G (1996) Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-glycolylneuraminic acid) binding activity. J Virol 70:5634-5637
    • (1996) J Virol , vol.70 , pp. 5634-5637
    • Schultze, B.1    Krempl, C.2    Ballesteros, M.L.3    Shaw, L.4    Schauer, R.5    Enjuanes, L.6    Herrler, G.7
  • 105
    • 0030001570 scopus 로고    scopus 로고
    • Virus entry into a polarized epithelial cell line (MDCK): Similarities and dissimilarities between influenza C virus and bovine coronavirus
    • Schultze B, Zimmer G, Herrler G (1996) Virus entry into a polarized epithelial cell line (MDCK): similarities and dissimilarities between influenza C virus and bovine coronavirus. J Gen Virol 77(Pt 10):2507-2514
    • (1996) J Gen Virol , vol.77 , pp. 2507-2514
    • Schultze, B.1    Zimmer, G.2    Herrler, G.3
  • 106
    • 0021925755 scopus 로고
    • Bovine coronavirus hemagglutinin protein
    • King B, Potts BJ, Brian DA (1985) Bovine coronavirus hemagglutinin protein. Virus Res 2:53-59
    • (1985) Virus Res , vol.2 , pp. 53-59
    • King, B.1    Potts, B.J.2    Brian, D.A.3
  • 107
    • 0026649297 scopus 로고
    • Synthesis and processing of the haemagglutinin-esterase glycoprotein of bovine coronavirus encoded in the E3 region of adenovirus
    • Yoo D, Graham FL, Prevec L, Parker MD, Benko M, Zamb T, Babiuk LA (1992) Synthesis and processing of the haemagglutinin-esterase glycoprotein of bovine coronavirus encoded in the E3 region of adenovirus. J Gen Virol 73:2591-2600
    • (1992) J Gen Virol , vol.73 , pp. 2591-2600
    • Yoo, D.1    Graham, F.L.2    Prevec, L.3    Parker, M.D.4    Benko, M.5    Zamb, T.6    Babiuk, L.A.7
  • 108
    • 0026085172 scopus 로고
    • The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant
    • Schultze B, Gross HJ, Brossmer R, Herrler G (1991) The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant. J Virol 65:6232-6237
    • (1991) J Virol , vol.65 , pp. 6232-6237
    • Schultze, B.1    Gross, H.J.2    Brossmer, R.3    Herrler, G.4
  • 109
    • 0028813624 scopus 로고
    • Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein
    • Gagneten S, Gout O, Dubois-Dalcq M, Rottier P, Rossen J, Holmes KV (1995) Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein. J Virol 69:889-895
    • (1995) J Virol , vol.69 , pp. 889-895
    • Gagneten, S.1    Gout, O.2    Dubois-Dalcq, M.3    Rottier, P.4    Rossen, J.5    Holmes, K.V.6
  • 110
    • 77956622340 scopus 로고    scopus 로고
    • Attachment of mouse hepatitis virus to O-acetylated sialic acid is mediated by hemagglutinin-esterase and not by the spike protein
    • Langereis MA, van Vliet AL, Boot W, de Groot RJ (2010) Attachment of mouse hepatitis virus to O-acetylated sialic acid is mediated by hemagglutinin-esterase and not by the spike protein. J Virol 84:8970-8974
    • (2010) J Virol , vol.84 , pp. 8970-8974
    • Langereis, M.A.1    van Vliet, A.L.2    Boot, W.3    de Groot, R.J.4
  • 111
    • 0023731601 scopus 로고
    • Physicochemical properties of transmissible gastroenteritis virus hemagglutinin
    • Noda M, Koide F, Asagi M, Inaba Y (1988) Physicochemical properties of transmissible gastroenteritis virus hemagglutinin. Arch Virol 99:163-172
    • (1988) Arch Virol , vol.99 , pp. 163-172
    • Noda, M.1    Koide, F.2    Asagi, M.3    Inaba, Y.4
  • 113
    • 0030893578 scopus 로고    scopus 로고
    • Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus
    • Krempl C, Schultze B, Laude H, Herrler G (1997) Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus. J Virol 71:3285-3287
    • (1997) J Virol , vol.71 , pp. 3285-3287
    • Krempl, C.1    Schultze, B.2    Laude, H.3    Herrler, G.4
  • 114
    • 0029092240 scopus 로고
    • Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity
    • Bernard S, Laude H (1995) Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity. J Gen Virol 76:2235-2241
    • (1995) J Gen Virol , vol.76 , pp. 2235-2241
    • Bernard, S.1    Laude, H.2
  • 115
    • 0033957648 scopus 로고    scopus 로고
    • Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants
    • Krempl C, Ballesteros ML, Zimmer G, Enjuanes L, Klenk HD, Herrler G (2000) Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants. J Gen Virol 81:489-496
    • (2000) J Gen Virol , vol.81 , pp. 489-496
    • Krempl, C.1    Ballesteros, M.L.2    Zimmer, G.3    Enjuanes, L.4    Klenk, H.D.5    Herrler, G.6
  • 116
    • 0142060813 scopus 로고    scopus 로고
    • Binding of transmissible gastroenteritis coronavirus to brush border membrane sialoglycoproteins
    • Schwegmann-Wessels C, Zimmer G, Schroder B, Breves G, Herrler G (2003) Binding of transmissible gastroenteritis coronavirus to brush border membrane sialoglycoproteins. J Virol 77:11846-11848
    • (2003) J Virol , vol.77 , pp. 11846-11848
    • Schwegmann-Wessels, C.1    Zimmer, G.2    Schroder, B.3    Breves, G.4    Herrler, G.5
  • 117
    • 0022746697 scopus 로고
    • Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis
    • Pensaert M, Callebaut P, Vergote J (1986) Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis. Vet Q 8:257-261
    • (1986) Vet Q , vol.8 , pp. 257-261
    • Pensaert, M.1    Callebaut, P.2    Vergote, J.3
  • 119
    • 0025033329 scopus 로고
    • Intestinal replication of a porcine respiratory coronavirus closely related antigenically to the enteric transmissible gastroenteritis virus
    • Cox E, Pensaert MB, Callebaut P, van Deun K (1990) Intestinal replication of a porcine respiratory coronavirus closely related antigenically to the enteric transmissible gastroenteritis virus. Vet Microbiol 23:237-243
    • (1990) Vet Microbiol , vol.23 , pp. 237-243
    • Cox, E.1    Pensaert, M.B.2    Callebaut, P.3    van Deun, K.4
  • 120
    • 0036102184 scopus 로고    scopus 로고
    • Binding of transmissible gastroenteritis coronavirus to cell surface sialoglycoproteins
    • Schwegmann-Wessels C, Zimmer G, Laude H, Enjuanes L, Herrler G (2002) Binding of transmissible gastroenteritis coronavirus to cell surface sialoglycoproteins. J Virol 76:6037-6043
    • (2002) J Virol , vol.76 , pp. 6037-6043
    • Schwegmann-Wessels, C.1    Zimmer, G.2    Laude, H.3    Enjuanes, L.4    Herrler, G.5
  • 121
    • 80052555424 scopus 로고    scopus 로고
    • The sialic acid binding activity of the S protein facilitates infection by porcine transmissible gastroenteritis coronavirus
    • Schwegmann-Wessels C, Bauer S, Winter C, Enjuanes L, Laude H, Herrler G (2011) The sialic acid binding activity of the S protein facilitates infection by porcine transmissible gastroenteritis coronavirus. Virol J 8:435
    • (2011) Virol J , vol.8 , pp. 435
    • Schwegmann-Wessels, C.1    Bauer, S.2    Winter, C.3    Enjuanes, L.4    Laude, H.5    Herrler, G.6
  • 122
    • 0016769167 scopus 로고
    • Haemagglutination by avian infectious bronchitis virus-a coronavirus
    • Bingham RW, Madge MH, Tyrrell DA (1975) Haemagglutination by avian infectious bronchitis virus-a coronavirus. J Gen Virol 28:381-390
    • (1975) J Gen Virol , vol.28 , pp. 381-390
    • Bingham, R.W.1    Madge, M.H.2    Tyrrell, D.A.3
  • 123
    • 0026685054 scopus 로고
    • Neuraminidase treatment of avian infectious bronchitis coronavirus reveals a hemagglutinating activity that is dependent on sialic acidcontaining receptors on erythrocytes
    • Schultze B, Cavanagh D, Herrler G (1992) Neuraminidase treatment of avian infectious bronchitis coronavirus reveals a hemagglutinating activity that is dependent on sialic acidcontaining receptors on erythrocytes. Virology 189:792-794
    • (1992) Virology , vol.189 , pp. 792-794
    • Schultze, B.1    Cavanagh, D.2    Herrler, G.3
  • 124
    • 33646155945 scopus 로고    scopus 로고
    • Sialic acid is a receptor determinant for infection of cells by avian infectious bronchitis virus
    • Winter C, Schwegmann-Wessels C, Cavanagh D, Neumann U, Herrler G (2006) Sialic acid is a receptor determinant for infection of cells by avian infectious bronchitis virus. J Gen Virol 87:1209-1216
    • (2006) J Gen Virol , vol.87 , pp. 1209-1216
    • Winter, C.1    Schwegmann-Wessels, C.2    Cavanagh, D.3    Neumann, U.4    Herrler, G.5
  • 125
    • 60549097922 scopus 로고    scopus 로고
    • Comparative analysis of the sialic acid binding activity and the tropism for the respiratory epithelium of four different strains of avian infectious bronchitis virus
    • Abd El Rahman S, El-Kenawy AA, Neumann U, Herrler G, Winter C (2009) Comparative analysis of the sialic acid binding activity and the tropism for the respiratory epithelium of four different strains of avian infectious bronchitis virus. Avian Pathol 38:41-45
    • (2009) Avian Pathol , vol.38 , pp. 41-45
    • Abd El Rahman, S.1    El-Kenawy, A.A.2    Neumann, U.3    Herrler, G.4    Winter, C.5
  • 126
    • 77956638445 scopus 로고    scopus 로고
    • Differential sensitivity of well-differentiated avian respiratory epithelial cells to infection by different strains of infectious bronchitis virus
    • Abd El Rahman S, Winter C, El-Kenawy A, Neumann U, Herrler G (2010) Differential sensitivity of well-differentiated avian respiratory epithelial cells to infection by different strains of infectious bronchitis virus. J Virol 84:8949-8952
    • (2010) J Virol , vol.84 , pp. 8949-8952
    • Abd El Rahman, S.1    Winter, C.2    El-Kenawy, A.3    Neumann, U.4    Herrler, G.5
  • 127
    • 42649093768 scopus 로고    scopus 로고
    • Infection of the tracheal epithelium by infectious bronchitis virus is sialic acid dependent
    • Winter C, Herrler G, Neumann U (2008) Infection of the tracheal epithelium by infectious bronchitis virus is sialic acid dependent. Microbes Infect 10:367-373
    • (2008) Microbes Infect , vol.10 , pp. 367-373
    • Winter, C.1    Herrler, G.2    Neumann, U.3
  • 129
    • 0032824287 scopus 로고    scopus 로고
    • The novel hemagglutinin-esterase genes of human torovirus and Breda virus
    • Duckmanton L, Tellier R, Richardson C, Petric M (1999) The novel hemagglutinin-esterase genes of human torovirus and Breda virus. Virus Res 64:137-149
    • (1999) Virus Res , vol.64 , pp. 137-149
    • Duckmanton, L.1    Tellier, R.2    Richardson, C.3    Petric, M.4
  • 131
    • 34547601896 scopus 로고    scopus 로고
    • Paramyxoviridae: The viruses and their replication
    • Knipe DM, Howley PM (eds), Lippincott, Williams and Wilkins, Philadelphia
    • Lamb RA, Parks GD (2007) Paramyxoviridae: the viruses and their replication. In: Knipe DM, Howley PM (eds) Fields Virology. Lippincott, Williams and Wilkins, Philadelphia, pp 1449-1496
    • (2007) Fields Virology , pp. 1449-1496
    • Lamb, R.A.1    Parks, G.D.2
  • 132
    • 1842614339 scopus 로고    scopus 로고
    • Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: Implications for fusion
    • Zaitsev V, von Itzstein M, Groves D, Kiefel M, Takimoto T, Portner A, Taylor G (2004) Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion. J Virol 78:3733-3741
    • (2004) J Virol , vol.78 , pp. 3733-3741
    • Zaitsev, V.1    von Itzstein, M.2    Groves, D.3    Kiefel, M.4    Takimoto, T.5    Portner, A.6    Taylor, G.7
  • 134
    • 18944375873 scopus 로고    scopus 로고
    • Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose
    • Yuan P, Thompson TB, Wurzburg BA, Paterson RG, Lamb RA, Jardetzky TS (2005) Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose. Structure 13:803-815
    • (2005) Structure , vol.13 , pp. 803-815
    • Yuan, P.1    Thompson, T.B.2    Wurzburg, B.A.3    Paterson, R.G.4    Lamb, R.A.5    Jardetzky, T.S.6
  • 135
    • 50149118372 scopus 로고    scopus 로고
    • Loss of the N-linked glycan at residue 173 of human parainfluenza virus type 1 hemagglutinin-neuraminidase exposes a second receptor-binding site
    • Alymova IV, Taylor G, Mishin VP, Watanabe M, Murti KG, Boyd K, Chand P, Babu YS, Portner A (2008) Loss of the N-linked glycan at residue 173 of human parainfluenza virus type 1 hemagglutinin-neuraminidase exposes a second receptor-binding site. J Virol 82:8400-8410
    • (2008) J Virol , vol.82 , pp. 8400-8410
    • Alymova, I.V.1    Taylor, G.2    Mishin, V.P.3    Watanabe, M.4    Murti, K.G.5    Boyd, K.6    Chand, P.7    Babu, Y.S.8    Portner, A.9
  • 136
    • 0018848822 scopus 로고
    • Sendai virus receptor: Proposed recognition structure based on binding to plastic-adsorbed gangliosides
    • Holmgren J, Svennerholm L, Elwing H, Fredman P, Strannegard O (1980) Sendai virus receptor: proposed recognition structure based on binding to plastic-adsorbed gangliosides. Proc Natl Acad Sci U S A 77:1947-1950
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 1947-1950
    • Holmgren, J.1    Svennerholm, L.2    Elwing, H.3    Fredman, P.4    Strannegard, O.5
  • 137
    • 0000877438 scopus 로고
    • Specific gangliosides function as host cell receptors for Sendai virus
    • Markwell MA, Svennerholm L, Paulson JC (1981) Specific gangliosides function as host cell receptors for Sendai virus. Proc Natl Acad Sci U S A 78:5406-5410
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 5406-5410
    • Markwell, M.A.1    Svennerholm, L.2    Paulson, J.C.3
  • 138
    • 0011822536 scopus 로고
    • Sendai virus utilizes specific sialyloligosaccharides as host cell receptor determinants
    • Markwell MA, Paulson JC (1980) Sendai virus utilizes specific sialyloligosaccharides as host cell receptor determinants. Proc Natl Acad Sci U S A 77:5693-5697
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 5693-5697
    • Markwell, M.A.1    Paulson, J.C.2
  • 139
    • 0020770775 scopus 로고
    • Isolation and characterization of receptor sialoglycoprotein for hemagglutinating virus of Japan (Sendai virus) from bovine erythrocyte membrane
    • Suzuki Y, Suzuki T, MatsumotoM(1983) Isolation and characterization of receptor sialoglycoprotein for hemagglutinating virus of Japan (Sendai virus) from bovine erythrocyte membrane. J Biochem 93:1621-1633
    • (1983) J Biochem , vol.93 , pp. 1621-1633
    • Suzuki, Y.1    Suzuki, T.2    Matsumoto, M.3
  • 140
    • 0021908023 scopus 로고
    • Gangliosides as paramyxovirus receptor. Structural requirement of sialo-oligosaccharides in receptors for hemagglutinating virus of Japan (Sendai virus) and Newcastle disease virus
    • Suzuki Y, Suzuki T, Matsunaga M, Matsumoto M (1985) Gangliosides as paramyxovirus receptor. Structural requirement of sialo-oligosaccharides in receptors for hemagglutinating virus of Japan (Sendai virus) and Newcastle disease virus. J Biochem 97:1189-1199
    • (1985) J Biochem , vol.97 , pp. 1189-1199
    • Suzuki, Y.1    Suzuki, T.2    Matsunaga, M.3    Matsumoto, M.4
  • 143
    • 0028321481 scopus 로고
    • Three-dimensional structure of baculovirus-expressed Norwalk virus capsids
    • Prasad BV, Rothnagel R, Jiang X, Estes MK (1994) Three-dimensional structure of baculovirus-expressed Norwalk virus capsids. J Virol 68:5117-5125
    • (1994) J Virol , vol.68 , pp. 5117-5125
    • Prasad, B.V.1    Rothnagel, R.2    Jiang, X.3    Estes, M.K.4
  • 144
    • 43949129092 scopus 로고    scopus 로고
    • Structural basis for the receptor binding specificity of Norwalk virus
    • Bu W, Mamedova A, Tan M, Xia M, Jiang X, Hegde RS (2008) Structural basis for the receptor binding specificity of Norwalk virus. J Virol 82:5340-5347
    • (2008) J Virol , vol.82 , pp. 5340-5347
    • Bu, W.1    Mamedova, A.2    Tan, M.3    Xia, M.4    Jiang, X.5    Hegde, R.S.6
  • 146
    • 48249142845 scopus 로고    scopus 로고
    • Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus
    • Choi JM, Hutson AM, Estes MK, Prasad BV (2008) Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus. Proc Natl Acad Sci U S A 105:9175-9180
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9175-9180
    • Choi, J.M.1    Hutson, A.M.2    Estes, M.K.3    Prasad, B.V.4
  • 147
    • 77951983848 scopus 로고    scopus 로고
    • High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains
    • Katpally U, Voss NR, Cavazza T, Taube S, Rubin JR, Young VL, Stuckey J, Ward VK, Virgin HWT, Wobus CE et al. (2010) High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains. J Virol 84:5836-5841
    • (2010) J Virol , vol.84 , pp. 5836-5841
    • Katpally, U.1    Voss, N.R.2    Cavazza, T.3    Taube, S.4    Rubin, J.R.5    Young, V.L.6    Stuckey, J.7    Ward, V.K.8    Virgin, H.W.T.9    Wobus, C.E.10
  • 148
    • 77951986493 scopus 로고    scopus 로고
    • Highresolution X-ray structure and functional analysis of the murine norovirus 1 capsid protein protruding domain
    • Taube S, Rubin JR, Katpally U, Smith TJ, Kendall A, Stuckey JA, Wobus CE (2010) Highresolution X-ray structure and functional analysis of the murine norovirus 1 capsid protein protruding domain. J Virol 84:5695-5705
    • (2010) J Virol , vol.84 , pp. 5695-5705
    • Taube, S.1    Rubin, J.R.2    Katpally, U.3    Smith, T.J.4    Kendall, A.5    Stuckey, J.A.6    Wobus, C.E.7
  • 149
    • 33646718792 scopus 로고    scopus 로고
    • Murine norovirus: A model system to study norovirus biology and pathogenesis
    • Wobus CE, Thackray LB, Virgin HWT (2006) Murine norovirus: a model system to study norovirus biology and pathogenesis. J Virol 80:5104-5112
    • (2006) J Virol , vol.80 , pp. 5104-5112
    • Wobus, C.E.1    Thackray, L.B.2    Virgin, H.W.T.3
  • 152
    • 34547459640 scopus 로고    scopus 로고
    • Norovirus-host interaction: Implications for disease control and prevention
    • Tan M, Jiang X (2007) Norovirus-host interaction: implications for disease control and prevention. Expert Rev Mol Med 9:1-22
    • (2007) Expert Rev Mol Med , vol.9 , pp. 1-22
    • Tan, M.1    Jiang, X.2
  • 153
    • 1842589456 scopus 로고    scopus 로고
    • Genogroup II noroviruses efficiently bind to heparan sulfate proteoglycan associated with the cellular membrane
    • Tamura M, Natori K, Kobayashi M, Miyamura T, Takeda N (2004) Genogroup II noroviruses efficiently bind to heparan sulfate proteoglycan associated with the cellular membrane. J Virol 78:3817-3826
    • (2004) J Virol , vol.78 , pp. 3817-3826
    • Tamura, M.1    Natori, K.2    Kobayashi, M.3    Miyamura, T.4    Takeda, N.5
  • 155
  • 156
    • 33846169715 scopus 로고    scopus 로고
    • Alpha2,6-linked sialic acid acts as a receptor for Feline calicivirus
    • Stuart AD, Brown TD (2007) Alpha2,6-linked sialic acid acts as a receptor for Feline calicivirus. J Gen Virol 88:177-186
    • (2007) J Gen Virol , vol.88 , pp. 177-186
    • Stuart, A.D.1    Brown, T.D.2
  • 157
    • 0025602404 scopus 로고
    • Evidence for a direct role for sialic acid in the attachment of encephalomyocarditis virus to human erythrocytes
    • Tavakkol A, Burness AT (1990) Evidence for a direct role for sialic acid in the attachment of encephalomyocarditis virus to human erythrocytes. Biochemistry 29:10684-10690
    • (1990) Biochemistry , vol.29 , pp. 10684-10690
    • Tavakkol, A.1    Burness, A.T.2
  • 158
    • 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 (2000) Sialylation of the host receptor may modulate entry of demyelinating persistent Theiler's virus. J Virol 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
  • 159
    • 0023139727 scopus 로고
    • Biological properties of mengovirus: Characterization of avirulent, hemagglutination-defective mutants
    • Anderson K, Bond CW (1987) Biological properties of mengovirus: characterization of avirulent, hemagglutination-defective mutants. Arch Virol 93:31-49
    • (1987) Arch Virol , vol.93 , pp. 31-49
    • Anderson, K.1    Bond, C.W.2
  • 160
    • 0015861473 scopus 로고
    • Effect of neuraminidase pretreatment on the susceptibility of normal and transformed mammalian cells to bovine enterovirus 261
    • Stoner GD, Williams B, Kniazeff A, Shimkin MB (1973) Effect of neuraminidase pretreatment on the susceptibility of normal and transformed mammalian cells to bovine enterovirus 261. Nature 245:319-320
    • (1973) Nature , vol.245 , pp. 319-320
    • Stoner, G.D.1    Williams, B.2    Kniazeff, A.3    Shimkin, M.B.4
  • 162
    • 21344444595 scopus 로고    scopus 로고
    • Theiler's virus persistence in the central nervous system of mice is associated with continuous viral replication and a difference in outcome of infection of infiltrating macrophages versus oligodendrocytes
    • Lipton HL, Kumar AS, Trottier M (2005) Theiler's virus persistence in the central nervous system of mice is associated with continuous viral replication and a difference in outcome of infection of infiltrating macrophages versus oligodendrocytes. Virus Res 111:214-223
    • (2005) Virus Res , vol.111 , pp. 214-223
    • Lipton, H.L.1    Kumar, A.S.2    Trottier, M.3
  • 163
    • 0038082242 scopus 로고    scopus 로고
    • The viral sigma1 protein and glycoconjugates containing alpha2-3-linked sialic acid are involved in type 1 reovirus adherence to M cell apical surfaces
    • Helander A, Silvey KJ, Mantis NJ, Hutchings AB, Chandran K, Lucas WT, Nibert ML, Neutra MR (2003) The viral sigma1 protein and glycoconjugates containing alpha2-3-linked sialic acid are involved in type 1 reovirus adherence to M cell apical surfaces. J Virol 77:7964-7977
    • (2003) J Virol , vol.77 , pp. 7964-7977
    • Helander, A.1    Silvey, K.J.2    Mantis, N.J.3    Hutchings, A.B.4    Chandran, K.5    Lucas, W.T.6    Nibert, M.L.7    Neutra, M.R.8
  • 164
    • 0035910468 scopus 로고    scopus 로고
    • Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening
    • Barton ES, Connolly JL, Forrest JC, Chappell JD, Dermody TS (2001) Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening. J Biol Chem 276:2200-2211
    • (2001) J Biol Chem , vol.276 , pp. 2200-2211
    • Barton, E.S.1    Connolly, J.L.2    Forrest, J.C.3    Chappell, J.D.4    Dermody, T.S.5
  • 166
    • 0035043244 scopus 로고    scopus 로고
    • Reovirus binding to cell surface sialic acid potentiates virus-induced apoptosis
    • Connolly JL, Barton ES, Dermody TS (2001) Reovirus binding to cell surface sialic acid potentiates virus-induced apoptosis. J Virol 75:4029-4039
    • (2001) J Virol , vol.75 , pp. 4029-4039
    • Connolly, J.L.1    Barton, E.S.2    Dermody, T.S.3
  • 167
    • 0036500085 scopus 로고    scopus 로고
    • The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site
    • Dormitzer PR, Sun ZY, Wagner G, Harrison SC (2002) The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site. EMBO J 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
  • 168
    • 58949100353 scopus 로고    scopus 로고
    • Effects on sialic acid recognition of amino acid mutations in the carbohydrate-binding cleft of the rotavirus spike protein
    • Kraschnefski MJ, Bugarcic A, Fleming FE, Yu X, von Itzstein M, Coulson BS, Blanchard H (2009) Effects on sialic acid recognition of amino acid mutations in the carbohydrate-binding cleft of the rotavirus spike protein. Glycobiology 19:194-200
    • (2009) Glycobiology , vol.19 , pp. 194-200
    • Kraschnefski, M.J.1    Bugarcic, A.2    Fleming, F.E.3    Yu, X.4    von Itzstein, M.5    Coulson, B.S.6    Blanchard, H.7
  • 169
    • 0018911088 scopus 로고
    • Attachment of SA-11 rotavirus to erythrocyte receptors
    • Bastardo JW, Holmes IH (1980) Attachment of SA-11 rotavirus to erythrocyte receptors. Infect Immun 29:1134-1140
    • (1980) Infect Immun , vol.29 , pp. 1134-1140
    • Bastardo, J.W.1    Holmes, I.H.2
  • 171
    • 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 MK (1999) Human and most animal rotavirus strains do not require the presence of sialic acid on the cell surface for efficient infectivity. J Gen Virol 80:943-948
    • (1999) J Gen Virol , vol.80 , pp. 943-948
    • Ciarlet, M.1    Estes, M.K.2
  • 172
    • 58249112782 scopus 로고    scopus 로고
    • 'Sialidase sensitivity' of rotaviruses revisited
    • Banda K, Kang G, Varki A (2009) 'Sialidase sensitivity' of rotaviruses revisited. Nat Chem Biol 5:71-72
    • (2009) Nat Chem Biol , vol.5 , pp. 71-72
    • Banda, K.1    Kang, G.2    Varki, A.3
  • 174
    • 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 ZY, Prasad BV, Taniguchi K, Dormitzer PR (2006) High-resolution molecular and antigen structure of the VP8* core of a sialic acid-independent human rotavirus strain. J Virol 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
  • 176
    • 0036785609 scopus 로고    scopus 로고
    • Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core
    • Dormitzer PR, Sun ZY, Blixt O, Paulson JC, Wagner G, Harrison SC (2002) Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core. J Virol 76:10512-10517
    • (2002) J Virol , vol.76 , pp. 10512-10517
    • Dormitzer, P.R.1    Sun, Z.Y.2    Blixt, O.3    Paulson, J.C.4    Wagner, G.5    Harrison, S.C.6
  • 178
    • 0035128179 scopus 로고    scopus 로고
    • Glycosphingolipid binding specificities of rotavirus: Identification of a sialic acid-binding epitope
    • Delorme C, Brussow H, Sidoti J, Roche N, Karlsson KA, Neeser JR, Teneberg S (2001) Glycosphingolipid binding specificities of rotavirus: identification of a sialic acid-binding epitope. J Virol 75:2276-2287
    • (2001) J Virol , vol.75 , pp. 2276-2287
    • Delorme, C.1    Brussow, H.2    Sidoti, J.3    Roche, N.4    Karlsson, K.A.5    Neeser, J.R.6    Teneberg, S.7
  • 179
    • 0026094402 scopus 로고
    • Gangliosides as binding sites in SA-11 rotavirus infection of LLC-MK2 cells
    • Superti F, Donelli G (1991) Gangliosides as binding sites in SA-11 rotavirus infection of LLC-MK2 cells. J Gen Virol 72:2467-2474
    • (1991) J Gen Virol , vol.72 , pp. 2467-2474
    • Superti, F.1    Donelli, G.2
  • 182
    • 42449139527 scopus 로고    scopus 로고
    • Structural basis of GM1 ganglioside recognition by simian virus 40
    • Neu U, Woellner K, Gauglitz G, Stehle T (2008) Structural basis of GM1 ganglioside recognition by simian virus 40. Proc Natl Acad Sci U S A 105:5219-5224
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5219-5224
    • Neu, U.1    Woellner, K.2    Gauglitz, G.3    Stehle, T.4
  • 183
    • 0030839256 scopus 로고    scopus 로고
    • High-resolution structure of a polyomavirus VP1-oligosaccharide complex: Implications for assembly and receptor binding
    • Stehle T, Harrison SC (1997) High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding. EMBO J 16:5139-5148
    • (1997) EMBO J , vol.16 , pp. 5139-5148
    • Stehle, T.1    Harrison, S.C.2
  • 184
    • 0028303852 scopus 로고
    • Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment
    • Stehle T, Yan Y, Benjamin TL, Harrison SC (1994) Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment. Nature 369:160-163
    • (1994) Nature , vol.369 , pp. 160-163
    • Stehle, T.1    Yan, Y.2    Benjamin, T.L.3    Harrison, S.C.4
  • 185
    • 0018903946 scopus 로고
    • Polyoma virus adsorbs to specific sialyloligosaccharide receptors on erythrocytes
    • Cahan LD, Paulson JC (1980) Polyoma virus adsorbs to specific sialyloligosaccharide receptors on erythrocytes. Virology 103:505-509
    • (1980) Virology , vol.103 , pp. 505-509
    • Cahan, L.D.1    Paulson, J.C.2
  • 186
    • 0021086115 scopus 로고
    • Sialyloligosaccharide receptors of binding variants of polyoma virus
    • Cahan LD, Singh R, Paulson JC (1983) Sialyloligosaccharide receptors of binding variants of polyoma virus. Virology 130:281-289
    • (1983) Virology , vol.130 , pp. 281-289
    • Cahan, L.D.1    Singh, R.2    Paulson, J.C.3
  • 187
    • 0019382866 scopus 로고
    • Polyoma virus recognizes specific sialyligosaccharide receptors on host cells
    • Fried H, Cahan LD, Paulson JC (1981) Polyoma virus recognizes specific sialyligosaccharide receptors on host cells. Virology 109:188-192
    • (1981) Virology , vol.109 , pp. 188-192
    • Fried, H.1    Cahan, L.D.2    Paulson, J.C.3
  • 189
    • 0030584127 scopus 로고    scopus 로고
    • Crystal structures of murine polyomavirus in complex with straight-chain and branched-chain sialyloligosaccharide receptor fragments
    • Stehle T, Harrison SC (1996) Crystal structures of murine polyomavirus in complex with straight-chain and branched-chain sialyloligosaccharide receptor fragments. Structure 4:183-194
    • (1996) Structure , vol.4 , pp. 183-194
    • Stehle, T.1    Harrison, S.C.2
  • 190
    • 0037374763 scopus 로고    scopus 로고
    • Alpha4beta1 integrin acts as a cell receptor for murine polyomavirus at the postattachment level
    • Caruso M, Belloni L, Sthandier O, Amati P, Garcia MI (2003) Alpha4beta1 integrin acts as a cell receptor for murine polyomavirus at the postattachment level. J Virol 77:3913-3921
    • (2003) J Virol , vol.77 , pp. 3913-3921
    • Caruso, M.1    Belloni, L.2    Sthandier, O.3    Amati, P.4    Garcia, M.I.5
  • 192
    • 67650912077 scopus 로고    scopus 로고
    • A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection
    • Qian M, Cai D, Verhey KJ, Tsai B (2009) A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection. PLoS Pathog 5:e1000465
    • (2009) PLoS Pathog , vol.5
    • Qian, M.1    Cai, D.2    Verhey, K.J.3    Tsai, B.4
  • 193
    • 0028113951 scopus 로고
    • Regulation of susceptibility and cell surface receptor for the B-lymphotropic papovavirus by N glycosylation
    • Keppler OT, Herrmann M, Oppenlander M, Meschede W, Pawlita M (1994) Regulation of susceptibility and cell surface receptor for the B-lymphotropic papovavirus by N glycosylation. J Virol 68:6933-6939
    • (1994) J Virol , vol.68 , pp. 6933-6939
    • Keppler, O.T.1    Herrmann, M.2    Oppenlander, M.3    Meschede, W.4    Pawlita, M.5
  • 194
    • 39749155812 scopus 로고    scopus 로고
    • Direct correlation between sialic acid binding and infection of cells by two human polyomaviruses (JC virus and BK virus)
    • Dugan AS, Gasparovic ML, Atwood WJ (2008) Direct correlation between sialic acid binding and infection of cells by two human polyomaviruses (JC virus and BK virus). J Virol 82:2560-2564
    • (2008) J Virol , vol.82 , pp. 2560-2564
    • Dugan, A.S.1    Gasparovic, M.L.2    Atwood, W.J.3
  • 195
    • 0031950092 scopus 로고    scopus 로고
    • Infection of glial cells by the human polyomavirus JC is mediated by an N-linked glycoprotein containing terminal alpha(2-6)-linked sialic acids
    • Liu CK, Wei G, Atwood WJ (1998) Infection of glial cells by the human polyomavirus JC is mediated by an N-linked glycoprotein containing terminal alpha(2-6)-linked sialic acids. J Virol 72:4643-4649
    • (1998) J Virol , vol.72 , pp. 4643-4649
    • Liu, C.K.1    Wei, G.2    Atwood, W.J.3
  • 198
    • 27644460490 scopus 로고    scopus 로고
    • An N-linked glycoprotein with alpha(2,3)-linked sialic acid is a receptor for BK virus
    • Dugan AS, Eash S, Atwood WJ (2005) An N-linked glycoprotein with alpha(2,3)-linked sialic acid is a receptor for BK virus. J Virol 79:14442-14445
    • (2005) J Virol , vol.79 , pp. 14442-14445
    • Dugan, A.S.1    Eash, S.2    Atwood, W.J.3
  • 199
    • 31144470194 scopus 로고    scopus 로고
    • Identification of gangliosides GD1b and GT1b as receptors for BK virus
    • Low JA, Magnuson B, Tsai B, Imperiale MJ (2006) Identification of gangliosides GD1b and GT1b as receptors for BK virus. J Virol 80:1361-1366
    • (2006) J Virol , vol.80 , pp. 1361-1366
    • Low, J.A.1    Magnuson, B.2    Tsai, B.3    Imperiale, M.J.4
  • 200
    • 70349276758 scopus 로고    scopus 로고
    • Ganglioside GT1b is a putative host cell receptor for the Merkel cell polyomavirus
    • Erickson KD, Garcea RL, Tsai B (2009) Ganglioside GT1b is a putative host cell receptor for the Merkel cell polyomavirus. J Virol 83:10275-10279
    • (2009) J Virol , vol.83 , pp. 10275-10279
    • Erickson, K.D.1    Garcea, R.L.2    Tsai, B.3
  • 201
    • 0036434357 scopus 로고    scopus 로고
    • Adenovirus type 37 binds to cell surface sialic acid through a charge-dependent interaction
    • Arnberg N, Kidd AH, Edlund K, Nilsson J, Pring-Akerblom P, Wadell G (2002) Adenovirus type 37 binds to cell surface sialic acid through a charge-dependent interaction. Virology 302:33-43
    • (2002) Virology , vol.302 , pp. 33-43
    • Arnberg, N.1    Kidd, A.H.2    Edlund, K.3    Nilsson, J.4    Pring-Akerblom, P.5    Wadell, G.6
  • 202
    • 3142729320 scopus 로고    scopus 로고
    • Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites
    • Burmeister WP, Guilligay D, Cusack S, Wadell G, Arnberg N (2004) Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites. J Virol 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
  • 203
    • 33646723883 scopus 로고    scopus 로고
    • Gangliosides are essential for bovine adeno-associated virus entry
    • Schmidt M, Chiorini JA (2006) Gangliosides are essential for bovine adeno-associated virus entry. J Virol 80:5516-5522
    • (2006) J Virol , vol.80 , pp. 5516-5522
    • Schmidt, M.1    Chiorini, J.A.2
  • 204
    • 0034957168 scopus 로고    scopus 로고
    • Adeno-associated virus serotype 4 (AAV4) and AAV5 both require sialic acid binding for hemagglutination and efficient transduction but differ in sialic acid linkage specificity
    • Kaludov N, Brown KE, Walters RW, Zabner J, Chiorini JA (2001) Adeno-associated virus serotype 4 (AAV4) and AAV5 both require sialic acid binding for hemagglutination and efficient transduction but differ in sialic acid linkage specificity. J Virol 75:6884-6893
    • (2001) J Virol , vol.75 , pp. 6884-6893
    • Kaludov, N.1    Brown, K.E.2    Walters, R.W.3    Zabner, J.4    Chiorini, J.A.5
  • 205
    • 80052298685 scopus 로고    scopus 로고
    • Enhanced sialic acid-dependent endocytosis explains the increased efficiency of infection of airway epithelia by a novel adeno-associated virus
    • Dickey DD, Excoffon KJ, Koerber JT, Bergen J, Steines B, Klesney-Tait J, Schaffer DV, Zabner J (2011) Enhanced sialic acid-dependent endocytosis explains the increased efficiency of infection of airway epithelia by a novel adeno-associated virus. J Virol 85:9023-9030
    • (2011) J Virol , vol.85 , pp. 9023-9030
    • Dickey, D.D.1    Excoffon, K.J.2    Koerber, J.T.3    Bergen, J.4    Steines, B.5    Klesney-Tait, J.6    Schaffer, D.V.7    Zabner, J.8


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