메뉴 건너뛰기




Volumn 2, Issue 4, 2010, Pages 1011-1049

Glycosphingolipids as receptors for non-enveloped viruses

Author keywords

Calicivirus; Glycosphingolipid; Non enveloped virus; Parvovirus; Polyomavirus; Receptor; Rotavirus

Indexed keywords

FUCOSYLTRANSFERASE; GLOBOSIDE; GLYCOSPHINGOLIPID; SIALIDASE; VIRUS RECEPTOR;

EID: 78049507903     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v2041011     Document Type: Review
Times cited : (91)

References (215)
  • 1
    • 84974698845 scopus 로고    scopus 로고
    • Virus entry and uncoating
    • 5 ed.; Knipe, D. M., Howley, P. M., Ed. Wolters Kluwer: Philadelphia
    • Helenius, A. Virus entry and uncoating. In Fields Virology; 5 ed.; Knipe, D. M., Howley, P. M., Ed. Wolters Kluwer: Philadelphia, 2007; Vol. 1, pp. 99-118.
    • (2007) Fields Virology , vol.1 , pp. 99-118
    • Helenius, A.1
  • 2
    • 20344381822 scopus 로고    scopus 로고
    • Glycoconjugate glycans as viral receptors
    • Olofsson, S.; Bergstrom, T. Glycoconjugate glycans as viral receptors. Ann. Med. 2005, 37, 154-172.
    • (2005) Ann. Med , vol.37 , pp. 154-172
    • Olofsson, S.1    Bergstrom, T.2
  • 3
    • 34248661900 scopus 로고    scopus 로고
    • A new turning point in glycosphingolipid research
    • Iwamori, M. A new turning point in glycosphingolipid research. Hum. Cell 2005, 18, 117-133.
    • (2005) Hum. Cell , vol.18 , pp. 117-133
    • Iwamori, M.1
  • 5
    • 0037215494 scopus 로고    scopus 로고
    • Structure, organization, and function of glycosphingolipids in membrane
    • Hakomori, S. Structure, organization, and function of glycosphingolipids in membrane. Curr. Opin. Hematol. 2003, 10, 16-24.
    • (2003) Curr. Opin. Hematol , vol.10 , pp. 16-24
    • Hakomori, S.1
  • 6
    • 0032532863 scopus 로고    scopus 로고
    • IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN). Nomenclature of glycolipids--recommendations 1997
    • Chester, M.A. IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN). Nomenclature of glycolipids--recommendations 1997. Eur. J. Biochem. 1998, 257, 293-298.
    • (1998) Eur. J. Biochem , vol.257 , pp. 293-298
    • Chester, M.A.1
  • 7
    • 0028917379 scopus 로고
    • The P blood group system: Biochemical, serological, and clinical aspects
    • Spitalnik, P.F.; Spitalnik, S.L. The P blood group system: biochemical, serological, and clinical aspects. Transfus. Med. Rev. 1995, 9, 110-122.
    • (1995) Transfus. Med. Rev , vol.9 , pp. 110-122
    • Spitalnik, P.F.1    Spitalnik, S.L.2
  • 8
    • 0034444166 scopus 로고    scopus 로고
    • Traveling for the glycosphingolipid path
    • Hakomori, S. Traveling for the glycosphingolipid path. Glycoconj. J. 2000, 17, 627-647.
    • (2000) Glycoconj. J , vol.17 , pp. 627-647
    • Hakomori, S.1
  • 9
    • 0024339704 scopus 로고
    • Animal glycosphingolipids as membrane attachment sites for bacteria
    • Karlsson, K.A. Animal glycosphingolipids as membrane attachment sites for bacteria. Annu. Rev. Biochem. 1989, 58, 309-350.
    • (1989) Annu. Rev. Biochem , vol.58 , pp. 309-350
    • Karlsson, K.A.1
  • 10
    • 34548415971 scopus 로고    scopus 로고
    • Caliciviridae
    • ed.; D. M. Knipe, P. M. H., Ed. Lippincott Williams & Wilkins: Philadelphia
    • Green, K.Y. Caliciviridae. In Fields Virology; 5 ed.; D. M. Knipe, P. M. H., Ed. Lippincott Williams & Wilkins: Philadelphia, 2007; Vol. 1, pp. 949-980.
    • (2007) Fields Virology , vol.1 , pp. 949-980
    • Green, K.Y.1
  • 11
    • 43949129765 scopus 로고    scopus 로고
    • Characterization of a rhesus monkey calicivirus representing a new genus of Caliciviridae
    • Farkas, T.; Sestak, K.; Wei, C.; Jiang, X. Characterization of a rhesus monkey calicivirus representing a new genus of Caliciviridae. J. Virol. 2008, 82, 5408-5416.
    • (2008) J. Virol , vol.82 , pp. 5408-5416
    • Farkas, T.1    Sestak, K.2    Wei, C.3    Jiang, X.4
  • 12
    • 33745015266 scopus 로고    scopus 로고
    • Genomic characterization of the unclassified bovine enteric virus Newbury agent-1 (Newbury1) endorses a new genus in the family Caliciviridae
    • Oliver, S.L.; Asobayire, E.; Dastjerdi, A.M.; Bridger, J.C. Genomic characterization of the unclassified bovine enteric virus Newbury agent-1 (Newbury1) endorses a new genus in the family Caliciviridae. Virology 2006, 350, 240-250.
    • (2006) Virology , vol.350 , pp. 240-250
    • Oliver, S.L.1    Asobayire, E.2    Dastjerdi, A.M.3    Bridger, J.C.4
  • 13
    • 0034634331 scopus 로고    scopus 로고
    • Identification and genomic mapping of the ORF3 and VPg proteins in feline calicivirus virions
    • Sosnovtsev, S.V.; Green, K.Y. Identification and genomic mapping of the ORF3 and VPg proteins in feline calicivirus virions. Virology 2000, 277, 193-203.
    • (2000) Virology , vol.277 , pp. 193-203
    • Sosnovtsev, S.V.1    Green, K.Y.2
  • 14
    • 34648824648 scopus 로고    scopus 로고
    • Murine noroviruses comprising a single genogroup exhibit biological diversity despite limited sequence divergence
    • Thackray, L.B.; Wobus, C.E.; Chachu, K.A.; Liu, B.; Alegre, E.R.; Henderson, K.S.; Kelley, S.T.; Virgin, H.W. Murine noroviruses comprising a single genogroup exhibit biological diversity despite limited sequence divergence. J. Virol. 2007, 81, 10460-10473.
    • (2007) J. Virol , vol.81 , pp. 10460-10473
    • Thackray, L.B.1    Wobus, C.E.2    Chachu, K.A.3    Liu, B.4    Alegre, E.R.5    Henderson, K.S.6    Kelley, S.T.7    Virgin IV, H.W.8
  • 17
    • 0028321481 scopus 로고
    • Three-dimensional structure of baculovirus-expressed Norwalk virus capsids
    • Prasad, B.V.; Rothnagel, R.; Jiang, X.; Estes, M.K. Three-dimensional structure of baculovirus-expressed Norwalk virus capsids. J. Virol. 1994, 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
  • 18
    • 39749202900 scopus 로고    scopus 로고
    • Structure of antibody-neutralized murine norovirus and unexpected differences from viruslike particles
    • Katpally, U.; Wobus, C.E.; Dryden, K.; Virgin, H.W.; Smith, T.J. Structure of antibody-neutralized murine norovirus and unexpected differences from viruslike particles. J. Virol. 2008, 82, 2079-2088.
    • (2008) J. Virol , vol.82 , pp. 2079-2088
    • Katpally, U.1    Wobus, C.E.2    Dryden, K.3    Virgin IV, H.W.4    Smith, T.J.5
  • 19
    • 2642539948 scopus 로고    scopus 로고
    • Inter- and intragenus structural variations in caliciviruses and their functional implications
    • Chen, R.; Neill, J.D.; Noel, J.S.; Hutson, A.M.; Glass, R.I.; Estes, M.K.; Prasad, B.V. Inter- and intragenus structural variations in caliciviruses and their functional implications. J. Virol. 2004, 78, 6469-6479.
    • (2004) J. Virol , vol.78 , pp. 6469-6479
    • Chen, R.1    Neill, J.D.2    Noel, J.S.3    Hutson, A.M.4    Glass, R.I.5    Estes, M.K.6    Prasad, B.V.7
  • 20
    • 33744494819 scopus 로고    scopus 로고
    • X-ray structure of a native calicivirus: Structural insights into antigenic diversity and host specificity
    • Chen, R.; Neill, J.D.; Estes, M.K.; Prasad, B.V. X-ray structure of a native calicivirus: structural insights into antigenic diversity and host specificity. Proc. Natl. Acad. Sci. U. S. A. 2006, 103, 8048-8053.
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 8048-8053
    • Chen, R.1    Neill, J.D.2    Estes, M.K.3    Prasad, B.V.4
  • 21
    • 2642552973 scopus 로고    scopus 로고
    • The P domain of norovirus capsid protein forms dimer and binds to histo-blood group antigen receptors
    • Tan, M.; Hegde, R.S.; Jiang, X. The P domain of norovirus capsid protein forms dimer and binds to histo-blood group antigen receptors. J. Virol. 2004, 78, 6233-6242.
    • (2004) J. Virol , vol.78 , pp. 6233-6242
    • Tan, M.1    Hegde, R.S.2    Jiang, X.3
  • 22
    • 0036199391 scopus 로고    scopus 로고
    • Structural requirements for the assembly of Norwalk virus-like particles
    • Bertolotti-Ciarlet, A.; White, L.J.; Chen, R.; Prasad, B.V.; Estes, M.K. Structural requirements for the assembly of Norwalk virus-like particles. J. Virol. 2002, 76, 4044-4055.
    • (2002) J. Virol , vol.76 , pp. 4044-4055
    • Bertolotti-Ciarlet, A.1    White, L.J.2    Chen, R.3    Prasad, B.V.4    Estes, M.K.5
  • 24
    • 77951986493 scopus 로고    scopus 로고
    • High Resolution X-Ray Structure and Functional Analysis of the Murine Norovirus (MNV)-1 Capsid Protein Protruding (P) Domain
    • Taube, S.; Rubin, J.R.; Katpally, U.; Smith, T.J.; Kendall, A.; Stuckey, J.A.; Wobus, C.E. High Resolution X-Ray Structure and Functional Analysis of the Murine Norovirus (MNV)-1 Capsid Protein Protruding (P) Domain. J. Virol. 2010, [Epub ahead of print].
    • (2010) J. Virol
    • 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
  • 25
    • 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, R.S. Structural basis for the receptor binding specificity of Norwalk virus. J. Virol. 2008, 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
  • 26
    • 48249142845 scopus 로고    scopus 로고
    • Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus
    • Choi, J.M.; Hutson, A.M.; Estes, M.K.; Prasad, B.V. Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus. Proc. Natl. Acad. Sci. U. S. A. 2008, 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
  • 27
  • 28
    • 40849140609 scopus 로고    scopus 로고
    • An efficient plant viral expression system generating orally immunogenic Norwalk virus-like particles
    • Santi, L.; Batchelor, L.; Huang, Z.; Hjelm, B.; Kilbourne, J.; Arntzen, C.J.; Chen, Q.; Mason, H.S. An efficient plant viral expression system generating orally immunogenic Norwalk virus-like particles. Vaccine 2008, 26, 1846-1854.
    • (2008) Vaccine , vol.26 , pp. 1846-1854
    • Santi, L.1    Batchelor, L.2    Huang, Z.3    Hjelm, B.4    Kilbourne, J.5    Arntzen, C.J.6    Chen, Q.7    Mason, H.S.8
  • 29
    • 0027240069 scopus 로고
    • Comparison of the reactivities of baculovirus-expressed recombinant Norwalk virus capsid antigen with those of the native Norwalk virus antigen in serologic assays and some epidemiologic observations
    • Green, K.Y.; Lew, J.F.; Jiang, X.; Kapikian, A.Z.; Estes, M.K. Comparison of the reactivities of baculovirus-expressed recombinant Norwalk virus capsid antigen with those of the native Norwalk virus antigen in serologic assays and some epidemiologic observations. J. Clin. Microbiol. 1993, 31, 2185-2191.
    • (1993) J. Clin. Microbiol , vol.31 , pp. 2185-2191
    • Green, K.Y.1    Lew, J.F.2    Jiang, X.3    Kapikian, A.Z.4    Estes, M.K.5
  • 30
    • 20544440607 scopus 로고    scopus 로고
    • Generation of recombinant norovirus-like particles (VLP) in the human endothelial kidney cell line 293T
    • Taube, S.; Kurth, A.; Schreier, E. Generation of recombinant norovirus-like particles (VLP) in the human endothelial kidney cell line 293T. Arch. Virol. 2005, 150, 1425-1431.
    • (2005) Arch. Virol , vol.150 , pp. 1425-1431
    • Taube, S.1    Kurth, A.2    Schreier, E.3
  • 31
    • 0026649563 scopus 로고
    • Expression, self-assembly, and antigenicity of the Norwalk virus capsid protein
    • Jiang, X.; Wang, M.; Graham, D.Y.; Estes, M.K. Expression, self-assembly, and antigenicity of the Norwalk virus capsid protein. J. Virol. 1992, 66, 6527-6532.
    • (1992) J. Virol , vol.66 , pp. 6527-6532
    • Jiang, X.1    Wang, M.2    Graham, D.Y.3    Estes, M.K.4
  • 32
    • 0036139183 scopus 로고    scopus 로고
    • Systemic, mucosal, and heterotypic immune induction in mice inoculated with Venezuelan equine encephalitis replicons expressing Norwalk virus-like particles
    • Harrington, P.R.; Yount, B.; Johnston, R.E.; Davis, N.; Moe, C.; Baric, R.S. Systemic, mucosal, and heterotypic immune induction in mice inoculated with Venezuelan equine encephalitis replicons expressing Norwalk virus-like particles. J. Virol. 2002, 76, 730-742.
    • (2002) J. Virol , vol.76 , pp. 730-742
    • Harrington, P.R.1    Yount, B.2    Johnston, R.E.3    Davis, N.4    Moe, C.5    Baric, R.S.6
  • 33
    • 33745085830 scopus 로고    scopus 로고
    • Tomato is a highly effective vehicle for expression and oral immunization with Norwalk virus capsid protein
    • Zhang, X.; Buehner, N.A.; Hutson, A.M.; Estes, M.K.; Mason, H.S. Tomato is a highly effective vehicle for expression and oral immunization with Norwalk virus capsid protein. Plant Biotechnol. J. 2006, 4, 419-432.
    • (2006) Plant Biotechnol. J , vol.4 , pp. 419-432
    • Zhang, X.1    Buehner, N.A.2    Hutson, A.M.3    Estes, M.K.4    Mason, H.S.5
  • 35
    • 0026066278 scopus 로고
    • Serial propagation of porcine enteric calicivirus in a continuous cell line. Effect of medium supplementation with intestinal contents or enzymes
    • Parwani, A.V.; Flynn, W.T.; Gadfield, K.L.; Saif, L.J. Serial propagation of porcine enteric calicivirus in a continuous cell line. Effect of medium supplementation with intestinal contents or enzymes. Arch. Virol. 1991, 120, 115-122.
    • (1991) Arch. Virol , vol.120 , pp. 115-122
    • Parwani, A.V.1    Flynn, W.T.2    Gadfield, K.L.3    Saif, L.J.4
  • 36
    • 0037290948 scopus 로고    scopus 로고
    • A feline kidney cell line-based plaque assay for feline calicivirus, a surrogate for Norwalk virus
    • Bidawid, S.; Malik, N.; Adegbunrin, O.; Sattar, S.A.; Farber, J.M. A feline kidney cell line-based plaque assay for feline calicivirus, a surrogate for Norwalk virus. J. Virol. Methods 2003, 107, 163-167.
    • (2003) J. Virol. Methods , vol.107 , pp. 163-167
    • Bidawid, S.1    Malik, N.2    Adegbunrin, O.3    Sattar, S.A.4    Farber, J.M.5
  • 37
    • 33846169715 scopus 로고    scopus 로고
    • Alpha2,6-linked sialic acid acts as a receptor for Feline calicivirus
    • Stuart, A.D.; Brown, T.D. Alpha2,6-linked sialic acid acts as a receptor for Feline calicivirus. J. Gen. Virol. 2007, 88, 177-186.
    • (2007) J. Gen. Virol , vol.88 , pp. 177-186
    • Stuart, A.D.1    Brown, T.D.2
  • 38
    • 37049005596 scopus 로고    scopus 로고
    • Identification of regions and residues in feline junctional adhesion molecule required for feline calicivirus binding and infection
    • Ossiboff, R.J.; Parker, J.S. Identification of regions and residues in feline junctional adhesion molecule required for feline calicivirus binding and infection. J. Virol. 2007, 81, 13608-13621.
    • (2007) J. Virol , vol.81 , pp. 13608-13621
    • Ossiboff, R.J.1    Parker, J.S.2
  • 39
    • 33646184221 scopus 로고    scopus 로고
    • Junctional adhesion molecule 1 is a functional receptor for feline calicivirus
    • Makino, A.; Shimojima, M.; Miyazawa, T.; Kato, K.; Tohya, Y.; Akashi, H. Junctional adhesion molecule 1 is a functional receptor for feline calicivirus. J. Virol. 2006, 80, 4482-4490.
    • (2006) J. Virol , vol.80 , pp. 4482-4490
    • Makino, A.1    Shimojima, M.2    Miyazawa, T.3    Kato, K.4    Tohya, Y.5    Akashi, H.6
  • 40
    • 33746214697 scopus 로고    scopus 로고
    • Entry of feline calicivirus is dependent on clathrin-mediated endocytosis and acidification in endosomes
    • Stuart, A.D.; Brown, T.D. Entry of feline calicivirus is dependent on clathrin-mediated endocytosis and acidification in endosomes. J. Virol. 2006, 80, 7500-7509.
    • (2006) J. Virol , vol.80 , pp. 7500-7509
    • Stuart, A.D.1    Brown, T.D.2
  • 41
    • 77952676295 scopus 로고    scopus 로고
    • Murine norovirus-1 cell entry is mediated through a non-clathrin, non-caveolae, dynamin and cholesterol dependent pathway
    • Gerondopoulos, A.; Jackson, T.; Monaghan, P.; Doyle, N.; Roberts, L.O. Murine norovirus-1 cell entry is mediated through a non-clathrin, non-caveolae, dynamin and cholesterol dependent pathway. J. Gen. Virol. 2010, [Epub ahead of print].
    • (2010) J. Gen. Virol
    • Gerondopoulos, A.1    Jackson, T.2    Monaghan, P.3    Doyle, N.4    Roberts, L.O.5
  • 42
    • 67349267018 scopus 로고    scopus 로고
    • Murine norovirus-1 entry into permissive macrophages and dendritic cells is pH-independent
    • Perry, J.W.; Taube, S.; Wobus, C.E. Murine norovirus-1 entry into permissive macrophages and dendritic cells is pH-independent. Virus Res. 2009, 143, 125-129.
    • (2009) Virus Res , vol.143 , pp. 125-129
    • Perry, J.W.1    Taube, S.2    Wobus, C.E.3
  • 43
    • 77952693635 scopus 로고    scopus 로고
    • Endocytosis of Murine Norovirus 1 into Murine Macrophages is dependent on dynamin II and cholesterol
    • Perry, J.; Wobus, C.E. Endocytosis of Murine Norovirus 1 into Murine Macrophages is dependent on dynamin II and cholesterol. J. Virol. 2010, 84, in press.
    • (2010) J. Virol , vol.84
    • Perry, J.1    Wobus, C.E.2
  • 46
    • 0347481458 scopus 로고    scopus 로고
    • Foodborne viruses: An emerging problem
    • Koopmans, M.; Duizer, E. Foodborne viruses: an emerging problem. Int. J. Food Microbiol. 2004, 90, 23-41.
    • (2004) Int. J. Food Microbiol , vol.90 , pp. 23-41
    • Koopmans, M.1    Duizer, E.2
  • 47
    • 36248978196 scopus 로고    scopus 로고
    • New trends in emerging pathogens
    • Skovgaard, N. New trends in emerging pathogens. Int. J. Food Microbiol. 2007, 120, 217-224.
    • (2007) Int. J. Food Microbiol , vol.120 , pp. 217-224
    • Skovgaard, N.1
  • 48
    • 0037423838 scopus 로고    scopus 로고
    • H.W. STAT1-dependent innate immunity to a Norwalk-like virus
    • Karst, S.M.; Wobus, C.E.; Lay, M.; Davidson, J.; Virgin IV, H.W. STAT1-dependent innate immunity to a Norwalk-like virus. Science 2003, 299, 1575-1578.
    • (2003) Science , vol.299 , pp. 1575-1578
    • Karst, S.M.1    Wobus, C.E.2    Lay, M.3    Davidson, J.4    Virgin, I.V.5
  • 51
    • 1442324393 scopus 로고    scopus 로고
    • Molecular characterization of noroviruses detected in diarrheic stools of Michigan and Wisconsin dairy calves: Circulation of two distinct subgroups
    • Wise, A.G.; Monroe, S.S.; Hanson, L.E.; Grooms, D.L.; Sockett, D.; Maes, R.K. Molecular characterization of noroviruses detected in diarrheic stools of Michigan and Wisconsin dairy calves: circulation of two distinct subgroups. Virus Res. 2004, 100, 165-177.
    • (2004) Virus Res , vol.100 , pp. 165-177
    • Wise, A.G.1    Monroe, S.S.2    Hanson, L.E.3    Grooms, D.L.4    Sockett, D.5    Maes, R.K.6
  • 62
    • 34547459640 scopus 로고    scopus 로고
    • Norovirus-host interaction: Implications for disease control and prevention
    • Tan, M.; Jiang, X. Norovirus-host interaction: implications for disease control and prevention. Exp. Rev. Mol. Med. 2007, 9, 1-22.
    • (2007) Exp. Rev. Mol. Med , vol.9 , pp. 1-22
    • Tan, M.1    Jiang, X.2
  • 63
    • 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. Genogroup II noroviruses efficiently bind to heparan sulfate proteoglycan associated with the cellular membrane. J. Virol. 2004, 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
  • 65
    • 0024537246 scopus 로고
    • ABH and related histo-blood group antigens; immunochemical differences in carrier isotypes and their distribution
    • Clausen, H.; Hakomori, S. ABH and related histo-blood group antigens; immunochemical differences in carrier isotypes and their distribution. Vox Sang. 1989, 56, 1-20.
    • (1989) Vox Sang , vol.56 , pp. 1-20
    • Clausen, H.1    Hakomori, S.2
  • 66
    • 0028556293 scopus 로고
    • Immunochemical and immunohistological expression of Lewis histo-blood group antigens in small intestine including individuals of the Le(a+b+) and Le(a-b-) nonsecretor phenotypes
    • Henry, S.M.; Samuelsson, B.E.; Oriol, R. Immunochemical and immunohistological expression of Lewis histo-blood group antigens in small intestine including individuals of the Le(a+b+) and Le(a-b-) nonsecretor phenotypes. Glycoconj. J. 1994, 11, 600-607.
    • (1994) Glycoconj. J , vol.11 , pp. 600-607
    • Henry, S.M.1    Samuelsson, B.E.2    Oriol, R.3
  • 67
    • 0034838386 scopus 로고    scopus 로고
    • ABH and Lewis histo-blood group antigens, a model for the meaning of oligosaccharide diversity in the face of a changing world
    • Marionneau, S.; Cailleau-Thomas, A.; Rocher, J.; Le Moullac-Vaidye, B.; Ruvoen, N.; Clement, M.; Le Pendu, J. ABH and Lewis histo-blood group antigens, a model for the meaning of oligosaccharide diversity in the face of a changing world. Biochimie 2001, 83, 565-573.
    • (2001) Biochimie , vol.83 , pp. 565-573
    • Marionneau, S.1    Cailleau-Thomas, A.2    Rocher, J.3    Le Moullac-Vaidye, B.4    Ruvoen, N.5    Clement, M.6    Le Pendu, J.7
  • 68
    • 4644316068 scopus 로고    scopus 로고
    • Histo-blood group antigen and human milk oligosaccharides: Genetic polymorphism and risk of infectious diseases
    • Le Pendu, J. Histo-blood group antigen and human milk oligosaccharides: genetic polymorphism and risk of infectious diseases. Adv. Exp. Med. Biol. 2004, 554, 135-143.
    • (2004) Adv. Exp. Med. Biol , vol.554 , pp. 135-143
    • Le Pendu, J.1
  • 69
    • 0032760682 scopus 로고    scopus 로고
    • Antigen structure and genetic basis of histo-blood groups A, B and O: Their changes associated with human cancer
    • Hakomori, S. Antigen structure and genetic basis of histo-blood groups A, B and O: their changes associated with human cancer. Biochim. Biophys. Acta 1999, 1473, 247-266.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 247-266
    • Hakomori, S.1
  • 71
    • 70049115904 scopus 로고    scopus 로고
    • The alphaGal epitope of the histo-blood group antigen family is a ligand for bovine norovirus Newbury2 expected to prevent cross-species transmission
    • Zakhour, M.; Ruvoen-Clouet, N.; Charpilienne, A.; Langpap, B.; Poncet, D.; Peters, T.; Bovin, N.; Le Pendu, J. The alphaGal epitope of the histo-blood group antigen family is a ligand for bovine norovirus Newbury2 expected to prevent cross-species transmission. PLoS Path. 2009, 5, e1000504.
    • (2009) PLoS Path , vol.5
    • Zakhour, M.1    Ruvoen-Clouet, N.2    Charpilienne, A.3    Langpap, B.4    Poncet, D.5    Peters, T.6    Bovin, N.7    Le Pendu, J.8
  • 72
    • 0034466823 scopus 로고    scopus 로고
    • Binding of rabbit hemorrhagic disease virus to antigens of the ABH histo-blood group family
    • Ruvoen-Clouet, N.; Ganiere, J.P.; Andre-Fontaine, G.; Blanchard, D.; Le Pendu, J. Binding of rabbit hemorrhagic disease virus to antigens of the ABH histo-blood group family. J. Virol. 2000, 74, 11950-11954.
    • (2000) J. Virol , vol.74 , pp. 11950-11954
    • Ruvoen-Clouet, N.1    Ganiere, J.P.2    Andre-Fontaine, G.3    Blanchard, D.4    Le Pendu, J.5
  • 74
    • 0027976783 scopus 로고
    • Assay for evaluation of rotavirus-cell interactions: Identification of an enterocyte ganglioside fraction that mediates group A porcine rotavirus recognition
    • Rolsma, M.D.; Gelberg, H.B.; Kuhlenschmidt, M.S. Assay for evaluation of rotavirus-cell interactions: identification of an enterocyte ganglioside fraction that mediates group A porcine rotavirus recognition. J. Virol. 1994, 68, 258-268.
    • (1994) J. Virol , vol.68 , pp. 258-268
    • Rolsma, M.D.1    Gelberg, H.B.2    Kuhlenschmidt, M.S.3
  • 75
    • 0031657985 scopus 로고    scopus 로고
    • Structure and function of a ganglioside receptor for porcine rotavirus
    • Rolsma, M.D.; Kuhlenschmidt, T.B.; Gelberg, H.B.; Kuhlenschmidt, M.S. Structure and function of a ganglioside receptor for porcine rotavirus. J. Virol. 1998, 72, 9079-9091.
    • (1998) J. Virol , vol.72 , pp. 9079-9091
    • Rolsma, M.D.1    Kuhlenschmidt, T.B.2    Gelberg, H.B.3    Kuhlenschmidt, M.S.4
  • 77
    • 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, K.A.; Neeser, J.R.; Teneberg, S. 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    Roche, N.4    Karlsson, K.A.5    Neeser, J.R.6    Teneberg, S.7
  • 78
    • 0036785609 scopus 로고    scopus 로고
    • Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core
    • Dormitzer, P.R.; Sun, Z.Y.; Blixt, O.; Paulson, J.C.; Wagner, G.; Harrison, S.C. Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core. J. Virol. 2002, 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
  • 81
    • 0030584127 scopus 로고    scopus 로고
    • Crystal structures of murine polyomavirus in complex with straight-chain and branched-chain sialyloligosaccharide receptor fragments
    • Stehle, T.; Harrison, S.C. Crystal structures of murine polyomavirus in complex with straight-chain and branched-chain sialyloligosaccharide receptor fragments. Structure 1996, 4, 183-194.
    • (1996) Structure , vol.4 , pp. 183-194
    • Stehle, T.1    Harrison, S.C.2
  • 82
    • 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, M.I. Alpha4beta1 integrin acts as a cell receptor for murine polyomavirus at the postattachment level. J. Virol. 2003, 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
  • 83
    • 33847033430 scopus 로고    scopus 로고
    • Mutation in the VP1-LDV motif of the murine polyomavirus affects viral infectivity and conditions virus tissue tropism in vivo
    • Caruso, M.; Busanello, A.; Sthandier, O.; Cavaldesi, M.; Gentile, M.; Garcia, M.I.; Amati, P. Mutation in the VP1-LDV motif of the murine polyomavirus affects viral infectivity and conditions virus tissue tropism in vivo. J. Mol. Biol. 2007, 367, 54-64.
    • (2007) J. Mol. Biol , vol.367 , pp. 54-64
    • Caruso, M.1    Busanello, A.2    Sthandier, O.3    Cavaldesi, M.4    Gentile, M.5    Garcia, M.I.6    Amati, P.7
  • 84
    • 0026578801 scopus 로고
    • Class I major histocompatibility proteins are an essential component of the simian virus 40 receptor
    • Breau, W.C.; Atwood, W.J.; Norkin, L.C. Class I major histocompatibility proteins are an essential component of the simian virus 40 receptor. J. Virol. 1992, 66, 2037-2045.
    • (1992) J. Virol , vol.66 , pp. 2037-2045
    • Breau, W.C.1    Atwood, W.J.2    Norkin, L.C.3
  • 85
    • 0024434514 scopus 로고
    • Class I major histocompatibility proteins as cell surface receptors for simian virus 40
    • Atwood, W.J.; Norkin, L.C. Class I major histocompatibility proteins as cell surface receptors for simian virus 40. J. Virol. 1989, 63, 4474-4477.
    • (1989) J. Virol , vol.63 , pp. 4474-4477
    • Atwood, W.J.1    Norkin, L.C.2
  • 86
    • 31144470194 scopus 로고    scopus 로고
    • Identification of gangliosides GD1b and GT1b as receptors for BK virus
    • Low, J.A.; Magnuson, B.; Tsai, B.; Imperiale, M.J. Identification of gangliosides GD1b and GT1b as receptors for BK virus. J. Virol. 2006, 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
  • 87
    • 27644460490 scopus 로고    scopus 로고
    • An N-linked glycoprotein with alpha(2,3)-linked sialic acid is a receptor for BK virus
    • Dugan, A.S.; Eash, S.; Atwood, W.J. An N-linked glycoprotein with alpha(2,3)-linked sialic acid is a receptor for BK virus. J. Virol. 2005, 79, 14442-14445.
    • (2005) J. Virol , vol.79 , pp. 14442-14445
    • Dugan, A.S.1    Eash, S.2    Atwood, W.J.3
  • 90
    • 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, A.S.; Gasparovic, M.L.; Atwood, W.J. Direct correlation between sialic acid binding and infection of cells by two human polyomaviruses (JC virus and BK virus). J. Virol. 2008, 82, 2560-2564.
    • (2008) J. Virol , vol.82 , pp. 2560-2564
    • Dugan, A.S.1    Gasparovic, M.L.2    Atwood, W.J.3
  • 91
    • 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, C.K.; Wei, G.; Atwood, W.J. 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. 1998, 72, 4643-4649.
    • (1998) J. Virol , vol.72 , pp. 4643-4649
    • Liu, C.K.1    Wei, G.2    Atwood, W.J.3
  • 92
    • 70349276758 scopus 로고    scopus 로고
    • Ganglioside GT1b is a putative host cell receptor for the Merkel cell polyomavirus
    • Erickson, K.D.; Garcea, R.L.; Tsai, B. Ganglioside GT1b is a putative host cell receptor for the Merkel cell polyomavirus. J. Virol. 2009, 83, 10275-10279.
    • (2009) J. Virol , vol.83 , pp. 10275-10279
    • Erickson, K.D.1    Garcea, R.L.2    Tsai, B.3
  • 93
    • 0027686846 scopus 로고
    • Erythrocyte P antigen: Cellular receptor for B19 parvovirus
    • Brown, K.E.; Anderson, S.M.; Young, N.S. Erythrocyte P antigen: cellular receptor for B19 parvovirus. Science 1993, 262, 114-117.
    • (1993) Science , vol.262 , pp. 114-117
    • Brown, K.E.1    Anderson, S.M.2    Young, N.S.3
  • 94
    • 0028871359 scopus 로고
    • Multiple glycosphingolipids determine the tissue tropism of parvovirus B19
    • Cooling, L.L.; Koerner, T.A.; Naides, S.J. Multiple glycosphingolipids determine the tissue tropism of parvovirus B19. J. Infect. Dis. 1995, 172, 1198-1205.
    • (1995) J. Infect. Dis , vol.172 , pp. 1198-1205
    • Cooling, L.L.1    Koerner, T.A.2    Naides, S.J.3
  • 95
    • 0345257726 scopus 로고    scopus 로고
    • Alpha5beta1 integrin as a cellular coreceptor for human parvovirus B19: Requirement of functional activation of beta1 integrin for viral entry
    • Weigel-Kelley, K.A.; Yoder, M.C.; Srivastava, A. Alpha5beta1 integrin as a cellular coreceptor for human parvovirus B19: requirement of functional activation of beta1 integrin for viral entry. Blood 2003, 102, 3927-3933.
    • (2003) Blood , vol.102 , pp. 3927-3933
    • Weigel-Kelley, K.A.1    Yoder, M.C.2    Srivastava, A.3
  • 98
    • 33646723883 scopus 로고    scopus 로고
    • Gangliosides are essential for bovine adeno-associated virus entry
    • Schmidt, M.; Chiorini, J.A. Gangliosides are essential for bovine adeno-associated virus entry. J. Virol. 2006, 80, 5516-5522.
    • (2006) J. Virol , vol.80 , pp. 5516-5522
    • Schmidt, M.1    Chiorini, J.A.2
  • 99
    • 40849119996 scopus 로고    scopus 로고
    • Structure and function of glycosphingolipids and sphingolipids: Recollections and future trends
    • Hakomori, S.I. Structure and function of glycosphingolipids and sphingolipids: recollections and future trends. Biochim. Biophys. Acta 2008, 1780, 325-346.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 325-346
    • Hakomori, S.I.1
  • 100
    • 0033980199 scopus 로고    scopus 로고
    • Tissue distribution of histo-blood group antigens
    • Ravn, V.; Dabelsteen, E. Tissue distribution of histo-blood group antigens. APMIS 2000, 108, 1-28.
    • (2000) APMIS , vol.108 , pp. 1-28
    • Ravn, V.1    Dabelsteen, E.2
  • 102
    • 0036889419 scopus 로고    scopus 로고
    • Binding of Norwalk viruslike particles to ABH histo-blood group antigens is blocked by antisera from infected human volunteers or experimentally vaccinated mice
    • Harrington, P.R.; Lindesmith, L.; Yount, B.; Moe, C.L.; Baric, R.S. Binding of Norwalk viruslike particles to ABH histo-blood group antigens is blocked by antisera from infected human volunteers or experimentally vaccinated mice. J. Virol. 2002, 76, 12335-12343.
    • (2002) J. Virol , vol.76 , pp. 12335-12343
    • Harrington, P.R.1    Lindesmith, L.2    Yount, B.3    Moe, C.L.4    Baric, R.S.5
  • 103
    • 1542377534 scopus 로고    scopus 로고
    • Norovirus capture with histo-blood group antigens reveals novel virus-ligand interactions
    • Harrington, P.R.; Vinje, J.; Moe, C.L.; Baric, R.S. Norovirus capture with histo-blood group antigens reveals novel virus-ligand interactions. J. Virol. 2004, 78, 3035-3045.
    • (2004) J. Virol , vol.78 , pp. 3035-3045
    • Harrington, P.R.1    Vinje, J.2    Moe, C.L.3    Baric, R.S.4
  • 104
    • 0037213273 scopus 로고    scopus 로고
    • Norwalk virus-like particle hemagglutination by binding to h histo-blood group antigens
    • Hutson, A.M.; Atmar, R.L.; Marcus, D.M.; Estes, M.K. Norwalk virus-like particle hemagglutination by binding to h histo-blood group antigens. J. Virol. 2003, 77, 405-415.
    • (2003) J. Virol , vol.77 , pp. 405-415
    • Hutson, A.M.1    Atmar, R.L.2    Marcus, D.M.3    Estes, M.K.4
  • 108
    • 0036569142 scopus 로고    scopus 로고
    • Norwalk virus infection and disease is associated with ABO histo-blood group type
    • Hutson, A.M.; Atmar, R.L.; Graham, D.Y.; Estes, M.K. Norwalk virus infection and disease is associated with ABO histo-blood group type. J. Infect. Dis. 2002, 185, 1335-1337.
    • (2002) J. Infect. Dis , vol.185 , pp. 1335-1337
    • Hutson, A.M.1    Atmar, R.L.2    Graham, D.Y.3    Estes, M.K.4
  • 109
    • 77649262827 scopus 로고    scopus 로고
    • Norwalk virus-like particles bind specifically to A, H and difucosylated Lewis but not to B histo-blood group active glycosphingolipids
    • Nilsson, J.; Rydell, G.E.; Le Pendu, J.; Larson, G. Norwalk virus-like particles bind specifically to A, H and difucosylated Lewis but not to B histo-blood group active glycosphingolipids. Glycoconj. J. 2009.
    • (2009) Glycoconj. J
    • Nilsson, J.1    Rydell, G.E.2    Le Pendu, J.3    Larson, G.4
  • 110
    • 70349991887 scopus 로고    scopus 로고
    • QCM-D studies of human norovirus VLPs binding to glycosphingolipids in supported lipid bilayers reveal strain-specific characteristics
    • Rydell, G.E.; Dahlin, A.B.; Hook, F.; Larson, G. QCM-D studies of human norovirus VLPs binding to glycosphingolipids in supported lipid bilayers reveal strain-specific characteristics. Glycobiology 2009, 19, 1176-1184.
    • (2009) Glycobiology , vol.19 , pp. 1176-1184
    • Rydell, G.E.1    Dahlin, A.B.2    Hook, F.3    Larson, G.4
  • 112
    • 13944275858 scopus 로고    scopus 로고
    • Association of histo-blood group antigens and susceptibility to norovirus infections
    • Rockx, B.H.; Vennema, H.; Hoebe, C.J.; Duizer, E.; Koopmans, M.P. Association of histo-blood group antigens and susceptibility to norovirus infections. J. Infect. Dis. 2005, 191, 749-754.
    • (2005) J. Infect. Dis , vol.191 , pp. 749-754
    • Rockx, B.H.1    Vennema, H.2    Hoebe, C.J.3    Duizer, E.4    Koopmans, M.P.5
  • 113
    • 0038235584 scopus 로고    scopus 로고
    • Norwalk virus infection and disease is associated with ABO histo-blood group type
    • Hennessy, E.P.; Green, A.D.; Connor, M.P.; Darby, R.; MacDonald, P. Norwalk virus infection and disease is associated with ABO histo-blood group type. J. Infect. Dis. 2003, 188, 176-177.
    • (2003) J. Infect. Dis , vol.188 , pp. 176-177
    • Hennessy, E.P.1    Green, A.D.2    Connor, M.P.3    Darby, R.4    Macdonald, P.5
  • 114
    • 24644483568 scopus 로고    scopus 로고
    • Influence of the combined ABO, FUT2, and FUT3 polymorphism on susceptibility to Norwalk virus attachment
    • Marionneau, S.; Airaud, F.; Bovin, N.V.; Le Pendu, J.; Ruvoen-Clouet, N. Influence of the combined ABO, FUT2, and FUT3 polymorphism on susceptibility to Norwalk virus attachment. J. Infect. Dis. 2005, 192, 1071-1077.
    • (2005) J. Infect. Dis , vol.192 , pp. 1071-1077
    • Marionneau, S.1    Airaud, F.2    Bovin, N.V.3    Le Pendu, J.4    Ruvoen-Clouet, N.5
  • 115
    • 33750695005 scopus 로고    scopus 로고
    • Antibody prevalence and titer to norovirus (genogroup II) correlate with secretor (FUT2) but not with ABO phenotype or Lewis (FUT3) genotype
    • Larsson, M.M.; Rydell, G.E.; Grahn, A.; Rodriguez-Diaz, J.; Akerlind, B.; Hutson, A.M.; Estes, M.K.; Larson, G.; Svensson, L. Antibody prevalence and titer to norovirus (genogroup II) correlate with secretor (FUT2) but not with ABO phenotype or Lewis (FUT3) genotype. J. Infect. Dis. 2006, 194, 1422-1427.
    • (2006) J. Infect. Dis , vol.194 , pp. 1422-1427
    • Larsson, M.M.1    Rydell, G.E.2    Grahn, A.3    Rodriguez-Diaz, J.4    Akerlind, B.5    Hutson, A.M.6    Estes, M.K.7    Larson, G.8    Svensson, L.9
  • 118
    • 52049112292 scopus 로고    scopus 로고
    • Norovirus pathogenesis: Mechanisms of persistence and immune evasion in human populations
    • Donaldson, E.F.; Lindesmith, L.C.; Lobue, A.D.; Baric, R.S. Norovirus pathogenesis: mechanisms of persistence and immune evasion in human populations. Immunol. Rev. 2008, 225, 190-211.
    • (2008) Immunol. Rev , vol.225 , pp. 190-211
    • Donaldson, E.F.1    Lindesmith, L.C.2    Lobue, A.D.3    Baric, R.S.4
  • 119
    • 26944492149 scopus 로고    scopus 로고
    • Development of a microsphere-based serologic multiplexed fluorescent immunoassay and a reverse transcriptase PCR assay to detect murine norovirus 1 infection in mice
    • Hsu, C.C.; Wobus, C.E.; Steffen, E.K.; Riley, L.K.; Livingston, R.S. Development of a microsphere-based serologic multiplexed fluorescent immunoassay and a reverse transcriptase PCR assay to detect murine norovirus 1 infection in mice. Clin. Diagn. Lab. Immunol. 2005, 12, 1145-1151.
    • (2005) Clin. Diagn. Lab. Immunol , vol.12 , pp. 1145-1151
    • Hsu, C.C.1    Wobus, C.E.2    Steffen, E.K.3    Riley, L.K.4    Livingston, R.S.5
  • 120
    • 34548278958 scopus 로고    scopus 로고
    • Genetic diversity and recombination of murine noroviruses in immunocompromised mice
    • Muller, B.; Klemm, U.; Mas Marques, A.; Schreier, E. Genetic diversity and recombination of murine noroviruses in immunocompromised mice. Arch. Virol. 2007, 152, 1709-1719.
    • (2007) Arch. Virol , vol.152 , pp. 1709-1719
    • Muller, B.1    Klemm, U.2    Mas Marques, A.3    Schreier, E.4
  • 121
    • 45749130161 scopus 로고    scopus 로고
    • Murine norovirus, a recently discovered and highly prevalent viral agent of mice
    • Henderson, K.S. Murine norovirus, a recently discovered and highly prevalent viral agent of mice. Lab Anim (NY) 2008, 37, 314-320.
    • (2008) Lab Anim (NY) , vol.37 , pp. 314-320
    • Henderson, K.S.1
  • 122
    • 65349118782 scopus 로고    scopus 로고
    • A serological survey to evaluate contemporary prevalence of viral agents and Mycoplasma pulmonis in laboratory mice and rats in western Europe
    • Mahler, M.; Kohl, W. A serological survey to evaluate contemporary prevalence of viral agents and Mycoplasma pulmonis in laboratory mice and rats in western Europe. Lab Anim (NY) 2009, 38, 161-165.
    • (2009) Lab Anim (NY) , vol.38 , pp. 161-165
    • Mahler, M.1    Kohl, W.2
  • 123
    • 75749094015 scopus 로고    scopus 로고
    • Development of a broadly reactive nested reverse transcription-PCR assay to detect murine noroviruses, and investigation of the prevalence of murine noroviruses in laboratory mice in Japan
    • Kitajima, M.; Oka, T.; Tohya, Y.; Katayama, H.; Takeda, N.; Katayama, K. Development of a broadly reactive nested reverse transcription-PCR assay to detect murine noroviruses, and investigation of the prevalence of murine noroviruses in laboratory mice in Japan. Microbiol. Immunol. 2009, 53, 531-534.
    • (2009) Microbiol. Immunol , vol.53 , pp. 531-534
    • Kitajima, M.1    Oka, T.2    Tohya, Y.3    Katayama, H.4    Takeda, N.5    Katayama, K.6
  • 124
    • 71149101383 scopus 로고    scopus 로고
    • Molecular characterization of murine norovirus isolates from South Korea
    • Kim, M.; Lee, H.; Chang, K.O.; Ko, G. Molecular characterization of murine norovirus isolates from South Korea. Virus Res. 2010, 147, 1-6.
    • (2010) Virus Res , vol.147 , pp. 1-6
    • Kim, M.1    Lee, H.2    Chang, K.O.3    Ko, G.4
  • 125
    • 33646718792 scopus 로고    scopus 로고
    • Murine norovirus: A model system to study norovirus biology and pathogenesis
    • Wobus, C.E.; Thackray, L.B.; Virgin, H.W. Murine norovirus: a model system to study norovirus biology and pathogenesis. J. Virol. 2006, 80, 5104-5112.
    • (2006) J. Virol , vol.80 , pp. 5104-5112
    • Wobus, C.E.1    Thackray, L.B.2    Virgin IV., H.W.3
  • 126
    • 0018038918 scopus 로고
    • Isolation of small viruses resembling astroviruses and caliciviruses from acute enteritis of calves
    • Woode, G.N.; Bridger, J.C. Isolation of small viruses resembling astroviruses and caliciviruses from acute enteritis of calves. J. Med. Microbiol. 1978, 11, 441-452.
    • (1978) J. Med. Microbiol , vol.11 , pp. 441-452
    • Woode, G.N.1    Bridger, J.C.2
  • 127
    • 57749117400 scopus 로고    scopus 로고
    • Association between expression of the H histo-blood group antigen, alpha1,2fucosyltransferases polymorphism of wild rabbits, and sensitivity to rabbit hemorrhagic disease virus
    • Guillon, P.; Ruvoen-Clouet, N.; Le Moullac-Vaidye, B.; Marchandeau, S.; Le Pendu, J. Association between expression of the H histo-blood group antigen, alpha1,2fucosyltransferases polymorphism of wild rabbits, and sensitivity to rabbit hemorrhagic disease virus. Glycobiology 2009, 19, 21-28.
    • (2009) Glycobiology , vol.19 , pp. 21-28
    • Guillon, P.1    Ruvoen-Clouet, N.2    Le Moullac-Vaidye, B.3    Marchandeau, S.4    Le Pendu, J.5
  • 129
    • 0027053692 scopus 로고
    • Detection of rabbit haemorrhagic disease virus particles in the rabbit liver tissues
    • Park, J.H.; Ochiai, K.; Itakura, C. Detection of rabbit haemorrhagic disease virus particles in the rabbit liver tissues. J. Comp. Pathol. 1992, 107, 329-340.
    • (1992) J. Comp. Pathol , vol.107 , pp. 329-340
    • Park, J.H.1    Ochiai, K.2    Itakura, C.3
  • 130
    • 0028122560 scopus 로고
    • Recombinant rabbit hemorrhagic disease virus capsid protein expressed in baculovirus self-assembles into viruslike particles and induces protection
    • Laurent, S.; Vautherot, J.F.; Madelaine, M.F.; Le Gall, G.; Rasschaert, D. Recombinant rabbit hemorrhagic disease virus capsid protein expressed in baculovirus self-assembles into viruslike particles and induces protection. J. Virol. 1994, 68, 6794-6798.
    • (1994) J. Virol , vol.68 , pp. 6794-6798
    • Laurent, S.1    Vautherot, J.F.2    Madelaine, M.F.3    Le Gall, G.4    Rasschaert, D.5
  • 131
    • 41449101560 scopus 로고    scopus 로고
    • NMR experiments reveal the molecular basis of receptor recognition by a calicivirus
    • Rademacher, C.; Krishna, N.R.; Palcic, M.; Parra, F.; Peters, T. NMR experiments reveal the molecular basis of receptor recognition by a calicivirus. J. Am. Chem. Soc. 2008, 130, 3669-3675.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 3669-3675
    • Rademacher, C.1    Krishna, N.R.2    Palcic, M.3    Parra, F.4    Peters, T.5
  • 132
    • 0026168489 scopus 로고
    • Hepatitis of viral origin in Leporidae: Introduction and aetiological hypotheses
    • Morisse, J.P.; Le Gall, G.; Boilletot, E. Hepatitis of viral origin in Leporidae: introduction and aetiological hypotheses. Rev. Sci. Tech. 1991, 10, 269-310.
    • (1991) Rev. Sci. Tech , vol.10 , pp. 269-310
    • Morisse, J.P.1    Le Gall, G.2    Boilletot, E.3
  • 133
    • 0026167152 scopus 로고
    • Application of control measures against viral haemorrhagic disease of rabbits in the Czech and Slovak Federal Republic
    • Rodak, L.; Smid, B.; Valicek, L. Application of control measures against viral haemorrhagic disease of rabbits in the Czech and Slovak Federal Republic. Rev. Sci. Tech. 1991, 10, 513-524.
    • (1991) Rev. Sci. Tech , vol.10 , pp. 513-524
    • Rodak, L.1    Smid, B.2    Valicek, L.3
  • 135
    • 34047155105 scopus 로고    scopus 로고
    • How do the rotavirus NSP4 and bacterial enterotoxins lead differently to diarrhea?
    • Lorrot, M.; Vasseur, M. How do the rotavirus NSP4 and bacterial enterotoxins lead differently to diarrhea? Virol. J. 2007, 4, 31.
    • (2007) Virol. J , vol.4 , pp. 31
    • Lorrot, M.1    Vasseur, M.2
  • 136
    • 33645450068 scopus 로고    scopus 로고
    • Role of sialic acids in rotavirus infection
    • Isa, P.; Arias, C.F.; Lopez, S. Role of sialic acids in rotavirus infection. Glycoconj. J. 2006, 23, 27-37.
    • (2006) Glycoconj. J , vol.23 , pp. 27-37
    • Isa, P.1    Arias, C.F.2    Lopez, S.3
  • 137
    • 0036007135 scopus 로고    scopus 로고
    • VLA-2 (alpha2beta1) integrin promotes rotavirus entry into cells but is not necessary for rotavirus attachment
    • Ciarlet, M.; Crawford, S.E.; Cheng, E.; Blutt, S.E.; Rice, D.A.; Bergelson, J.M.; Estes, M.K. VLA-2 (alpha2beta1) integrin promotes rotavirus entry into cells but is not necessary for rotavirus attachment. J. Virol. 2002, 76, 1109-1123.
    • (2002) J. Virol , vol.76 , pp. 1109-1123
    • Ciarlet, M.1    Crawford, S.E.2    Cheng, E.3    Blutt, S.E.4    Rice, D.A.5    Bergelson, J.M.6    Estes, M.K.7
  • 138
    • 75449100099 scopus 로고    scopus 로고
    • A rotavirus spike protein conformational intermediate binds lipid bilayers
    • Trask, S.D.; Kim, I.S.; Harrison, S.C.; Dormitzer, P.R. A rotavirus spike protein conformational intermediate binds lipid bilayers. J. Virol. 2010, 84, 1764-1770.
    • (2010) J. Virol , vol.84 , pp. 1764-1770
    • Trask, S.D.1    Kim, I.S.2    Harrison, S.C.3    Dormitzer, P.R.4
  • 139
    • 0033937215 scopus 로고    scopus 로고
    • Selective membrane permeabilization by the rotavirus VP5* protein is abrogated by mutations in an internal hydrophobic domain
    • Dowling, W.; Denisova, E.; LaMonica, R.; Mackow, E.R. Selective membrane permeabilization by the rotavirus VP5* protein is abrogated by mutations in an internal hydrophobic domain. J. Virol. 2000, 74, 6368-6376.
    • (2000) J. Virol , vol.74 , pp. 6368-6376
    • Dowling, W.1    Denisova, E.2    Lamonica, R.3    Mackow, E.R.4
  • 140
    • 0023973434 scopus 로고
    • Characterization of binding of simian rotavirus SA-11 to cultured epithelial cells
    • Keljo, D.J.; Smith, A.K. Characterization of binding of simian rotavirus SA-11 to cultured epithelial cells. J. Pediatr. Gastroenterol. Nutr. 1988, 7, 249-256.
    • (1988) J. Pediatr. Gastroenterol. Nutr , vol.7 , pp. 249-256
    • Keljo, D.J.1    Smith, A.K.2
  • 141
    • 0018911088 scopus 로고
    • Attachment of SA-11 rotavirus to erythrocyte receptors
    • Bastardo, J.W.; Holmes, I.H. Attachment of SA-11 rotavirus to erythrocyte receptors. Infect. Immun. 1980, 29, 1134-1140.
    • (1980) Infect. Immun , vol.29 , pp. 1134-1140
    • Bastardo, J.W.1    Holmes, I.H.2
  • 142
    • 0017913174 scopus 로고
    • Hemagglutination and hemagglutination-inhibition studies with a strain of Nebraska calf diarrhea virus (bovine rotavirus)
    • Fauvel, M.; Spence, L.; Babiuk, L.A.; Petro, R.; Bloch, S. Hemagglutination and hemagglutination-inhibition studies with a strain of Nebraska calf diarrhea virus (bovine rotavirus). Intervirology 1978, 9, 95-105.
    • (1978) Intervirology , vol.9 , pp. 95-105
    • Fauvel, M.1    Spence, L.2    Babiuk, L.A.3    Petro, R.4    Bloch, S.5
  • 143
    • 0017802802 scopus 로고
    • Comparison of rotavirus strains by hemagglutination inhibition
    • Spence, L.; Fauvel, M.; Petro, R.; Babiuk, L.A. Comparison of rotavirus strains by hemagglutination inhibition. Can. J. Microbiol. 1978, 24, 353-362.
    • (1978) Can. J. Microbiol , vol.24 , pp. 353-362
    • Spence, L.1    Fauvel, M.2    Petro, R.3    Babiuk, L.A.4
  • 145
    • 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 (Pt 4), 943-948.
    • (1999) J. Gen. Virol , vol.80 , Issue.Pt 4 , pp. 943-948
    • Ciarlet, M.1    Estes, M.K.2
  • 146
    • 58249112782 scopus 로고    scopus 로고
    • 'Sialidase sensitivity' of rotaviruses revisited
    • Banda, K.; Kang, G.; Varki, A. 'Sialidase sensitivity' of rotaviruses revisited. Nat. Chem. Biol. 2009, 5, 71-72.
    • (2009) Nat. Chem. Biol , vol.5 , pp. 71-72
    • Banda, K.1    Kang, G.2    Varki, A.3
  • 147
    • 73149088602 scopus 로고    scopus 로고
    • Rotaviruses require basolateral molecules for efficient infection of polarized MDCKII cells
    • Realpe, M.; Espinosa, R.; Lopez, S.; Arias, C.F. Rotaviruses require basolateral molecules for efficient infection of polarized MDCKII cells. Virus Res. 2010, 147, 231-241.
    • (2010) Virus Res , vol.147 , pp. 231-241
    • Realpe, M.1    Espinosa, R.2    Lopez, S.3    Arias, C.F.4
  • 148
    • 33845346428 scopus 로고    scopus 로고
    • Rotavirus: To the gut and beyond!
    • Blutt, S.E.; Conner, M.E. Rotavirus: to the gut and beyond! Curr. Opin. Gastro. 2007, 23, 39-43.
    • (2007) Curr. Opin. Gastro , vol.23 , pp. 39-43
    • Blutt, S.E.1    Conner, M.E.2
  • 152
    • 0026801971 scopus 로고
    • Group C rotavirus requires sialic acid for erythrocyte and cell receptor binding
    • Svensson, L. Group C rotavirus requires sialic acid for erythrocyte and cell receptor binding. J. Virol. 1992, 66, 5582-5585.
    • (1992) J. Virol , vol.66 , pp. 5582-5585
    • Svensson, L.1
  • 154
    • 0025066089 scopus 로고
    • Rotaviruses specifically bind to the neutral glycosphingolipid asialo-GM1
    • Willoughby, R.E.; Yolken, R.H.; Schnaar, R.L. Rotaviruses specifically bind to the neutral glycosphingolipid asialo-GM1. J. Virol. 1990, 64, 4830-4835.
    • (1990) J. Virol , vol.64 , pp. 4830-4835
    • Willoughby, R.E.1    Yolken, R.H.2    Schnaar, R.L.3
  • 155
    • 0026094402 scopus 로고
    • Gangliosides as binding sites in SA-11 rotavirus infection of LLC-MK2 cells
    • Superti, F.; Donelli, G. Gangliosides as binding sites in SA-11 rotavirus infection of LLC-MK2 cells. J. Gen. Virol. 1991, 72 2467-2474.
    • (1991) J. Gen. Virol , vol.72 , pp. 2467-2474
    • Superti, F.1    Donelli, G.2
  • 157
    • 0024426261 scopus 로고
    • Comparison of human, simian, and bovine rotaviruses for requirement of sialic acid in hemagglutination and cell adsorption
    • Fukudome, K.; Yoshie, O.; Konno, T. Comparison of human, simian, and bovine rotaviruses for requirement of sialic acid in hemagglutination and cell adsorption. Virology 1989, 172, 196-205.
    • (1989) Virology , vol.172 , pp. 196-205
    • Fukudome, K.1    Yoshie, O.2    Konno, T.3
  • 158
    • 0029655241 scopus 로고    scopus 로고
    • Genetic mapping indicates that VP4 is the rotavirus cell attachment protein in vitro and in vivo
    • Ludert, J.E.; Feng, N.; Yu, J.H.; Broome, R.L.; Hoshino, Y.; Greenberg, H.B. Genetic mapping indicates that VP4 is the rotavirus cell attachment protein in vitro and in vivo. J. Virol. 1996, 70, 487-493.
    • (1996) J. Virol , vol.70 , pp. 487-493
    • Ludert, J.E.1    Feng, N.2    Yu, J.H.3    Broome, R.L.4    Hoshino, Y.5    Greenberg, H.B.6
  • 159
    • 0035167247 scopus 로고    scopus 로고
    • Differential infection of polarized epithelial cell lines by sialic acid-dependent and sialic acid-independent rotavirus strains
    • Ciarlet, M.; Crawford, S.E.; Estes, M.K. Differential infection of polarized epithelial cell lines by sialic acid-dependent and sialic acid-independent rotavirus strains. J. Virol. 2001, 75, 11834-11850.
    • (2001) J. Virol , vol.75 , pp. 11834-11850
    • Ciarlet, M.1    Crawford, S.E.2    Estes, M.K.3
  • 160
    • 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, M.J.; Bugarcic, A.; Fleming, F.E.; Yu, X.; von Itzstein, M.; Coulson, B.S.; Blanchard, H. Effects on sialic acid recognition of amino acid mutations in the carbohydrate-binding cleft of the rotavirus spike protein. Glycobiology 2009, 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
  • 161
    • 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
  • 162
    • 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
  • 163
    • 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
  • 164
    • 36749064529 scopus 로고    scopus 로고
    • Polyomaviruses
    • Fifth ed.; Knipe, D. M.; Howley, P. M., Eds.; Lippincott Williams & Wilkins: Philadelphia, PA
    • Imperiale, M.J.; Major, E.O. Polyomaviruses. In Fields Virology; Fifth ed.; Knipe, D. M.; Howley, P. M., Eds.; Lippincott Williams & Wilkins: Philadelphia, PA, 2007; Vol. 2, pp. 2263-2298.
    • (2007) Fields Virology , vol.2 , pp. 2263-2298
    • Imperiale, M.J.1    Major, E.O.2
  • 167
    • 0018085602 scopus 로고
    • Higher order structure of simian virus 40 chromatin
    • Muller, U.; Zentgraf, H.; Eicken, I.; Keller, W. Higher order structure of simian virus 40 chromatin. Science 1978, 201, 406-415.
    • (1978) Science , vol.201 , pp. 406-415
    • Muller, U.1    Zentgraf, H.2    Eicken, I.3    Keller, W.4
  • 168
    • 0030584124 scopus 로고    scopus 로고
    • The structure of simian virus 40 refined at 3.1 A resolution
    • Stehle, T.; Gamblin, S.J.; Yan, Y.; Harrison, S.C. The structure of simian virus 40 refined at 3.1 A resolution. Structure 1996, 4, 165-182.
    • (1996) Structure , vol.4 , pp. 165-182
    • Stehle, T.1    Gamblin, S.J.2    Yan, Y.3    Harrison, S.C.4
  • 169
    • 0022549499 scopus 로고
    • Self-assembly of purified polyomavirus capsid protein VP1
    • Salunke, D.M.; Caspar, D.L.; Garcea, R.L. Self-assembly of purified polyomavirus capsid protein VP1. Cell 1986, 46, 895-904.
    • (1986) Cell , vol.46 , pp. 895-904
    • Salunke, D.M.1    Caspar, D.L.2    Garcea, R.L.3
  • 170
    • 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
  • 171
    • 0028303852 scopus 로고
    • Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment
    • Stehle, T.; Yan, Y.; Benjamin, T.L.; Harrison, S.C. Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment. Nature 1994, 369, 160-163.
    • (1994) Nature , vol.369 , pp. 160-163
    • Stehle, T.1    Yan, Y.2    Benjamin, T.L.3    Harrison, S.C.4
  • 172
  • 173
    • 0026024629 scopus 로고
    • Polyomavirus replication in mice: Influences of VP1 type and route of inoculation
    • Dubensky, T.W.; Freund, R.; Dawe, C.J.; Benjamin, T.L. Polyomavirus replication in mice: influences of VP1 type and route of inoculation. J. Virol. 1991, 65, 342-349.
    • (1991) J. Virol , vol.65 , pp. 342-349
    • Dubensky, T.W.1    Freund, R.2    Dawe, C.J.3    Benjamin, T.L.4
  • 175
    • 0036387268 scopus 로고    scopus 로고
    • Construction of a novel JCV/SV40 hybrid virus (JCSV) reveals a role for the JCV capsid in viral tropism
    • Chen, B.J.; Atwood, W.J. Construction of a novel JCV/SV40 hybrid virus (JCSV) reveals a role for the JCV capsid in viral tropism. Virology 2002, 300, 282-290.
    • (2002) Virology , vol.300 , pp. 282-290
    • Chen, B.J.1    Atwood, W.J.2
  • 176
    • 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, W.J. The Polyomaviridae: Contributions of virus structure to our understanding of virus receptors and infectious entry. Virology 2009, 384, 389-399.
    • (2009) Virology , vol.384 , pp. 389-399
    • Neu, U.1    Stehle, T.2    Atwood, W.J.3
  • 177
    • 34547808119 scopus 로고    scopus 로고
    • Caveolar endocytosis is critical for BK virus infection of human renal proximal tubular epithelial cells
    • Moriyama, T.; Marquez, J.P.; Wakatsuki, T.; Sorokin, A. Caveolar endocytosis is critical for BK virus infection of human renal proximal tubular epithelial cells. J. Virol. 2007, 81, 8552-8562.
    • (2007) J. Virol , vol.81 , pp. 8552-8562
    • Moriyama, T.1    Marquez, J.P.2    Wakatsuki, T.3    Sorokin, A.4
  • 178
    • 6344219974 scopus 로고    scopus 로고
    • Infection of vero cells by BK virus is dependent on caveolae
    • Eash, S.; Querbes, W.; Atwood, W.J. Infection of vero cells by BK virus is dependent on caveolae. J. Virol. 2004, 78, 11583-11590.
    • (2004) J. Virol , vol.78 , pp. 11583-11590
    • Eash, S.1    Querbes, W.2    Atwood, W.J.3
  • 179
    • 0033968050 scopus 로고    scopus 로고
    • JC virus enters human glial cells by clathrin-dependent receptor-mediated endocytosis
    • Pho, M.T.; Ashok, A.; Atwood, W.J. JC virus enters human glial cells by clathrin-dependent receptor-mediated endocytosis. J. Virol. 2000, 74, 2288-2292.
    • (2000) J. Virol , vol.74 , pp. 2288-2292
    • Pho, M.T.1    Ashok, A.2    Atwood, W.J.3
  • 180
    • 0036233218 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 is followed by brefeldin A-sensitive transport to the endoplasmic reticulum, where the virus disassembles
    • Norkin, L.C.; Anderson, H.A.; Wolfrom, S.A.; Oppenheim, A. Caveolar endocytosis of simian virus 40 is followed by brefeldin A-sensitive transport to the endoplasmic reticulum, where the virus disassembles. J. Virol. 2002, 76, 5156-5166.
    • (2002) J. Virol , vol.76 , pp. 5156-5166
    • Norkin, L.C.1    Anderson, H.A.2    Wolfrom, S.A.3    Oppenheim, A.4
  • 181
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans, L.; Kartenbeck, J.; Helenius, A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat. Cell Biol. 2001, 3, 473-483.
    • (2001) Nat. Cell Biol , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 182
    • 0034755553 scopus 로고    scopus 로고
    • Caveolae are involved in the trafficking of mouse polyomavirus virions and artificial VP1 pseudocapsids toward cell nuclei
    • Richterova, Z.; Liebl, D.; Horak, M.; Palkova, Z.; Stokrova, J.; Hozak, P.; Korb, J.; Forstova, J. Caveolae are involved in the trafficking of mouse polyomavirus virions and artificial VP1 pseudocapsids toward cell nuclei. J. Virol. 2001, 75, 10880-10891.
    • (2001) J. Virol , vol.75 , pp. 10880-10891
    • Richterova, Z.1    Liebl, D.2    Horak, M.3    Palkova, Z.4    Stokrova, J.5    Hozak, P.6    Korb, J.7    Forstova, J.8
  • 183
    • 26944450514 scopus 로고    scopus 로고
    • ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding
    • Magnuson, B.; Rainey, E.K.; Benjamin, T.; Baryshev, M.; Mkrtchian, S.; Tsai, B. ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding. Mol. Cell 2005, 20, 289-300.
    • (2005) Mol. Cell , vol.20 , pp. 289-300
    • Magnuson, B.1    Rainey, E.K.2    Benjamin, T.3    Baryshev, M.4    Mkrtchian, S.5    Tsai, B.6
  • 184
    • 35548992416 scopus 로고    scopus 로고
    • Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells
    • Schelhaas, M.; Malmstrom, J.; Pelkmans, L.; Haugstetter, J.; Ellgaard, L.; Grunewald, K.; Helenius, A. Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells. Cell 2007, 131, 516-529.
    • (2007) Cell , vol.131 , pp. 516-529
    • Schelhaas, M.1    Malmstrom, J.2    Pelkmans, L.3    Haugstetter, J.4    Ellgaard, L.5    Grunewald, K.6    Helenius, A.7
  • 185
    • 59749086300 scopus 로고    scopus 로고
    • Early events during BK virus entry and disassembly
    • Jiang, M.; Abend, J.R.; Tsai, B.; Imperiale, M.J. Early events during BK virus entry and disassembly. J. Virol. 2009, 83, 1350-1358.
    • (2009) J. Virol , vol.83 , pp. 1350-1358
    • Jiang, M.1    Abend, J.R.2    Tsai, B.3    Imperiale, M.J.4
  • 186
    • 33748658449 scopus 로고    scopus 로고
    • Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection
    • Lilley, B.N.; Gilbert, J.M.; Ploegh, H.L.; Benjamin, T.L. Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection. J. Virol. 2006, 80, 8739-8744.
    • (2006) J. Virol , vol.80 , pp. 8739-8744
    • Lilley, B.N.1    Gilbert, J.M.2    Ploegh, H.L.3    Benjamin, T.L.4
  • 187
    • 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, K.J.; Tsai, B. A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection. PLoS Path. 2009, 5, e1000465.
    • (2009) PLoS Path , vol.5
    • Qian, M.1    Cai, D.2    Verhey, K.J.3    Tsai, B.4
  • 188
    • 0001488319 scopus 로고
    • A filterable agent, recovered from Ak leukemic extracts, causing salivary gland carcinomas in C3H mice
    • Gross, L. A filterable agent, recovered from Ak leukemic extracts, causing salivary gland carcinomas in C3H mice. Proc. Soc. Exp. Biol. Med. 1953, 83, 414-421.
    • (1953) Proc. Soc. Exp. Biol. Med , vol.83 , pp. 414-421
    • Gross, L.1
  • 189
    • 0021086115 scopus 로고
    • Sialyloligosaccharide receptors of binding variants of polyoma virus
    • Cahan, L.D.; Singh, R.; Paulson, J.C. Sialyloligosaccharide receptors of binding variants of polyoma virus. Virology 1983, 130, 281-289.
    • (1983) Virology , vol.130 , pp. 281-289
    • Cahan, L.D.1    Singh, R.2    Paulson, J.C.3
  • 190
    • 0019382866 scopus 로고
    • Polyoma virus recognizes specific sialyligosaccharide receptors on host cells
    • Fried, H.; Cahan, L.D.; Paulson, J.C. Polyoma virus recognizes specific sialyligosaccharide receptors on host cells. Virology 1981, 109, 188-192.
    • (1981) Virology , vol.109 , pp. 188-192
    • Fried, H.1    Cahan, L.D.2    Paulson, J.C.3
  • 191
    • 0018903946 scopus 로고
    • Polyoma virus adsorbs to specific sialyloligosaccharide receptors on erythrocytes
    • Cahan, L.D.; Paulson, J.C. Polyoma virus adsorbs to specific sialyloligosaccharide receptors on erythrocytes. Virology 1980, 103, 505-509.
    • (1980) Virology , vol.103 , pp. 505-509
    • Cahan, L.D.1    Paulson, J.C.2
  • 192
    • 0026064895 scopus 로고
    • Polyomavirus tumor induction in mice: Effects of polymorphisms of VP1 and large T antigen
    • Freund, R.; Calderone, A.; Dawe, C.J.; Benjamin, T.L. Polyomavirus tumor induction in mice: effects of polymorphisms of VP1 and large T antigen. J. Virol. 1991, 65, 335-341.
    • (1991) J. Virol , vol.65 , pp. 335-341
    • Freund, R.1    Calderone, A.2    Dawe, C.J.3    Benjamin, T.L.4
  • 193
    • 0026064896 scopus 로고
    • A single-amino-acid substitution in polyomavirus VP1 correlates with plaque size and hemagglutination behavior
    • Freund, R.; Garcea, R.L.; Sahli, R.; Benjamin, T.L. A single-amino-acid substitution in polyomavirus VP1 correlates with plaque size and hemagglutination behavior. J. Virol. 1991, 65, 350-355.
    • (1991) J. Virol , vol.65 , pp. 350-355
    • Freund, R.1    Garcea, R.L.2    Sahli, R.3    Benjamin, T.L.4
  • 194
    • 10644290782 scopus 로고    scopus 로고
    • Ganglioside GD1a restores infectibility to mouse cells lacking functional receptors for polyomavirus
    • Gilbert, J.; Dahl, J.; Riney, C.; You, J.; Cui, C.; Holmes, R.; Lencer, W.; Benjamin, T. Ganglioside GD1a restores infectibility to mouse cells lacking functional receptors for polyomavirus. J. Virol. 2005, 79, 615-618.
    • (2005) J. Virol , vol.79 , pp. 615-618
    • Gilbert, J.1    Dahl, J.2    Riney, C.3    You, J.4    Cui, C.5    Holmes, R.6    Lencer, W.7    Benjamin, T.8
  • 196
    • 0037405891 scopus 로고    scopus 로고
    • Simian virus 40 infection of humans
    • Garcea, R.L.; Imperiale, M.J. Simian virus 40 infection of humans. J. Virol. 2003, 77, 5039-5045.
    • (2003) J. Virol , vol.77 , pp. 5039-5045
    • Garcea, R.L.1    Imperiale, M.J.2
  • 197
    • 0024596809 scopus 로고
    • Characterization of simian virus 40 receptor moieties on the surfaces of Vero C1008 cells
    • Clayson, E.T.; Compans, R.W. Characterization of simian virus 40 receptor moieties on the surfaces of Vero C1008 cells. J. Virol. 1989, 63, 1095-1100.
    • (1989) J. Virol , vol.63 , pp. 1095-1100
    • Clayson, E.T.1    Compans, R.W.2
  • 199
    • 0033062572 scopus 로고    scopus 로고
    • Simian virus 40 infection via MHC class I molecules and caveolae
    • Norkin, L.C. Simian virus 40 infection via MHC class I molecules and caveolae. Immunol. Rev. 1999, 168, 13-22.
    • (1999) Immunol. Rev , vol.168 , pp. 13-22
    • Norkin, L.C.1
  • 200
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin- and caveolin-1-independent endocytosis: Entry of simian virus 40 into cells devoid of caveolae
    • Damm, E.M.; Pelkmans, L.; Kartenbeck, J.; Mezzacasa, A.; Kurzchalia, T.; Helenius, A. Clathrin- and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae. J. Cell Biol. 2005, 168, 477-488.
    • (2005) J. Cell Biol , vol.168 , pp. 477-488
    • Damm, E.M.1    Pelkmans, L.2    Kartenbeck, J.3    Mezzacasa, A.4    Kurzchalia, T.5    Helenius, A.6
  • 201
    • 73349130473 scopus 로고    scopus 로고
    • High-speed nanoscopic tracking of the position and orientation of a single virus
    • Kukura, P.; Ewers, H.; Muller, C.; Renn, A.; Helenius, A.; Sandoghdar, V. High-speed nanoscopic tracking of the position and orientation of a single virus. Nat. Methods. 2009, 6, 923-927.
    • (2009) Nat. Methods , vol.6 , pp. 923-927
    • Kukura, P.1    Ewers, H.2    Muller, C.3    Renn, A.4    Helenius, A.5    Sandoghdar, V.6
  • 203
    • 0015232481 scopus 로고
    • New human papovavirus (B.K.) isolated from urine after renal transplantation
    • Gardner, S.D.; Field, A.M.; Coleman, D.V.; Hulme, B. New human papovavirus (B.K.) isolated from urine after renal transplantation. Lancet 1971, 1, 1253-1257.
    • (1971) Lancet , vol.1 , pp. 1253-1257
    • Gardner, S.D.1    Field, A.M.2    Coleman, D.V.3    Hulme, B.4
  • 204
    • 0015232447 scopus 로고
    • Cultivation of papova-like virus from human brain with progressive multifocal leucoencephalopathy
    • Padgett, B.L.; Walker, D.L.; ZuRhein, G.M.; Eckroade, R.J.; Dessel, B.H. Cultivation of papova-like virus from human brain with progressive multifocal leucoencephalopathy. Lancet 1971, 1, 1257-1260.
    • (1971) Lancet , vol.1 , pp. 1257-1260
    • Padgett, B.L.1    Walker, D.L.2    Zurhein, G.M.3    Eckroade, R.J.4    Dessel, B.H.5
  • 206
    • 16644393095 scopus 로고    scopus 로고
    • The JC virus-like particle overlay assay
    • Sawa, H.; Komagome, R. The JC virus-like particle overlay assay. Methods Mol. Biol. 2005, 292, 175-186.
    • (2005) Methods Mol. Biol , vol.292 , pp. 175-186
    • Sawa, H.1    Komagome, R.2
  • 207
    • 39749113080 scopus 로고    scopus 로고
    • Clonal integration of a polyomavirus in human Merkel cell carcinoma
    • Feng, H.; Shuda, M.; Chang, Y.; Moore, P.S. Clonal integration of a polyomavirus in human Merkel cell carcinoma. Science 2008, 319, 1096-1100.
    • (2008) Science , vol.319 , pp. 1096-1100
    • Feng, H.1    Shuda, M.2    Chang, Y.3    Moore, P.S.4
  • 208
    • 36249027278 scopus 로고    scopus 로고
    • Parvoviridae
    • 5 ed.; Knipe, D. M., Howley, P. M., Ed. Lippincott Williams&Wilkins: Philadelphia, PA
    • Berns, K.; Parish, C.R. Parvoviridae. In Fields Virology; 5 ed.; Knipe, D. M., Howley, P. M., Ed. Lippincott Williams&Wilkins: Philadelphia, PA, 2007; Vol. 2, pp. 2437-2477.
    • (2007) Fields Virology , vol.2 , pp. 2437-2477
    • Berns, K.1    Parish, C.R.2
  • 209
    • 0028860432 scopus 로고
    • Parvovirus B19 infection and hematopoiesis
    • Brown, K.E.; Young, N.S. Parvovirus B19 infection and hematopoiesis. Blood Rev. 1995, 9, 176-182.
    • (1995) Blood Rev , vol.9 , pp. 176-182
    • Brown, K.E.1    Young, N.S.2
  • 213
    • 40949119024 scopus 로고    scopus 로고
    • Simian parvoviruses: Biology and implications for research
    • Simon, M.A. Simian parvoviruses: biology and implications for research. Comp. Med. 2008, 58, 47-50.
    • (2008) Comp. Med , vol.58 , pp. 47-50
    • Simon, M.A.1
  • 214
    • 1542369977 scopus 로고    scopus 로고
    • From virus evolution to vector revolution: Use of naturally occurring serotypes of adeno-associated virus (AAV) as novel vectors for human gene therapy
    • Grimm, D.; Kay, M.A. From virus evolution to vector revolution: use of naturally occurring serotypes of adeno-associated virus (AAV) as novel vectors for human gene therapy. Curr. Gene Ther. 2003, 3, 281-304.
    • (2003) Curr. Gene Ther , vol.3 , pp. 281-304
    • Grimm, D.1    Kay, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.