메뉴 건너뛰기




Volumn 12, Issue 5, 2017, Pages 1288-1296

Histo-Blood Group Antigen Presentation Is Critical for Binding of Norovirus VLP to Glycosphingolipids in Model Membranes

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD GROUP ANTIGEN; EPITOPE; GLYCAN; GLYCOSPHINGOLIPID; HISTO BLOOD GROUP ANTIGEN; UNCLASSIFIED DRUG;

EID: 85019578656     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.7b00152     Document Type: Article
Times cited : (25)

References (45)
  • 1
    • 84969791255 scopus 로고    scopus 로고
    • Human norovirus transmission and evolution in a changing world
    • de Graaf, M., van Beek, J., and Koopmans, M. P. (2016) Human norovirus transmission and evolution in a changing world Nat. Rev. Microbiol. 14, 421-433 10.1038/nrmicro.2016.48
    • (2016) Nat. Rev. Microbiol. , vol.14 , pp. 421-433
    • De Graaf, M.1    Van Beek, J.2    Koopmans, M.P.3
  • 2
    • 85019550876 scopus 로고    scopus 로고
    • Norovirus strikes back
    • David, R. (2013) Norovirus strikes back Nat. Rev. Microbiol. 11, 70-70 10.1038/nrmicro2962
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 70
    • David, R.1
  • 3
    • 84872863060 scopus 로고    scopus 로고
    • Molecular epidemiology of noroviruses associated with acute sporadic gastroenteritis in children: Global distribution of genogroups, genotypes and GII.4 variants
    • Hoa Tran, T. N., Trainor, E., Nakagomi, T., Cunliffe, N. A., and Nakagomi, O. (2013) Molecular epidemiology of noroviruses associated with acute sporadic gastroenteritis in children: global distribution of genogroups, genotypes and GII.4 variants J. Clin. Virol. 56, 269-277 10.1016/j.jcv.2012.11.011
    • (2013) J. Clin. Virol. , vol.56 , pp. 269-277
    • Hoa Tran, T.N.1    Trainor, E.2    Nakagomi, T.3    Cunliffe, N.A.4    Nakagomi, O.5
  • 4
    • 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., and Larson, G. (2009) QCM-D studies of human norovirus VLPs binding to glycosphingolipids in supported lipid bilayers reveal strain-specific characteristics Glycobiology 19, 1176-1184 10.1093/glycob/cwp103
    • (2009) Glycobiology , vol.19 , pp. 1176-1184
    • Rydell, G.E.1    Dahlin, A.B.2    Hook, F.3    Larson, G.4
  • 5
    • 18744372741 scopus 로고    scopus 로고
    • Norovirus and histo-blood group antigens: Demonstration of a wide spectrum of strain specificities and classification of two major binding groups among multiple binding patterns
    • Huang, P., Farkas, T., Zhong, W., Tan, M., Thornton, S., Morrow, A. L., and Jiang, X. (2005) Norovirus and histo-blood group antigens: demonstration of a wide spectrum of strain specificities and classification of two major binding groups among multiple binding patterns J. Virol. 79, 6714-6722 10.1128/JVI.79.11.6714-6722.2005
    • (2005) J. Virol. , vol.79 , pp. 6714-6722
    • Huang, P.1    Farkas, T.2    Zhong, W.3    Tan, M.4    Thornton, S.5    Morrow, A.L.6    Jiang, X.7
  • 7
    • 80055101132 scopus 로고    scopus 로고
    • Susceptibility to winter vomiting disease: A sweet matter
    • Rydell, G. E., Kindberg, E., Larson, G., and Svensson, L. (2011) Susceptibility to winter vomiting disease: a sweet matter Rev. Med. Virol. 21, 370-382 10.1002/rmv.704
    • (2011) Rev. Med. Virol. , vol.21 , pp. 370-382
    • Rydell, G.E.1    Kindberg, E.2    Larson, G.3    Svensson, L.4
  • 8
    • 29744442306 scopus 로고    scopus 로고
    • A homozygous nonsense mutation (428G→ A) in the human secretor (FUT2) gene provides resistance to symptomatic norovirus (GGII) infections
    • Thorven, M., Grahn, A., Hedlund, K.-O., Johansson, H., Wahlfrid, C., Larson, G., and Svensson, L. (2005) A homozygous nonsense mutation (428G→ A) in the human secretor (FUT2) gene provides resistance to symptomatic norovirus (GGII) infections Journal of virology 79, 15351-15355 10.1128/JVI.79.24.15351-15355.2005
    • (2005) Journal of Virology , vol.79 , pp. 15351-15355
    • Thorven, M.1    Grahn, A.2    Hedlund, K.-O.3    Johansson, H.4    Wahlfrid, C.5    Larson, G.6    Svensson, L.7
  • 10
    • 0021363731 scopus 로고
    • Tissue specificity of glycosphingolipids as expressed in pancreas and small intestine of blood group A and B human individuals
    • Breimer, M. E. (1984) Tissue specificity of glycosphingolipids as expressed in pancreas and small intestine of blood group A and B human individuals Arch. Biochem. Biophys. 228, 71-85 10.1016/0003-9861(84)90048-1
    • (1984) Arch. Biochem. Biophys. , vol.228 , pp. 71-85
    • Breimer, M.E.1
  • 11
    • 0024580871 scopus 로고
    • Novel polyfucosylated N-linked glycopeptides with blood group A, H, X, and y determinants from human small intestinal epithelial cells
    • Finne, J., Breimer, M., Hansson, G., Karlsson, K., Leffler, H., Vliegenthart, J., and Van Halbeek, H. (1989) Novel polyfucosylated N-linked glycopeptides with blood group A, H, X, and Y determinants from human small intestinal epithelial cells J. Biol. Chem. 264, 5720-5735
    • (1989) J. Biol. Chem. , vol.264 , pp. 5720-5735
    • Finne, J.1    Breimer, M.2    Hansson, G.3    Karlsson, K.4    Leffler, H.5    Vliegenthart, J.6    Van Halbeek, H.7
  • 12
    • 0027474954 scopus 로고
    • Orientation of the saccharide chains of glycolipids at the membrane surface: Conformational analysis of the glucose-ceramide and the glucose-glyceride linkages using molecular mechanics (MM3)
    • Nyholm, P. G. and Pascher, I. (1993) Orientation of the saccharide chains of glycolipids at the membrane surface: conformational analysis of the glucose-ceramide and the glucose-glyceride linkages using molecular mechanics (MM3) Biochemistry 32, 1225-1234 10.1021/bi00056a005
    • (1993) Biochemistry , vol.32 , pp. 1225-1234
    • Nyholm, P.G.1    Pascher, I.2
  • 13
    • 0024761484 scopus 로고
    • Conformational analysis of blood group A-active glycosphingolipids using HSEA-calculations. the possible significance of the core oligosaccharide chain for the presentation and recognition of the A-determinant
    • Nyholm, P. G., Samuelsson, B. E., Breimer, M., and Pascher, I. (1989) Conformational analysis of blood group A-active glycosphingolipids using HSEA-calculations. The possible significance of the core oligosaccharide chain for the presentation and recognition of the A-determinant J. Mol. Recognit. 2, 103-113 10.1002/jmr.300020302
    • (1989) J. Mol. Recognit. , vol.2 , pp. 103-113
    • Nyholm, P.G.1    Samuelsson, B.E.2    Breimer, M.3    Pascher, I.4
  • 14
    • 0025990949 scopus 로고
    • Saccharide orientation at the cell surface affects glycolipid receptor function
    • Strömberg, N., Nyholm, P.-G., Pascher, I., and Normark, S. (1991) Saccharide orientation at the cell surface affects glycolipid receptor function Proc. Natl. Acad. Sci. U. S. A. 88, 9340-9344 10.1073/pnas.88.20.9340
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 9340-9344
    • Strömberg, N.1    Nyholm, P.-G.2    Pascher, I.3    Normark, S.4
  • 15
    • 0027989814 scopus 로고
    • Common tetrasaccharide epitope NeuAc alpha 2 - >3Gal beta 1 - >3(Neu-Ac alpha 2 - >6)GalNAc, presented by different carrier glycosylceramides or O-linked peptides, is recognized by different antibodies and ligands having distinct specificities
    • Saito, S., Levery, S. B., Salyan, M. E., Goldberg, R. I., and Hakomori, S. (1994) Common tetrasaccharide epitope NeuAc alpha 2 - >3Gal beta 1 - >3(Neu-Ac alpha 2 - >6)GalNAc, presented by different carrier glycosylceramides or O-linked peptides, is recognized by different antibodies and ligands having distinct specificities J. Biol. Chem. 269, 5644-5652
    • (1994) J. Biol. Chem. , vol.269 , pp. 5644-5652
    • Saito, S.1    Levery, S.B.2    Salyan, M.E.3    Goldberg, R.I.4    Hakomori, S.5
  • 17
    • 84856006189 scopus 로고    scopus 로고
    • Molecular details of the recognition of blood group antigens by a human norovirus as determined by STD NMR spectroscopy
    • Fiege, B., Rademacher, C., Cartmell, J., Kitov, P. I., Parra, F., and Peters, T. (2012) Molecular details of the recognition of blood group antigens by a human norovirus as determined by STD NMR spectroscopy Angew. Chem., Int. Ed. 51, 928-932 10.1002/anie.201105719
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 928-932
    • Fiege, B.1    Rademacher, C.2    Cartmell, J.3    Kitov, P.I.4    Parra, F.5    Peters, T.6
  • 18
    • 80155164903 scopus 로고    scopus 로고
    • Interaction of single viruslike particles with vesicles containing glycosphingolipids
    • Bally, M., Gunnarsson, A., Svensson, L., Larson, G., Zhdanov, V. P., and Hook, F. (2011) Interaction of single viruslike particles with vesicles containing glycosphingolipids Phys. Rev. Lett. 107, 188103 10.1103/PhysRevLett.107.188103
    • (2011) Phys. Rev. Lett. , vol.107 , pp. 188103
    • Bally, M.1    Gunnarsson, A.2    Svensson, L.3    Larson, G.4    Zhdanov, V.P.5    Hook, F.6
  • 19
    • 84941313212 scopus 로고    scopus 로고
    • Interaction of Virus-Like Particles with Vesicles Containing Glycolipids: Kinetics of Detachment
    • Nasir, W., Bally, M., Zhdanov, V. P., Larson, G., and Hook, F. (2015) Interaction of Virus-Like Particles with Vesicles Containing Glycolipids: Kinetics of Detachment J. Phys. Chem. B 119, 11466-11472 10.1021/acs.jpcb.5b04160
    • (2015) J. Phys. Chem. B , vol.119 , pp. 11466-11472
    • Nasir, W.1    Bally, M.2    Zhdanov, V.P.3    Larson, G.4    Hook, F.5
  • 20
    • 0023161197 scopus 로고
    • Overlay and solid-phase analysis of glycolipid receptors for bacteria and viruses
    • Karlsson, K. A. and Stromberg, N. (1987) Overlay and solid-phase analysis of glycolipid receptors for bacteria and viruses Methods Enzymol. 138, 220-232 10.1016/0076-6879(87)38019-X
    • (1987) Methods Enzymol. , vol.138 , pp. 220-232
    • Karlsson, K.A.1    Stromberg, N.2
  • 22
    • 75749138064 scopus 로고    scopus 로고
    • Presentation of membrane-anchored glycosphingolipids determined from molecular dynamics simulations and NMR paramagnetic relaxation rate enhancement
    • Demarco, M. L., Woods, R. J., Prestegard, J. H., and Tian, F. (2010) Presentation of membrane-anchored glycosphingolipids determined from molecular dynamics simulations and NMR paramagnetic relaxation rate enhancement J. Am. Chem. Soc. 132, 1334-1338 10.1021/ja907518x
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1334-1338
    • Demarco, M.L.1    Woods, R.J.2    Prestegard, J.H.3    Tian, F.4
  • 23
    • 79960933686 scopus 로고    scopus 로고
    • Crystallography of a Lewis-binding norovirus, elucidation of strain-specificity to the polymorphic human histo-blood group antigens
    • Chen, Y., Tan, M., Xia, M., Hao, N., Zhang, X. C., Huang, P., Jiang, X., Li, X., and Rao, Z. (2011) Crystallography of a Lewis-binding norovirus, elucidation of strain-specificity to the polymorphic human histo-blood group antigens PLoS Pathog. 7, e1002152 10.1371/journal.ppat.1002152
    • (2011) PLoS Pathog. , vol.7 , pp. e1002152
    • Chen, Y.1    Tan, M.2    Xia, M.3    Hao, N.4    Zhang, X.C.5    Huang, P.6    Jiang, X.7    Li, X.8    Rao, Z.9
  • 25
    • 0023000722 scopus 로고
    • Genetics of ABO, H, Lewis, X and related antigens
    • Oriol, R., Pendu, J., and Mollicone, R. (1986) Genetics of ABO, H, Lewis, X and related antigens Vox Sang. 51, 161-171 10.1111/j.1423-0410.1986.tb01946.x
    • (1986) Vox Sang. , vol.51 , pp. 161-171
    • Oriol, R.1    Pendu, J.2    Mollicone, R.3
  • 26
    • 0027218091 scopus 로고
    • 7 the blood group-specific human glycosyltransferases
    • Lowe, J. B. (1993) 7 The blood group-specific human glycosyltransferases Baillieres Clin. Haematol. 6, 465-492 10.1016/S0950-3536(05)80155-6
    • (1993) Baillieres Clin. Haematol. , vol.6 , pp. 465-492
    • Lowe, J.B.1
  • 28
    • 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., and Svensson, L. (2006) Antibody prevalence and titer to norovirus (genogroup II) correlate with secretor (FUT2) but not with ABO phenotype or Lewis (FUT3) genotype J. Infect. Dis. 194, 1422-1427 10.1086/508430
    • (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
  • 29
    • 0023654973 scopus 로고
    • Structures of blood group glycosphingolipids of human small intestine. A relation between the expression of fucolipids of epithelial cells and the ABO, le and Se phenotype of the donor
    • Björk, S., Breimer, M., Hansson, G. C., Karlsson, K.-A., and Leffler, H. (1987) Structures of blood group glycosphingolipids of human small intestine. A relation between the expression of fucolipids of epithelial cells and the ABO, Le and Se phenotype of the donor J. Biol. Chem. 262, 6758-6765
    • (1987) J. Biol. Chem. , vol.262 , pp. 6758-6765
    • Björk, S.1    Breimer, M.2    Hansson, G.C.3    Karlsson, K.-A.4    Leffler, H.5
  • 32
    • 84877057550 scopus 로고    scopus 로고
    • Human GII.4 norovirus VLP induces membrane invaginations on giant unilamellar vesicles containing secretor gene dependent alpha1,2-fucosylated glycosphingolipids
    • Rydell, G. E., Svensson, L., Larson, G., Johannes, L., and Romer, W. (2013) Human GII.4 norovirus VLP induces membrane invaginations on giant unilamellar vesicles containing secretor gene dependent alpha1,2-fucosylated glycosphingolipids Biochim. Biophys. Acta, Biomembr. 1828, 1840-1845 10.1016/j.bbamem.2013.03.016
    • (2013) Biochim. Biophys. Acta, Biomembr. , vol.1828 , pp. 1840-1845
    • Rydell, G.E.1    Svensson, L.2    Larson, G.3    Johannes, L.4    Romer, W.5
  • 33
    • 84875188554 scopus 로고    scopus 로고
    • Equilibrium-fluctuation-analysis of single liposome binding events reveals how cholesterol and Ca2+ modulate glycosphingolipid trans-interactions
    • Kunze, A., Bally, M., Hook, F., and Larson, G. (2013) Equilibrium-fluctuation-analysis of single liposome binding events reveals how cholesterol and Ca2+ modulate glycosphingolipid trans-interactions Sci. Rep. 3, 1452 10.1038/srep01452
    • (2013) Sci. Rep. , vol.3 , pp. 1452
    • Kunze, A.1    Bally, M.2    Hook, F.3    Larson, G.4
  • 34
    • 84941695633 scopus 로고    scopus 로고
    • Preserved transmembrane protein mobility in polymer-supported lipid bilayers derived from cell membranes
    • Pace, H., Simonsson Nyström, L., Gunnarsson, A., Eck, E., Monson, C., Geschwindner, S., Snijder, A., and Höök, F. (2015) Preserved transmembrane protein mobility in polymer-supported lipid bilayers derived from cell membranes Anal. Chem. 87, 9194-9203 10.1021/acs.analchem.5b01449
    • (2015) Anal. Chem. , vol.87 , pp. 9194-9203
    • Pace, H.1    Simonsson Nyström, L.2    Gunnarsson, A.3    Eck, E.4    Monson, C.5    Geschwindner, S.6    Snijder, A.7    Höök, F.8
  • 35
    • 0019407796 scopus 로고
    • Molecular characterization of cell surface antigens of fetal tissue. Detailed analysis of glycosphingolipids of meconium of a human O Le(a - B+) secretor
    • Karlsson, K. A. and Larson, G. (1981) Molecular characterization of cell surface antigens of fetal tissue. Detailed analysis of glycosphingolipids of meconium of a human O Le(a - b+) secretor J. Biol. Chem. 256, 3512-3524
    • (1981) J. Biol. Chem. , vol.256 , pp. 3512-3524
    • Karlsson, K.A.1    Larson, G.2
  • 36
    • 0023161196 scopus 로고
    • Preparation of total nonacid glycolipids for overlay analysis of receptors for bacteria and viruses and for other studies
    • Karlsson, K. A. (1987) Preparation of total nonacid glycolipids for overlay analysis of receptors for bacteria and viruses and for other studies Methods Enzymol. 138, 212-220 10.1016/0076-6879(87)38018-8
    • (1987) Methods Enzymol. , vol.138 , pp. 212-220
    • Karlsson, K.A.1
  • 38
    • 1942501581 scopus 로고    scopus 로고
    • Crystal structure of norwalk virus polymerase reveals the carboxyl terminus in the active site cleft
    • Ng, K. K., Pendas-Franco, N., Rojo, J., Boga, J. A., Machin, A., Alonso, J. M., and Parra, F. (2004) Crystal structure of norwalk virus polymerase reveals the carboxyl terminus in the active site cleft J. Biol. Chem. 279, 16638-16645 10.1074/jbc.M400584200
    • (2004) J. Biol. Chem. , vol.279 , pp. 16638-16645
    • Ng, K.K.1    Pendas-Franco, N.2    Rojo, J.3    Boga, J.A.4    Machin, A.5    Alonso, J.M.6    Parra, F.7
  • 39
    • 84908088475 scopus 로고    scopus 로고
    • YASARA View - Molecular graphics for all devices - From smartphones to workstations
    • Krieger, E. and Vriend, G. (2014) YASARA View-molecular graphics for all devices-from smartphones to workstations Bioinformatics 30, 2981-2982 10.1093/bioinformatics/btu426
    • (2014) Bioinformatics , vol.30 , pp. 2981-2982
    • Krieger, E.1    Vriend, G.2
  • 40
    • 84928476077 scopus 로고    scopus 로고
    • New ways to boost molecular dynamics simulations
    • Krieger, E. and Vriend, G. (2015) New ways to boost molecular dynamics simulations J. Comput. Chem. 36, 996-1007 10.1002/jcc.23899
    • (2015) J. Comput. Chem. , vol.36 , pp. 996-1007
    • Krieger, E.1    Vriend, G.2
  • 42
    • 33751155339 scopus 로고
    • Molecular mechanical and molecular dynamic simulations of glycoproteins and oligosaccharides. 1. GLYCAM-93 parameter development
    • Woods, R. J., Dwek, R. A., Edge, C. J., and Fraser-Reid, B. (1995) Molecular mechanical and molecular dynamic simulations of glycoproteins and oligosaccharides. 1. GLYCAM-93 parameter development J. Phys. Chem. 99, 3832-3846 10.1021/j100011a061
    • (1995) J. Phys. Chem. , vol.99 , pp. 3832-3846
    • Woods, R.J.1    Dwek, R.A.2    Edge, C.J.3    Fraser-Reid, B.4
  • 43
    • 0036890178 scopus 로고    scopus 로고
    • Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation
    • Jakalian, A., Jack, D. B., and Bayly, C. I. (2002) Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation J. Comput. Chem. 23, 1623-1641 10.1002/jcc.10128
    • (2002) J. Comput. Chem. , vol.23 , pp. 1623-1641
    • Jakalian, A.1    Jack, D.B.2    Bayly, C.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.