메뉴 건너뛰기




Volumn 25, Issue 2, 2015, Pages 170-180

Affinities of human histo-blood group antigens for norovirus capsid protein complexes

Author keywords

affinities; antigen; electrospray ionization mass spectrometry; norovirus

Indexed keywords

BLOOD GROUP ANTIGEN; CAPSID PROTEIN; DIMER; DISACCHARIDE; EPITOPE; OLIGOSACCHARIDE; PROTEIN VP1; TETRASACCHARIDE; PROTEIN BINDING;

EID: 84941059261     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwu100     Document Type: Article
Times cited : (25)

References (44)
  • 1
    • 84857030465 scopus 로고    scopus 로고
    • Structure, stability and dynamics of norovirus P domain derived protein complexes studied by native mass spectrometry
    • Bereszczak JZ, Barbu IM, Tan M, Xia M, Jiang X, van Duijn E, Heck AJR. 2012. Structure, stability and dynamics of norovirus P domain derived protein complexes studied by native mass spectrometry. J Struct Biol. 177:273-282.
    • (2012) J Struct Biol. , vol.177 , pp. 273-282
    • Bereszczak, J.Z.1    Barbu, I.M.2    Tan, M.3    Xia, M.4    Jiang, X.5    Van Duijn, E.6    Heck, A.J.R.7
  • 2
    • 43949129092 scopus 로고    scopus 로고
    • Structural basis for the receptor binding specificity of Norwalk virus
    • Bu WM, 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.M.1    Mamedova, A.2    Tan, M.3    Xia, M.4    Jiang, X.5    Hegde, R.S.6
  • 3
    • 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 BVV. 2008. Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus. Proc Natl Acad Sci USA. 105:9175-9180.
    • (2008) Proc Natl Acad Sci USA. , vol.105 , pp. 9175-9180
    • Choi, J.M.1    Hutson, A.M.2    Estes, M.K.3    Prasad, B.V.V.4
  • 5
    • 0037090377 scopus 로고    scopus 로고
    • Quantitative determination of noncovalent binding interactions using soft ionization mass spectrometry
    • Daniel JM, Friess SD, Rajagopalan S, Wendt S, Zenobi R. 2002. Quantitative determination of noncovalent binding interactions using soft ionization mass spectrometry. Int J Mass Spectrom. 216:1-27.
    • (2002) Int J Mass Spectrom. , vol.216 , pp. 1-27
    • Daniel, J.M.1    Friess, S.D.2    Rajagopalan, S.3    Wendt, S.4    Zenobi, R.5
  • 7
    • 84860487856 scopus 로고    scopus 로고
    • Quantifying ligand binding to large protein complexes using electrospray ionization mass spectrometry
    • El-Hawiet A, Kitova EN, Arutyunov D, Simpson DJ, Szymanski CM, Klassen JS. 2012. Quantifying ligand binding to large protein complexes using electrospray ionization mass spectrometry. Anal Chem. 84:3867-3870.
    • (2012) Anal Chem. , vol.84 , pp. 3867-3870
    • El-Hawiet, A.1    Kitova, E.N.2    Arutyunov, D.3    Simpson, D.J.4    Szymanski, C.M.5    Klassen, J.S.6
  • 8
    • 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 PI, Parra F, 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.
    • (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
  • 11
    • 80051665526 scopus 로고    scopus 로고
    • The Overall architecture and receptor binding of pneumococcal carbohydrateantigen-hydrolyzing enzymes
    • Higgins MA, Ficko-Blean E, Meloncelli PJ, Lowary TL, Boraston AB. 2011. The Overall architecture and receptor binding of pneumococcal carbohydrateantigen-hydrolyzing enzymes. J Mol Biol. 411:1017-1036.
    • (2011) J Mol Biol. , vol.411 , pp. 1017-1036
    • Higgins, M.A.1    Ficko-Blean, E.2    Meloncelli, P.J.3    Lowary, T.L.4    Boraston, A.B.5
  • 14
    • 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, Thornton S, Morrow AL, 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.
    • (2005) J Virol. , vol.79 , pp. 6714-6722
    • Huang, P.1    Farkas, T.2    Zhong, W.3    Thornton, S.4    Morrow, A.L.5    Jiang, X.6
  • 15
    • 0036569142 scopus 로고    scopus 로고
    • Norwalk virus infection and disease is associated with ABO histo-blood group type
    • Hutson AM, Atmar RL, Graham DY, Estes MK. 2002. Norwalk virus infection and disease is associated with ABO histo-blood group type. J Infect Dis. 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
  • 16
    • 0037213273 scopus 로고    scopus 로고
    • Norwalk virus-like particle hemagglutination by binding to H histo-blood group antigens
    • Hutson AM, Atmar RL, Marcus DM, Estes MK. 2003. Norwalk virus-like particle hemagglutination by binding to H histo-blood group antigens. J Virol. 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
  • 17
    • 0026649563 scopus 로고
    • Expression, self-assembly, and antigenicity of the Norwalk virus capsid protein
    • Jiang X, Wang M, Graham DY, Estes MK. 1992. Expression, self-assembly, and antigenicity of the Norwalk virus capsid protein. J Virol. 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
  • 19
    • 84860557228 scopus 로고    scopus 로고
    • Reliable determinations of protein-ligand interactions by direct ESI-MS measurements. Are we there yet?
    • Kitova EN, El-Hawiet A, Schnier PD, Klassen JS. 2012. Reliable determinations of protein-ligand interactions by direct ESI-MS measurements. Are we there yet? J Am Soc Mass Spectrom. 23:431-441.
    • (2012) J Am Soc Mass Spectrom. , vol.23 , pp. 431-441
    • Kitova, E.N.1    El-Hawiet, A.2    Schnier, P.D.3    Klassen, J.S.4
  • 20
    • 67650572153 scopus 로고    scopus 로고
    • Synthesis of ABO histo-blood group type v and VI antigens
    • Meloncelli PJ, Lowary TL. 2009. Synthesis of ABO histo-blood group type V and VI antigens. Aust J Chem. 62:558-574.
    • (2009) Aust J Chem. , vol.62 , pp. 558-574
    • Meloncelli, P.J.1    Lowary, T.L.2
  • 21
    • 77958083901 scopus 로고    scopus 로고
    • Synthesis of ABO histo-blood group type i and II antigens
    • Meloncelli PJ, Lowary TL. 2010. Synthesis of ABO histo-blood group type I and II antigens. Carbohydr Res. 345:2305-2322.
    • (2010) Carbohydr Res. , vol.345 , pp. 2305-2322
    • Meloncelli, P.J.1    Lowary, T.L.2
  • 22
    • 79960010824 scopus 로고    scopus 로고
    • Synthesis andNMR studies on the ABO histo-blood group antigens: Synthesis of type III and IV structures and NMR characterization of type I-VI antigens
    • Meloncelli PJ, West LJ, Lowary TL. 2011. Synthesis andNMR studies on the ABO histo-blood group antigens: Synthesis of type III and IV structures and NMR characterization of type I-VI antigens. Carbohydr Res. 346:1406-1426.
    • (2011) Carbohydr Res. , vol.346 , pp. 1406-1426
    • Meloncelli, P.J.1    West, L.J.2    Lowary, T.L.3
  • 23
    • 0025633159 scopus 로고
    • Genetic-control of the fucosylation of abh precursor chains-evidence for new epistatic interactions in different cells and tissues
    • Oriol R. 1990. Genetic-control of the fucosylation of abh precursor chains-evidence for new epistatic interactions in different cells and tissues. J Immunogenet. 17:235-245.
    • (1990) J Immunogenet. , vol.17 , pp. 235-245
    • Oriol, R.1
  • 27
    • 0033980199 scopus 로고    scopus 로고
    • Tissue distribution of histo-blood group antigens
    • Ravn V, Dabelsteen E. 2000. Tissue distribution of histo-blood group antigens. APMIS. 108:1-28.
    • (2000) APMIS. , vol.108 , pp. 1-28
    • Ravn, V.1    Dabelsteen, E.2
  • 28
    • 0030922424 scopus 로고    scopus 로고
    • Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferase boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes
    • Seto NOL, PalcicMM, Compston CA, Li H, Bundle DR, Narang SA. 1997. Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferase boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes. J Biol Chem. 272:14133-14138.
    • (1997) J Biol Chem. , vol.272 , pp. 14133-14138
    • Seto, N.O.L.1    Palcic, M.M.2    Compston, C.A.3    Li, H.4    Bundle, D.R.5    Narang, S.A.6
  • 30
    • 48349091000 scopus 로고    scopus 로고
    • Temperature-dependent cooperativity in donor-acceptor substrate binding to the human blood group glycosyltransferases
    • Shoemaker GK, Soya N, Palcic MM, Klassen JS. 2008. Temperature-dependent cooperativity in donor-acceptor substrate binding to the human blood group glycosyltransferases. Glycobiology. 18:587-592.
    • (2008) Glycobiology. , vol.18 , pp. 587-592
    • Shoemaker, G.K.1    Soya, N.2    Palcic, M.M.3    Klassen, J.S.4
  • 32
    • 70349996471 scopus 로고    scopus 로고
    • Comparative study of substrate and product binding to the human ABO(H) blood group glycosyltransferases
    • Soya N, Shoemaker GK, Palcic MM, Klassen JS. 2009. Comparative study of substrate and product binding to the human ABO(H) blood group glycosyltransferases. Glycobiology. 19:1224-1234.
    • (2009) Glycobiology. , vol.19 , pp. 1224-1234
    • Soya, N.1    Shoemaker, G.K.2    Palcic, M.M.3    Klassen, J.S.4
  • 33
    • 33646589615 scopus 로고    scopus 로고
    • Method for distinguishing specific from nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry
    • Sun J, Kitova EN, WangW, Klassen JS. 2006. Method for distinguishing specific from nonspecific protein-ligand complexes in nanoelectrospray ionization mass spectrometry. Anal Chem. 78:3010-3018.
    • (2006) Anal Chem. , vol.78 , pp. 3010-3018
    • Sun, J.1    Kitova, E.N.2    Wang, W.3    Klassen, J.S.4
  • 35
    • 55249104282 scopus 로고    scopus 로고
    • Noroviral P particle: Structure, function and applications in virus-host interaction
    • Tan M, Fang P, Chachiyo T, Xia M, Huang P, Fang Z, JiangW, Jiang X. 2008. Noroviral P particle: Structure, function and applications in virus-host interaction. Virology. 382:115-123.
    • (2008) Virology. , vol.382 , pp. 115-123
    • Tan, M.1    Fang, P.2    Chachiyo, T.3    Xia, M.4    Huang, P.5    Fang, Z.6    Jiang, W.7    Jiang, X.8
  • 36
    • 78751706360 scopus 로고    scopus 로고
    • Terminal modifications of norovirus P domain resulted in a new type of subviral particles, the small P particles
    • Tan M, Fang P, Xia M, Chachiyo T, Jiang W, Jiang X. 2011. Terminal modifications of norovirus P domain resulted in a new type of subviral particles, the small P particles. Virology. 410:345-352.
    • (2011) Virology. , vol.410 , pp. 345-352
    • Tan, M.1    Fang, P.2    Xia, M.3    Chachiyo, T.4    Jiang, W.5    Jiang, X.6
  • 37
    • 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 RS, Jiang X. 2004. The P domain of norovirus capsid protein forms dimer and binds to histo-blood group antigen receptors. J Virol. 78:6233-6242.
    • (2004) J Virol. , vol.78 , pp. 6233-6242
    • Tan, M.1    Hegde, R.S.2    Jiang, X.3
  • 38
    • 20344400111 scopus 로고    scopus 로고
    • Norovirus and its histo-blood group antigen receptors: An answer to a historical puzzle
    • TanM, Jiang X. 2005a. Norovirus and its histo-blood group antigen receptors: An answer to a historical puzzle. Trends Microbiol. 13:285-293.
    • (2005) Trends Microbiol. , vol.13 , pp. 285-293
    • Tan, M.1    Jiang, X.2
  • 39
    • 27644437147 scopus 로고    scopus 로고
    • The P domain of norovirus capsid protein forms a subviral particle that binds to histo-blood group antigen receptors
    • TanM, Jiang X. 2005b. The P domain of norovirus capsid protein forms a subviral particle that binds to histo-blood group antigen receptors. J Virol. 79:14017-14030.
    • (2005) J Virol. , vol.79 , pp. 14017-14030
    • Tan, M.1    Jiang, X.2
  • 43
    • 0030823649 scopus 로고    scopus 로고
    • Biochemical characterization of a smaller form of recombinant Norwalk virus capsids assembled in insect cells
    • White LJ, Hardy ME, Estes HK. 1997. Biochemical characterization of a smaller form of recombinant Norwalk virus capsids assembled in insect cells. J Virol. 71:8066-8072.
    • (1997) J Virol. , vol.71 , pp. 8066-8072
    • White, L.J.1    Hardy, M.E.2    Estes, H.K.3
  • 44
    • 0028231880 scopus 로고
    • Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1. 7-angstrom resolution
    • Zdanov A, Li Y, Bundle DR, Deng SJ, Mackenzie CR, Narang SA, Young NM, Cygler M. 1994. Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1. 7-angstrom resolution. Proc Natl Acad Sci USA. 91:6423-6427.
    • (1994) Proc Natl Acad Sci USA. , vol.91 , pp. 6423-6427
    • Zdanov, A.1    Li, Y.2    Bundle, D.R.3    Deng, S.J.4    Mackenzie, C.R.5    Narang, S.A.6    Young, N.M.7    Cygler, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.