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Volumn 27, Issue 1, 2017, Pages 80-86

Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistepbinding of L-fucose to norovirus particles

Author keywords

Cooperative binding; Norovirus infection; Protein carbohydrate interaction; STD NMR titrations; Virus like particles

Indexed keywords

CAPSID PROTEIN; DIMER; FUCOSE; LIGAND; BLOOD GROUP ANTIGEN; PROTEIN BINDING;

EID: 85014425426     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cww070     Document Type: Article
Times cited : (14)

References (42)
  • 2
    • 77954346685 scopus 로고    scopus 로고
    • Ligand-receptor binding affinities from saturation transfer difference (STD) NMR spectroscopy: The binding isotherm of STD initial growth rates
    • Angulo J, Enriquez-Navas PM, Nieto PM. 2010. Ligand-receptor binding affinities from saturation transfer difference (STD) NMR spectroscopy: The binding isotherm of STD initial growth rates. Chemistry. 16:7803-7812.
    • (2010) Chemistry , vol.16 , pp. 7803-7812
    • Angulo, J.1    Enriquez-Navas, P.M.2    Nieto, P.M.3
  • 3
    • 84869093870 scopus 로고    scopus 로고
    • The potential economic value of a human norovirus vaccine for the United States
    • Bartsch SM, Lopman BA, Hall AJ, Parashar UD, Lee BY. 2012. The potential economic value of a human norovirus vaccine for the United States. Vaccine. 30:7097-7104.
    • (2012) Vaccine , vol.30 , pp. 7097-7104
    • Bartsch, S.M.1    Lopman, B.A.2    Hall, A.J.3    Parashar, U.D.4    Lee, B.Y.5
  • 4
    • 0037425531 scopus 로고    scopus 로고
    • Virus-ligand interactions: Identification and characterization of ligand binding by NMR spectroscopy
    • Benie AJ, Moser R, Bauml E, Blaas D, Peters T. 2003. Virus-ligand interactions: Identification and characterization of ligand binding by NMR spectroscopy. J Am Chem Soc. 125:14-15.
    • (2003) J Am Chem Soc , vol.125 , pp. 14-15
    • Benie, A.J.1    Moser, R.2    Bauml, E.3    Blaas, D.4    Peters, T.5
  • 5
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar DLD, Klug A. 1962. Physical principles in the construction of regular viruses. Cold Spring Harb Symp Quant Biol. 27:1-24.
    • (1962) Cold Spring Harb Symp Quant Biol , vol.27 , pp. 1-24
    • Dld, C.1    Klug, A.2
  • 6
    • 0021658956 scopus 로고
    • Allostery without conformational change. A plausible model
    • Cooper A, Dryden DTF. 1984. Allostery without conformational change. A plausible model. Eur Biophys J. 11:103-109.
    • (1984) Eur Biophys J , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.F.2
  • 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. 51:928-932.
    • (2012) Angew Chem , 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
    • 80052054459 scopus 로고    scopus 로고
    • Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability
    • Hansman GS, Biertumpfel C, Georgiev I, McLellan JS, Chen L, Zhou T, Katayama K, Kwong PD. 2011. Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. J Virol. 85:6687-6701.
    • (2011) J Virol , vol.85 , pp. 6687-6701
    • Hansman, G.S.1    Biertumpfel, C.2    Georgiev, I.3    McLellan, J.S.4    Chen, L.5    Zhou, T.6    Katayama, K.7    Kwong, P.D.8
  • 16
    • 0036290185 scopus 로고    scopus 로고
    • Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes
    • Jayalakshmi V, Krishna NR. 2002. Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes. J Magn Reson. 155:106-118.
    • (2002) J Magn Reson , vol.155 , pp. 106-118
    • Jayalakshmi, V.1    Krishna, N.R.2
  • 17
    • 58149396562 scopus 로고    scopus 로고
    • Saturation transfer difference nuclear magnetic resonance study on the specific binding of ligand to protein
    • Ji Z, Yao Z, Liu M. 2009. Saturation transfer difference nuclear magnetic resonance study on the specific binding of ligand to protein. Anal Biochem. 385:380-382.
    • (2009) Anal Biochem , vol.385 , pp. 380-382
    • Ji, Z.1    Yao, Z.2    Liu, M.3
  • 19
    • 79551544664 scopus 로고    scopus 로고
    • Noroviruses: The principal cause of foodborne disease worldwide
    • Koo HL, Ajami N, Atmar RL, DuPont HL. 2010. Noroviruses: The principal cause of foodborne disease worldwide. Discov Med. 10:61-70.
    • (2010) Discov Med , vol.10 , pp. 61-70
    • Koo, H.L.1    Ajami, N.2    Atmar, R.L.3    DuPont, H.L.4
  • 23
    • 39849096606 scopus 로고    scopus 로고
    • The evolution of norovirus, the "gastric flu"
    • Lopman B, Zambon M, Brown DW. 2008. The evolution of norovirus, the "gastric flu". PLoS Med. 5:e42.
    • (2008) PLoS Med , vol.5 , pp. e42
    • Lopman, B.1    Zambon, M.2    Brown, D.W.3
  • 24
    • 84983142797 scopus 로고    scopus 로고
    • A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus
    • Mallagaray A, Dominguez G, Peters T, Perez-Castells J. 2016. A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus. Chem Commun (Camb). 52:601-604.
    • (2016) Chem Commun (Camb) , vol.52 , pp. 601-604
    • Mallagaray, A.1    Dominguez, G.2    Peters, T.3    Perez-Castells, J.4
  • 26
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • Mayer M, Meyer B. 1999. Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew Chem Int Ed. 38: 1784-1787.
    • (1999) Angew Chem Int Ed , vol.38 , pp. 1784-1787
    • Mayer, M.1    Meyer, B.2
  • 27
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • Mayer M, Meyer B. 2001. Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J Am Chem Soc. 123:6108-6117.
    • (2001) J Am Chem Soc , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 28
    • 34547584538 scopus 로고    scopus 로고
    • Rational optimization of the binding affinity of CD4 targeting peptidomimetics with potential anti HIV activity
    • Neffe AT, Bilang M, Grüneberg I, Meyer B. 2007. Rational optimization of the binding affinity of CD4 targeting peptidomimetics with potential anti HIV activity. J Med Chem. 50:3482-3488.
    • (2007) J Med Chem , vol.50 , pp. 3482-3488
    • Neffe, A.T.1    Bilang, M.2    Grüneberg, I.3    Meyer, B.4
  • 30
    • 84916887461 scopus 로고    scopus 로고
    • Allostery without a conformational change? Revisiting the paradigm
    • Nussinov R, Tsai CJ. 2015. Allostery without a conformational change? Revisiting the paradigm. Curr Opin Struct Biol. 30:17-24.
    • (2015) Curr Opin Struct Biol , vol.30 , pp. 17-24
    • Nussinov, R.1    Tsai, C.J.2
  • 32
    • 84858168537 scopus 로고    scopus 로고
    • Rossmann GM, Rao BV editors., Viral Molecular Machines Boston, MA, Springer US
    • Prasad BVV, Schmid MF. 2012. Principles of virus structural organization. In: Rossmann GM, Rao BV editors., Viral Molecular Machines Boston, MA, Springer US. p. 17-47.
    • (2012) Principles of Virus Structural Organization , pp. 17-47
    • Bvv, P.1    Schmid, M.F.2
  • 34
    • 41449101560 scopus 로고    scopus 로고
    • NMR experiments reveal the molecular basis of receptor recognition by a calicivirus
    • Rademacher C, Krishna NR, Palcic M, Parra F, Peters T. 2008. NMR experiments reveal the molecular basis of receptor recognition by a calicivirus. J Am Chem Soc. 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
  • 35
    • 70049086227 scopus 로고    scopus 로고
    • Molecular recognition of ligands by native viruses and virus-like particles as studied by NMR experiments
    • Peters T editor, Springer
    • Rademacher C, Peters T. 2008. Molecular recognition of ligands by native viruses and virus-like particles as studied by NMR experiments. In: Peters T editor., Topics in Current Chemistry, Bioactive Conformation II Berlin Heidelberg, Springer. p. 183-202.
    • (2008) Topics in Current Chemistry, Bioactive Conformation II Berlin Heidelberg , pp. 183-202
    • Rademacher, C.1    Peters, T.2
  • 36
    • 84969562012 scopus 로고    scopus 로고
    • A chemical perspective on allostery
    • Ribeiro AA, Ortiz V. 2016. A chemical perspective on allostery. Chem Rev. 116:6488-6502.
    • (2016) Chem Rev , vol.116 , pp. 6488-6502
    • Ribeiro, A.A.1    Ortiz, V.2
  • 37
    • 80052288988 scopus 로고    scopus 로고
    • Structural analysis of histo-blood group antigen binding specificity in a norovirus GII.4 epidemic variant: Implications for epochal evolution
    • Shanker S, Choi JM, Sankaran B, Atmar RL, Estes MK, Prasad BV. 2011. Structural analysis of histo-blood group antigen binding specificity in a norovirus GII.4 epidemic variant: Implications for epochal evolution. J Virol. 85:8635-8645.
    • (2011) J Virol , vol.85 , pp. 8635-8645
    • Shanker, S.1    Choi, J.M.2    Sankaran, B.3    Atmar, R.L.4    Estes, M.K.5    Prasad, B.V.6
  • 38
    • 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
  • 39
    • 20344400111 scopus 로고    scopus 로고
    • Norovirus and its histo-blood group antigen receptors: An answer to a historical puzzle
    • Tan M, Jiang X. 2005. 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
  • 40
    • 64249140044 scopus 로고    scopus 로고
    • Conservation of carbohydrate binding interfaces: Evidence of human HBGA selection in norovirus evolution
    • Tan M, Xia M, Chen Y, Bu W, Hegde RS, Meller J, Li X, Jiang X. 2009. Conservation of carbohydrate binding interfaces: Evidence of human HBGA selection in norovirus evolution. PLoS One. 4:e5058.
    • (2009) PLoS One , vol.4 , pp. e5058
    • Tan, M.1    Xia, M.2    Chen, Y.3    Bu, W.4    Hegde, R.S.5    Meller, J.6    Li, X.7    Jiang, X.8
  • 42
    • 4544338141 scopus 로고    scopus 로고
    • Improving baculovirus recombination
    • Zhao Y, Chapman DAG, Jones IM. 2003. Improving baculovirus recombination. Nucleic Acids Res. 31:6e-6.
    • (2003) Nucleic Acids Res , vol.31 , pp. 6e
    • Zhao, Y.1    Dag, C.2    Jones, I.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.