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Volumn 83, Issue 2, 2009, Pages 673-686

An arginine switch in the species B adenovirus knob determines high-affinity engagement of cellular receptor CD46

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; MEMBRANE COFACTOR PROTEIN;

EID: 58149517673     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01967-08     Document Type: Article
Times cited : (46)

References (55)
  • 1
    • 0031105386 scopus 로고    scopus 로고
    • Immunoassay reagents for thyroid testing. 2. Binding properties and energetic parameters of a T4 monoclonal antibody and its Fab fragment with a library of thyroxine analog biosensors using surface plasmon resonance
    • Adamczyk, M., J. C. Gebler, A. H. Gunasekera, P. G. Mattingly, and Y. Pan. 1997. Immunoassay reagents for thyroid testing. 2. Binding properties and energetic parameters of a T4 monoclonal antibody and its Fab fragment with a library of thyroxine analog biosensors using surface plasmon resonance. Bioconjug. Chem. 8:133-145.
    • (1997) Bioconjug. Chem , vol.8 , pp. 133-145
    • Adamczyk, M.1    Gebler, J.C.2    Gunasekera, A.H.3    Mattingly, P.G.4    Pan, Y.5
  • 2
    • 0034426623 scopus 로고    scopus 로고
    • Application of surface plasmon resonance toward studies of low-molecular-weight antigen-antibody binding interactions
    • Adamczyk, M., J. A. Moore, and Z. Yu. 2000. Application of surface plasmon resonance toward studies of low-molecular-weight antigen-antibody binding interactions. Methods 20:319-328.
    • (2000) Methods , vol.20 , pp. 319-328
    • Adamczyk, M.1    Moore, J.A.2    Yu, Z.3
  • 3
    • 34447539077 scopus 로고    scopus 로고
    • Adenoviridae: The viruses and their replication
    • D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus ed, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • Berk, A. J. 2007. Adenoviridae: the viruses and their replication, p. 2301-2326. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields virology , pp. 2301-2326
    • Berk, A.J.1
  • 4
    • 84890021933 scopus 로고
    • The calculation of small molecular interactions by the differences of separate total energies. Some procedures with reduced errors
    • Boys, S., and F. Bernardi. 1970. The calculation of small molecular interactions by the differences of separate total energies. Some procedures with reduced errors. Mol. Phys. 19:440-467.
    • (1970) Mol. Phys , vol.19 , pp. 440-467
    • Boys, S.1    Bernardi, F.2
  • 5
    • 29244487908 scopus 로고    scopus 로고
    • Oligomeric protein structure networks: Insights into protein-protein interactions
    • Brinda, K. V., and S. Vishveshwara. 2005. Oligomeric protein structure networks: insights into protein-protein interactions. BMC Bioinform. 6:296.
    • (2005) BMC Bioinform , vol.6 , pp. 296
    • Brinda, K.V.1    Vishveshwara, S.2
  • 6
    • 37049014272 scopus 로고    scopus 로고
    • Brunger, A. T. 2007. Version 1.2 of the Crystallography and NMR System. Nat. Protoc. 2:2728-2733
    • Brunger, A. T. 2007. Version 1.2 of the Crystallography and NMR System. Nat. Protoc. 2:2728-2733.
  • 8
    • 0022450133 scopus 로고
    • Amino-aromatic interactions in proteins
    • Burley, S. K., and G. A. Petsko. 1986. Amino-aromatic interactions in proteins. FEBS Lett. 203:139-143.
    • (1986) FEBS Lett , vol.203 , pp. 139-143
    • Burley, S.K.1    Petsko, G.A.2
  • 9
    • 0033151839 scopus 로고    scopus 로고
    • Crystal structure of two CD46 domains reveals an extended measles virus-binding surface
    • Casasnovas, J. M., M. Larvie, and T. Stehle. 1999. Crystal structure of two CD46 domains reveals an extended measles virus-binding surface. EMBO J. 18:2911-2922.
    • (1999) EMBO J , vol.18 , pp. 2911-2922
    • Casasnovas, J.M.1    Larvie, M.2    Stehle, T.3
  • 10
    • 4644364097 scopus 로고    scopus 로고
    • Four viruses, two bacteria, and one receptor: Membrane cofactor protein (CD46) as pathogens' magnet
    • Cattaneo, R. 2004. Four viruses, two bacteria, and one receptor: membrane cofactor protein (CD46) as pathogens' magnet. J. Virol. 78:4385-4388.
    • (2004) J. Virol , vol.78 , pp. 4385-4388
    • Cattaneo, R.1
  • 11
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computing Project No. 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50:760-763.
    • Collaborative Computing Project No. 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50:760-763.
  • 12
    • 33748325882 scopus 로고    scopus 로고
    • Drug-target residence time and its implications for lead optimization
    • Copeland, R. A., D. L. Pompliano, and T. D. Meek. 2006. Drug-target residence time and its implications for lead optimization. Nat. Rev. Drug Discov. 5:730-739.
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 730-739
    • Copeland, R.A.1    Pompliano, D.L.2    Meek, T.D.3
  • 13
    • 16344389701 scopus 로고    scopus 로고
    • Cation-pi interactions in proteinprotein interfaces
    • Crowley, P. B., and A. Golovin. 2005. Cation-pi interactions in proteinprotein interfaces. Proteins 59:231-239.
    • (2005) Proteins , vol.59 , pp. 231-239
    • Crowley, P.B.1    Golovin, A.2
  • 15
    • 0031285825 scopus 로고    scopus 로고
    • Auxiliary basis sets for main row atoms and transition metals and their use to approximate Coulomb potentials
    • Eichkorn, K., F. Weigend, O. Treutler, and R. Ahlrichs. 1997. Auxiliary basis sets for main row atoms and transition metals and their use to approximate Coulomb potentials. Theor. Chem. Acc. 97:119-124.
    • (1997) Theor. Chem. Acc , vol.97 , pp. 119-124
    • Eichkorn, K.1    Weigend, F.2    Treutler, O.3    Ahlrichs, R.4
  • 16
    • 20344381993 scopus 로고
    • Use of approximate integrals in ab initio theory. An application in MP2 energy calculation
    • Feyereisen, M., G. Fitzgerald, and A. Komornicki. 1993. Use of approximate integrals in ab initio theory. An application in MP2 energy calculation. Chem. Phys. Lett. 208:359-363.
    • (1993) Chem. Phys. Lett , vol.208 , pp. 359-363
    • Feyereisen, M.1    Fitzgerald, G.2    Komornicki, A.3
  • 17
    • 36248954498 scopus 로고    scopus 로고
    • Species B adenovirus serotypes 3, 7, 11 and 35 share similar binding sites on the membrane cofactor protein CD46 receptor
    • Fleischli, C., D. Sirena, G. Lesage, M. J. Havenga, R. Cattaneo, U. F. Greber, and S. Hemmi. 2007. Species B adenovirus serotypes 3, 7, 11 and 35 share similar binding sites on the membrane cofactor protein CD46 receptor. J. Gen. Virol. 88:2925-2934.
    • (2007) J. Gen. Virol , vol.88 , pp. 2925-2934
    • Fleischli, C.1    Sirena, D.2    Lesage, G.3    Havenga, M.J.4    Cattaneo, R.5    Greber, U.F.6    Hemmi, S.7
  • 18
    • 22544446465 scopus 로고    scopus 로고
    • The distal short consensus repeats 1 and 2 of the membrane cofactor protein CD46 and their distance from the cell membrane determine productive entry of species B adenovirus serotype 35
    • Fleischli, C., S. Verhaagh, M. Havenga, D. Sirena, W. Schaffner, R. Cattaneo, U. F. Greber, and S. Hemmi. 2005. The distal short consensus repeats 1 and 2 of the membrane cofactor protein CD46 and their distance from the cell membrane determine productive entry of species B adenovirus serotype 35. J. Virol. 79:10013-10022.
    • (2005) J. Virol , vol.79 , pp. 10013-10022
    • Fleischli, C.1    Verhaagh, S.2    Havenga, M.3    Sirena, D.4    Schaffner, W.5    Cattaneo, R.6    Greber, U.F.7    Hemmi, S.8
  • 19
    • 0028153795 scopus 로고
    • Planar stacking interactions of arginine and aromatic side-chains in proteins
    • Flocco, M. M., and S. L. Mowbray. 1994. Planar stacking interactions of arginine and aromatic side-chains in proteins. J. Mol. Biol. 235:709-717.
    • (1994) J. Mol. Biol , vol.235 , pp. 709-717
    • Flocco, M.M.1    Mowbray, S.L.2
  • 20
    • 0345708273 scopus 로고    scopus 로고
    • CD46 is a cellular receptor for group B adenoviruses
    • Gaggar, A., D. M. Shayakhmetov, and A. Lieber. 2003. CD46 is a cellular receptor for group B adenoviruses. Nat. Med. 9:1408-1412.
    • (2003) Nat. Med , vol.9 , pp. 1408-1412
    • Gaggar, A.1    Shayakhmetov, D.M.2    Lieber, A.3
  • 21
    • 32444436230 scopus 로고    scopus 로고
    • The Arg279Gln substitution in the adenovirus type 11p (Ad11p) fiber knob abolishes EDTA-resistant binding to A549 and CHO-CD46 cells, converting the phenotype to that of Ad7p
    • Gustafsson, D. J., A. Segerman, K. Lindman, Y. F. Mei, and G. Wadell. 2006. The Arg279Gln substitution in the adenovirus type 11p (Ad11p) fiber knob abolishes EDTA-resistant binding to A549 and CHO-CD46 cells, converting the phenotype to that of Ad7p. J. Virol. 80:1897-1905.
    • (2006) J. Virol , vol.80 , pp. 1897-1905
    • Gustafsson, D.J.1    Segerman, A.2    Lindman, K.3    Mei, Y.F.4    Wadell, G.5
  • 22
    • 33846386076 scopus 로고    scopus 로고
    • Multivalent sialic acid conjugates inhibit adenovirus type 37 from binding to and infecting human corneal epithelial cells
    • Johansson, S. M., E. C. Nilsson, M. Elofsson, N. Ahlskog, J. Kihlberg, and N. Arnberg. 2007. Multivalent sialic acid conjugates inhibit adenovirus type 37 from binding to and infecting human corneal epithelial cells. Antivir. Res. 73:92-100.
    • (2007) Antivir. Res , vol.73 , pp. 92-100
    • Johansson, S.M.1    Nilsson, E.C.2    Elofsson, M.3    Ahlskog, N.4    Kihlberg, J.5    Arnberg, N.6
  • 23
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. 1993. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26:795-800.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 24
    • 0038029587 scopus 로고    scopus 로고
    • The impact of adenovirus infection on the immunocompromised host
    • Kojaoghlanian, T., P. Flomenberg, and M. S. Horwitz. 2003. The impact of adenovirus infection on the immunocompromised host. Rev. Med. Virol. 13:155-171.
    • (2003) Rev. Med. Virol , vol.13 , pp. 155-171
    • Kojaoghlanian, T.1    Flomenberg, P.2    Horwitz, M.S.3
  • 28
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., A. A. Vagin, and E. J. Dodson. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D. 53:240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 29
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. 1994. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50:157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 30
    • 0030039913 scopus 로고    scopus 로고
    • Competition BIAcore for measuring true affinities: Large differences from values determined from binding kinetics
    • Nieba, L., A. Krebber, and A. Pluckthun. 1996. Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics. Anal. Biochem. 234:155-165.
    • (1996) Anal. Biochem , vol.234 , pp. 155-165
    • Nieba, L.1    Krebber, A.2    Pluckthun, A.3
  • 31
    • 17444407490 scopus 로고    scopus 로고
    • Kinetic studies of small molecule interactions with protein kinases using biosensor technology
    • Nordin, H., M. Jungnelius, R. Karlsson, and O. P. Karlsson. 2005. Kinetic studies of small molecule interactions with protein kinases using biosensor technology. Anal. Biochem. 340:359-368.
    • (2005) Anal. Biochem , vol.340 , pp. 359-368
    • Nordin, H.1    Jungnelius, M.2    Karlsson, R.3    Karlsson, O.P.4
  • 33
    • 0000491367 scopus 로고    scopus 로고
    • Linear scaling exchange gradients for Hartree-Fock and hybrid density funtional theory
    • Ochsenfeld, C. 2000. Linear scaling exchange gradients for Hartree-Fock and hybrid density funtional theory. Chem. Phys. Lett. 327:216-223.
    • (2000) Chem. Phys. Lett , vol.327 , pp. 216-223
    • Ochsenfeld, C.1
  • 34
    • 0000247202 scopus 로고    scopus 로고
    • Linear and sub-linear scaling formation of Hartree-Fock-type exchange matrices
    • Ochsenfeld, C., C. A. White, and M. J. Head-Gordon. 1998. Linear and sub-linear scaling formation of Hartree-Fock-type exchange matrices. J. Chem. Phys. 109:1663-1669.
    • (1998) J. Chem. Phys , vol.109 , pp. 1663-1669
    • Ochsenfeld, C.1    White, C.A.2    Head-Gordon, M.J.3
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 49149093468 scopus 로고    scopus 로고
    • Structural variations in species B adenovirus fibers impact CD46 association
    • Pache, L., S. Venkataraman, V. S. Reddy, and G. R. Nemerow. 2008. Structural variations in species B adenovirus fibers impact CD46 association. J. Virol. 82:7923-7931.
    • (2008) J. Virol , vol.82 , pp. 7923-7931
    • Pache, L.1    Venkataraman, S.2    Reddy, V.S.3    Nemerow, G.R.4
  • 38
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R. 2001. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. D 57:1373-1382.
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1373-1382
    • Read, R.1
  • 39
    • 33845931650 scopus 로고    scopus 로고
    • Survey of the year 2005 commercial optical biosensor literature
    • Rich, R. L., and D. G. Myszka. 2006. Survey of the year 2005 commercial optical biosensor literature. J. Mol. Recognit. 19:478-534.
    • (2006) J. Mol. Recognit , vol.19 , pp. 478-534
    • Rich, R.L.1    Myszka, D.G.2
  • 40
    • 26344435738 scopus 로고
    • Fully optimized contracted Gaussian basis sets for atoms Li to Kr
    • Schäfer, A., H. Horn, and R. Ahlrichs. 1992. Fully optimized contracted Gaussian basis sets for atoms Li to Kr. J. Chem. Phys. 97:2571-2577.
    • (1992) J. Chem. Phys , vol.97 , pp. 2571-2577
    • Schäfer, A.1    Horn, H.2    Ahlrichs, R.3
  • 41
    • 58149491860 scopus 로고    scopus 로고
    • Schrödinger, Inc. 2005. Maestro 7.5. Schrödinger Inc., Portland, OR.
    • Schrödinger, Inc. 2005. Maestro 7.5. Schrödinger Inc., Portland, OR.
  • 42
    • 0030795295 scopus 로고    scopus 로고
    • Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors
    • Schuck, P. 1997. Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors. Curr. Opin. Biotechnol. 8:498-502.
    • (1997) Curr. Opin. Biotechnol , vol.8 , pp. 498-502
    • Schuck, P.1
  • 43
    • 0037227549 scopus 로고    scopus 로고
    • There are two different species B adenovirus receptors: SBAR, common to species B1 and B2 adenoviruses, and sB2AR, exclusively used by species B2 adenoviruses
    • Segerman, A., N. Arnberg, A. Erikson, K. Lindman, and G. Wadell. 2003. There are two different species B adenovirus receptors: sBAR, common to species B1 and B2 adenoviruses, and sB2AR, exclusively used by species B2 adenoviruses. J. Virol. 77:1157-1162.
    • (2003) J. Virol , vol.77 , pp. 1157-1162
    • Segerman, A.1    Arnberg, N.2    Erikson, A.3    Lindman, K.4    Wadell, G.5
  • 45
    • 0033923367 scopus 로고    scopus 로고
    • Rational design of faster associating and tighter binding protein complexes
    • Selzer, T., S. Albeck, and G. Schreiber. 2000. Rational design of faster associating and tighter binding protein complexes. Nat. Struct. Biol. 7:537-541.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 537-541
    • Selzer, T.1    Albeck, S.2    Schreiber, G.3
  • 46
    • 0035870738 scopus 로고    scopus 로고
    • Efficient evaluation of the Coulomb force in density-functional theory calculations
    • Shao, Y., C. A. White, and M. Head-Gordon. 2001. Efficient evaluation of the Coulomb force in density-functional theory calculations. J. Chem. Phys. 114:6572-6577.
    • (2001) J. Chem. Phys , vol.114 , pp. 6572-6577
    • Shao, Y.1    White, C.A.2    Head-Gordon, M.3
  • 47
    • 0027209602 scopus 로고    scopus 로고
    • Sinning, I., G. J. Kleywegt, S. W. Cowan, P. Reinemer, H. W. Dirr, R. Huber, G. L. Gilliland, R. N. Armstrong, X. Ji, P. G. Board, et al. 1993. Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. J. Mol. Biol. 232:192-212.
    • Sinning, I., G. J. Kleywegt, S. W. Cowan, P. Reinemer, H. W. Dirr, R. Huber, G. L. Gilliland, R. N. Armstrong, X. Ji, P. G. Board, et al. 1993. Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. J. Mol. Biol. 232:192-212.
  • 48
    • 0024559003 scopus 로고
    • Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity
    • Stanley, P. 1989. Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity. Mol. Cell. Biol. 9:377-383.
    • (1989) Mol. Cell. Biol , vol.9 , pp. 377-383
    • Stanley, P.1
  • 53
    • 0025695273 scopus 로고
    • General analysis of receptor-mediated viral attachment to cell surfaces
    • Wickham, T. J., R. R. Granados, H. A. Wood, D. A. Hammer, and M. L. Shuler. 1990. General analysis of receptor-mediated viral attachment to cell surfaces. Biophys. J. 58:1501-1516.
    • (1990) Biophys. J , vol.58 , pp. 1501-1516
    • Wickham, T.J.1    Granados, R.R.2    Wood, H.A.3    Hammer, D.A.4    Shuler, M.L.5
  • 54
    • 0027166647 scopus 로고
    • Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment
    • Wickham, T. J., P. Mathias, D. A. Cheresh, and G. R. Nemerow. 1993. Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment. Cell 73:309-319.
    • (1993) Cell , vol.73 , pp. 309-319
    • Wickham, T.J.1    Mathias, P.2    Cheresh, D.A.3    Nemerow, G.R.4
  • 55
    • 0035943656 scopus 로고    scopus 로고
    • Affinity, kinetics, and thermodynamics of E-selectin binding to E-selectin ligand-1
    • Wild, M. K., M. C. Huang, U. Schulze-Horsel, P. A. van der Merwe, and D. Vestweber. 2001. Affinity, kinetics, and thermodynamics of E-selectin binding to E-selectin ligand-1. J. Biol. Chem. 276:31602-31612.
    • (2001) J. Biol. Chem , vol.276 , pp. 31602-31612
    • Wild, M.K.1    Huang, M.C.2    Schulze-Horsel, U.3    van der Merwe, P.A.4    Vestweber, D.5


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