메뉴 건너뛰기




Volumn 71, Issue 11, 1997, Pages 8357-8361

Arginine-glycine-aspartic acid-specific binding by foot-and-mouth disease viruses to the purified integrin αvβ3 in vitro

Author keywords

[No Author keywords available]

Indexed keywords

HEPARAN SULFATE; INTEGRIN;

EID: 0030764776     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.11.8357-8361.1997     Document Type: Article
Times cited : (138)

References (49)
  • 1
    • 0024578406 scopus 로고
    • The three-dimensional structure of foot-and-mouth disease virus at 2.9Å resolution
    • Acharya, R., E. Fry, D. Stuart, G. Fox, D. Rowlands, and F. Brown. 1989. The three-dimensional structure of foot-and-mouth disease virus at 2.9Å resolution. Nature 337:709-716.
    • (1989) Nature , vol.337 , pp. 709-716
    • Acharya, R.1    Fry, E.2    Stuart, D.3    Fox, G.4    Rowlands, D.5    Brown, F.6
  • 2
    • 0025186332 scopus 로고
    • The effect of peptides containing the arginine-glycine-aspartic acid sequence on the adsorption of foot-and-mouth disease virus to tissue culture cells
    • Baxt, B., and Y. Becker. 1990. The effect of peptides containing the arginine-glycine-aspartic acid sequence on the adsorption of foot-and-mouth disease virus to tissue culture cells. Virus Genes 4:73-83.
    • (1990) Virus Genes , vol.4 , pp. 73-83
    • Baxt, B.1    Becker, Y.2
  • 3
    • 0027520635 scopus 로고
    • Distinctive features of foot-and-mouth disease virus, a member of the picornavirus family: Aspects of virus protein synthesis, protein processing and structure
    • Belsham, G. J. 1993. Distinctive features of foot-and-mouth disease virus, a member of the picornavirus family: aspects of virus protein synthesis, protein processing and structure. Prog. Biophys. Mol. Biol. 69:241-260.
    • (1993) Prog. Biophys. Mol. Biol. , vol.69 , pp. 241-260
    • Belsham, G.J.1
  • 4
    • 0026580865 scopus 로고
    • Identification of the integrin VLA-2 as a receptor for echo-virus 1
    • Bergelson, J. M., M. P. Shepley, B. M. C. Chan, M. E. Helmer, and R. W. Finberg. 1992. Identification of the integrin VLA-2 as a receptor for echo-virus 1. Science 255:1718-1720.
    • (1992) Science , vol.255 , pp. 1718-1720
    • Bergelson, J.M.1    Shepley, M.P.2    Chan, B.M.C.3    Helmer, M.E.4    Finberg, R.W.5
  • 6
    • 0028904534 scopus 로고
    • Antibodies to the vitronectin receptor (integrin αvβ3) inhibit binding and infection of foot-and-mouth disease virus to cultured cells
    • Berinstein, A., M. Roivainen, T. Hovi, P. W. Mason, and B. Baxt. 1995. Antibodies to the vitronectin receptor (integrin αvβ3) inhibit binding and infection of foot-and-mouth disease virus to cultured cells. J. Virol. 69:2664-2666.
    • (1995) J. Virol. , vol.69 , pp. 2664-2666
    • Berinstein, A.1    Roivainen, M.2    Hovi, T.3    Mason, P.W.4    Baxt, B.5
  • 8
    • 0015875928 scopus 로고
    • Haemagglutination by type SAT-2 FMDV's
    • Bootly, J. C., and T. W. F. Pay. 1973. Haemagglutination by type SAT-2 FMDV's. J. Gen. Virol. 19:397-404.
    • (1973) J. Gen. Virol. , vol.19 , pp. 397-404
    • Bootly, J.C.1    Pay, T.W.F.2
  • 9
    • 0021140938 scopus 로고
    • Effect of lysosomotropic agents on the foot-and-mouth disease virus replication
    • Carrillo, E. C., C. Giachetti, and R. H. Campos. 1984. Effect of lysosomotropic agents on the foot-and-mouth disease virus replication. Virology 135: 542-545.
    • (1984) Virology , vol.135 , pp. 542-545
    • Carrillo, E.C.1    Giachetti, C.2    Campos, R.H.3
  • 10
    • 1842275505 scopus 로고    scopus 로고
    • Unpublished data
    • Clarke, B. E. Unpublished data.
    • Clarke, B.E.1
  • 12
    • 0030272735 scopus 로고    scopus 로고
    • Integrin cytoplasmic interactions and bidirectional transmembrane signalling
    • Dedhar, S., and G. E. Hannigan. 1996. Integrin cytoplasmic interactions and bidirectional transmembrane signalling. Curr. Opin. Cell Biol. 8:657-669.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 657-669
    • Dedhar, S.1    Hannigan, G.E.2
  • 13
    • 0028446566 scopus 로고
    • The dynamic regulation of integrin adhesiveness
    • Diamond, M. S., and T. A. Springer. 1994. The dynamic regulation of integrin adhesiveness. Curr. Biol. 4:506-517.
    • (1994) Curr. Biol. , vol.4 , pp. 506-517
    • Diamond, M.S.1    Springer, T.A.2
  • 14
    • 0026601096 scopus 로고
    • Divalent cation regulation of the function of the leukocyte integrin LFA-1
    • Dransfield, I., C. Cabañas, A. Craig, and N. Hogg. 1992. Divalent cation regulation of the function of the leukocyte integrin LFA-1. J. Cell Biol. 116:219-226.
    • (1992) J. Cell Biol. , vol.116 , pp. 219-226
    • Dransfield, I.1    Cabañas, C.2    Craig, A.3    Hogg, N.4
  • 15
    • 0030614485 scopus 로고    scopus 로고
    • Identification of the α6 integrin as a candidate receptor for papillomaviruses
    • Evander, M., I. H. Frazer, E. Payne, Y. M. Qi, K. Hengst, and N. A. McMillan. 1997. Identification of the α6 integrin as a candidate receptor for papillomaviruses. J. Virol. 71:2449-2456.
    • (1997) J. Virol. , vol.71 , pp. 2449-2456
    • Evander, M.1    Frazer, I.H.2    Payne, E.3    Qi, Y.M.4    Hengst, K.5    McMillan, N.A.6
  • 17
    • 0021769942 scopus 로고
    • Nucleotide sequence and genomic organisation of foot-and-mouth disease virus
    • Forss, S., K. Beck, and H. Schaller. 1984. Nucleotide sequence and genomic organisation of foot-and-mouth disease virus. Nucleic Acids Res. 12:6587-6601.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 6587-6601
    • Forss, S.1    Beck, K.2    Schaller, H.3
  • 18
    • 0024639043 scopus 로고
    • The cell attachment site on foot-and-mouth disease viruses includes the amino acid sequence RGD (arginine-glycine-aspartic acid)
    • Fox, G., N. R. Parry, P. V. Barnet, B. McGinn, D. J. Rowlands, and F. Brown. 1989. The cell attachment site on foot-and-mouth disease viruses includes the amino acid sequence RGD (arginine-glycine-aspartic acid). J. Gen. Virol. 70:625-637.
    • (1989) J. Gen. Virol. , vol.70 , pp. 625-637
    • Fox, G.1    Parry, N.R.2    Barnet, P.V.3    McGinn, B.4    Rowlands, D.J.5    Brown, F.6
  • 19
    • 0342982319 scopus 로고    scopus 로고
    • Antibody and host cell recognition of foot-and-mouth disease virus (serotype C) cleaved at the Arg-Gly-Asp (RGD) motif: A structural interpretation
    • Hernández, J., M. Luz Valero, D. Andreu, E. Domingo, and M. G. Mateu. 1996. Antibody and host cell recognition of foot-and-mouth disease virus (serotype C) cleaved at the Arg-Gly-Asp (RGD) motif: a structural interpretation. J. Gen. Virol. 77:257-264.
    • (1996) J. Gen. Virol. , vol.77 , pp. 257-264
    • Hernández, J.1    Luz Valero, M.2    Andreu, D.3    Domingo, E.4    Mateu, M.G.5
  • 20
    • 0028986791 scopus 로고
    • 2+ suppresses cell adhesion to osteopontin by attenuating binding affinity for integrin αvβ3
    • 2+ suppresses cell adhesion to osteopontin by attenuating binding affinity for integrin αvβ3. J. Biol. Chem. 270:9917-9925.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9917-9925
    • Hu, D.D.1    Hoyer, J.R.2    Smith, J.W.3
  • 21
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signalling in cell adhesion
    • Hynes, R. O. 1992. Integrins: versatility, modulation, and signalling in cell adhesion. Cell 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 23
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellén, L., and U. Lindahl. 1991. Proteoglycans: structures and interactions. Annu. Rev. Biochem. 60:443-475.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellén, L.1    Lindahl, U.2
  • 25
    • 0031048045 scopus 로고    scopus 로고
    • Molecular determinants of Arg-Gly-Asp ligand specificity for 3 integrins
    • Kunicki, T. J., D. S. Annis, and B. Felding-Habermann. 1997. Molecular determinants of Arg-Gly-Asp ligand specificity for 3 integrins. J. Biol. Chem. 272:4103-4107.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4103-4107
    • Kunicki, T.J.1    Annis, D.S.2    Felding-Habermann, B.3
  • 26
    • 0029646107 scopus 로고
    • Two conformations of the integrin A-domain (I-domain): A pathway for activation?
    • Lee, J.-O., L. A. Bankston, M. A. Arnaout, and R. C. Liddington. 1995. Two conformations of the integrin A-domain (I-domain): a pathway for activation? Structure 3:1333-1340.
    • (1995) Structure , vol.3 , pp. 1333-1340
    • Lee, J.-O.1    Bankston, L.A.2    Arnaout, M.A.3    Liddington, R.C.4
  • 27
    • 0030614463 scopus 로고    scopus 로고
    • Point mutations within the βG-βH loop of foot-and-mouth disease virus O1K affects attachment to target cells
    • Leippert, M., E. Beck, F. Weiland, and E. Pfaff. 1997. Point mutations within the βG-βH loop of foot-and-mouth disease virus O1K affects attachment to target cells. J. Virol. 71:1046-1051.
    • (1997) J. Virol. , vol.71 , pp. 1046-1051
    • Leippert, M.1    Beck, E.2    Weiland, F.3    Pfaff, E.4
  • 28
    • 0027257937 scopus 로고
    • Antibody-complexed foot-and-mouth disease virus, but not poliovirus, can infect normally insusceptible cells via the Fc receptor
    • Mason, P. W., B. Baxt, F. Brown, J. Harber, A. Murdin, and E. Wimmer. 1993. Antibody-complexed foot-and-mouth disease virus, but not poliovirus, can infect normally insusceptible cells via the Fc receptor. Virology 192:568-577.
    • (1993) Virology , vol.192 , pp. 568-577
    • Mason, P.W.1    Baxt, B.2    Brown, F.3    Harber, J.4    Murdin, A.5    Wimmer, E.6
  • 29
    • 0028201747 scopus 로고
    • RGD sequence of foot-and-mouth disease virus is essential for infecting cells via the natural receptor but can be bypassed by an antibody-dependant enhancement pathway
    • Mason, P. W., E. Reider, and B. Baxt. 1994. RGD sequence of foot-and-mouth disease virus is essential for infecting cells via the natural receptor but can be bypassed by an antibody-dependant enhancement pathway. Proc. Natl. Acad. Sci. USA 91:1932-1936.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1932-1936
    • Mason, P.W.1    Reider, E.2    Baxt, B.3
  • 30
    • 0029972140 scopus 로고    scopus 로고
    • Systematic replacement of amino acid residues within an Arg-Gly-Asp-containing loop of foot-and-mouth disease virus and effects on cell recognition
    • Mateu, M. G., M Luz Valero, D. Andreu, and E. Domingo. 1996. Systematic replacement of amino acid residues within an Arg-Gly-Asp-containing loop of foot-and-mouth disease virus and effects on cell recognition. J. Biol. Chem. 271:12814-12819.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12814-12819
    • Mateu, M.G.1    Luz Valero, M.2    Andreu, D.3    Domingo, E.4
  • 32
    • 0028970566 scopus 로고
    • Regulation of Integrin αβ1-Fibronectin Interactions by Divalent Cations
    • Mould, A. P., S. K. Akiyama, and M. J. Humphries. 1995. Regulation of Integrin αβ1-Fibronectin Interactions by Divalent Cations. J. Biol. Chem. 270:26270-26277.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26270-26277
    • Mould, A.P.1    Akiyama, S.K.2    Humphries, M.J.3
  • 33
    • 0026038885 scopus 로고
    • Arginine-glycine-aspartic acid binding leading to molecular stabilization between integrin αvβ3 and its ligand
    • Orlando, R. A., and D. A. Cheresh. 1991. Arginine-glycine-aspartic acid binding leading to molecular stabilization between integrin αvβ3 and its ligand. J. Biol. Chem. 266:19543-19550.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19543-19550
    • Orlando, R.A.1    Cheresh, D.A.2
  • 34
    • 0027997413 scopus 로고
    • Selective recognition of cyclic RGD peptides of NMR defined conformation by αIIbβ3, αvβ3, and α5β1 integrins
    • Pfaff, M., K. Tangemann, B. Müller, M. Gurrath, G. Müller, H. Kessler, R. Timpl, and J. Engels. 1994. Selective recognition of cyclic RGD peptides of NMR defined conformation by αIIbβ3, αvβ3, and α5β1 integrins. J. Biol. Chem. 269:20233-20238.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20233-20238
    • Pfaff, M.1    Tangemann, K.2    Müller, B.3    Gurrath, M.4    Müller, G.5    Kessler, H.6    Timpl, R.7    Engels, J.8
  • 36
    • 0028229640 scopus 로고
    • Animal-derived antigenic variants of foot-and-mouth disease virus type A12 have low affinity for cells in culture
    • Rieder, E., B. Baxt, and P. W. Mason. 1994. Animal-derived antigenic variants of foot-and-mouth disease virus type A12 have low affinity for cells in culture. J. Virol. 68:5296-5299.
    • (1994) J. Virol. , vol.68 , pp. 5296-5299
    • Rieder, E.1    Baxt, B.2    Mason, P.W.3
  • 37
    • 0028167928 scopus 로고
    • Entry of coxsackievirus A9 into host cells: Specific interactions with αvβ3 integrin, the vitronectin receptor
    • Roivainen, M., L. Piirainen, T. Hovi, I. Virtanen, T. Riikonen, J. Heino, and T. Hyypiä. 1994. Entry of coxsackievirus A9 into host cells: specific interactions with αvβ3 integrin, the vitronectin receptor. Virology 203:357-365.
    • (1994) Virology , vol.203 , pp. 357-365
    • Roivainen, M.1    Piirainen, L.2    Hovi, T.3    Virtanen, I.4    Riikonen, T.5    Heino, J.6    Hyypiä, T.7
  • 42
    • 0027979834 scopus 로고
    • A mechanism for divalent cation regulation of β3-integrins
    • Smith, J. W., R. S. Piotrowicz, and D. Mathis. 1994. A mechanism for divalent cation regulation of β3-integrins. J. Biol. Chem. 269:960-967.
    • (1994) J. Biol. Chem. , vol.269 , pp. 960-967
    • Smith, J.W.1    Piotrowicz, R.S.2    Mathis, D.3
  • 43
    • 0024839880 scopus 로고
    • Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1)
    • Sobrino, F., M. A. Martínez, C. Carrillo, and E. Beck. 1989. Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1). Virus Res. 14:273-280.
    • (1989) Virus Res. , vol.14 , pp. 273-280
    • Sobrino, F.1    Martínez, M.A.2    Carrillo, C.3    Beck, E.4
  • 44
    • 0021066747 scopus 로고
    • The attachment of the foot-and-mouth disease virus Asia-1 Iran 1/73 to BHK suspension cells does not require virus specific cell receptors
    • Spier, R. E., A. Murdin, and C. J. Whittle. 1983. The attachment of the foot-and-mouth disease virus Asia-1 Iran 1/73 to BHK suspension cells does not require virus specific cell receptors. Arch. Virol. 77:97-108.
    • (1983) Arch. Virol. , vol.77 , pp. 97-108
    • Spier, R.E.1    Murdin, A.2    Whittle, C.J.3
  • 45
    • 0027984227 scopus 로고
    • Molecular and biological characterisation of echovirus 22, a representative of a new picornavirus group
    • Stanway, G., N. Kalkkinen, M. Roivainen, F. Ghazi, M. Khan, M. Smyth, O. Meurman, and T. Hyypiä. 1994. Molecular and biological characterisation of echovirus 22, a representative of a new picornavirus group. J. Virol. 68:8232-8238.
    • (1994) J. Virol. , vol.68 , pp. 8232-8238
    • Stanway, G.1    Kalkkinen, N.2    Roivainen, M.3    Ghazi, F.4    Khan, M.5    Smyth, M.6    Meurman, O.7    Hyypiä, T.8
  • 46
    • 0019990849 scopus 로고
    • Location and characterisation of the antigenic protein of the FMDV immunizing protein
    • Strohmaier, K., R. Franze, and K. H. Adam. 1982. Location and characterisation of the antigenic protein of the FMDV immunizing protein. J. Gen. Virol. 59:295-306.
    • (1982) J. Gen. Virol. , vol.59 , pp. 295-306
    • Strohmaier, K.1    Franze, R.2    Adam, K.H.3
  • 47
    • 0027158079 scopus 로고
    • Bacterial internalization mediated by β1 chain integrins is determined by ligand affinity and receptor density
    • Tran Van Nhieu, G., and R. R. Isberg. 1993. Bacterial internalization mediated by β1 chain integrins is determined by ligand affinity and receptor density. EMBO. J. 12:1887-1895.
    • (1993) EMBO. J. , vol.12 , pp. 1887-1895
    • Van Tran Nhieu, G.1    Isberg, R.R.2
  • 48
    • 0027166647 scopus 로고
    • Integrins αvβ3 and αvβ5 promote adenovirus internalization but not virus attachment
    • Wickham, T. J., P. Mathias, D. A. Cheresh, and G. R. Nemerow. 1993. Integrins αvβ3 and αvβ5 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
  • 49
    • 0023259037 scopus 로고
    • Neutralization of foot-and-mouth disease virus can be mediated through any of at least three antigenic sites
    • Xie, Q-C., D. McCahon, J. R. Crowther, G. J. Belsham, and K. C. McCullough. 1987. Neutralization of foot-and-mouth disease virus can be mediated through any of at least three antigenic sites. J. Gen. Virol. 68:1637-1647.
    • (1987) J. Gen. Virol. , vol.68 , pp. 1637-1647
    • Xie, Q.-C.1    McCahon, D.2    Crowther, J.R.3    Belsham, G.J.4    McCullough, K.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.