메뉴 건너뛰기




Volumn 90, Issue 1, 2009, Pages 197-204

Integrin αVβ6 is a high-affinity receptor for coxsackievirus A9

Author keywords

[No Author keywords available]

Indexed keywords

ALPHAVBETA6 INTEGRIN; PROTEIN ANTIBODY; PROTEIN VP1; VITRONECTIN RECEPTOR; CAPSID PROTEIN; INTEGRIN; TUMOR ANTIGEN; VIRUS RECEPTOR;

EID: 59849106343     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/vir.0.004838-0     Document Type: Article
Times cited : (34)

References (28)
  • 1
    • 0021249482 scopus 로고
    • Many rhinovirus serotypes share the same cellular receptor
    • Abraham, G. & Colonno, R. J. (1984). Many rhinovirus serotypes share the same cellular receptor. J Virol 51, 340-345.
    • (1984) J Virol , vol.51 , pp. 340-345
    • Abraham, G.1    Colonno, R.J.2
  • 2
    • 33749995048 scopus 로고    scopus 로고
    • Benschop, K. S., Schinkel, J., Luken, M. E., van den Broek, P. J., Beersma, M. F., Menelik, N., van Eijk, H. W., Zaaijer, H. L., VandenBroucke-Grauls, C. M. & other authors (2006). Fourth human parechovirus serotype. Emerg Infect Dis 12, 1572-1575.
    • Benschop, K. S., Schinkel, J., Luken, M. E., van den Broek, P. J., Beersma, M. F., Menelik, N., van Eijk, H. W., Zaaijer, H. L., VandenBroucke-Grauls, C. M. & other authors (2006). Fourth human parechovirus serotype. Emerg Infect Dis 12, 1572-1575.
  • 4
    • 36249007499 scopus 로고    scopus 로고
    • Endogenous low-level expression of the coxsackievirus and adenovirus receptor enables coxsackievirus B3 infection of RD cells
    • Carson, S. D., Kim, K. S., Pirruccello, S. J., Tracy, S. & Chapman, N. M. (2007). Endogenous low-level expression of the coxsackievirus and adenovirus receptor enables coxsackievirus B3 infection of RD cells. J Gen Virol 88, 3031-3038.
    • (2007) J Gen Virol , vol.88 , pp. 3031-3038
    • Carson, S.D.1    Kim, K.S.2    Pirruccello, S.J.3    Tracy, S.4    Chapman, N.M.5
  • 5
    • 0024835345 scopus 로고
    • The nucleotide sequence of coxsackievirus A9; implications for receptor binding and enterovirus classification
    • Chang, K. H., Auvinen, P., Hyypiä, T. & Stanway, G. (1989). The nucleotide sequence of coxsackievirus A9; implications for receptor binding and enterovirus classification. J Gen Virol 70, 32693-280.
    • (1989) J Gen Virol , vol.70 , pp. 32693-33280
    • Chang, K.H.1    Auvinen, P.2    Hyypiä, T.3    Stanway, G.4
  • 6
    • 4444300136 scopus 로고    scopus 로고
    • Interactions of foot-and-mouth disease virus with soluble bovine αVβ3 and αVβ6 integrins
    • Duque, H., LaRocco, M., Golde, W. T. & Baxt, B. (2004). Interactions of foot-and-mouth disease virus with soluble bovine αVβ3 and αVβ6 integrins. J Virol 78, 9773-9781.
    • (2004) J Virol , vol.78 , pp. 9773-9781
    • Duque, H.1    LaRocco, M.2    Golde, W.T.3    Baxt, B.4
  • 7
    • 0031736246 scopus 로고    scopus 로고
    • Molecular analysis of human parechovirus type 2 (formerly echovirus 23)
    • Ghazi, F., Hughes, P. J., Hyypiä, T. & Stanway, G. (1998). Molecular analysis of human parechovirus type 2 (formerly echovirus 23). J Gen Virol 79, 2641-2650.
    • (1998) J Gen Virol , vol.79 , pp. 2641-2650
    • Ghazi, F.1    Hughes, P.J.2    Hyypiä, T.3    Stanway, G.4
  • 8
    • 0042854793 scopus 로고    scopus 로고
    • Pathogenesis of coxsackievirus A9 in mice: Role of the viral arginine-glycine-aspartic acid motif
    • Harvala, H., Kalimo, H., Stanway, G. & Hyypiä, T. (2003). Pathogenesis of coxsackievirus A9 in mice: role of the viral arginine-glycine-aspartic acid motif. J Gen Virol 84, 2375-2379.
    • (2003) J Gen Virol , vol.84 , pp. 2375-2379
    • Harvala, H.1    Kalimo, H.2    Stanway, G.3    Hyypiä, T.4
  • 9
    • 0028818268 scopus 로고
    • The coxsackievirus A9 RGD motif is not essential for virus viability
    • Hughes, P. J., Horsnell, C., Hyypiä, T. & Stanway, G. (1995). The coxsackievirus A9 RGD motif is not essential for virus viability. J Virol 69, 8035-8040.
    • (1995) J Virol , vol.69 , pp. 8035-8040
    • Hughes, P.J.1    Horsnell, C.2    Hyypiä, T.3    Stanway, G.4
  • 11
    • 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-dependent enhancement pathway
    • Mason, P. W., Rieder, E. & Baxt, B. (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-dependent enhancement pathway. Proc Natl Acad Sci U S A 91, 1932-1936.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1932-1936
    • Mason, P.W.1    Rieder, E.2    Baxt, B.3
  • 12
    • 26244449677 scopus 로고    scopus 로고
    • The αVβ6 integrin receptor for Foot-and-mouth disease virus is expressed constitutively on the epithelial cells targeted in cattle
    • Monaghan, P., Gold, S., Simpson, J., Zhang, Z., Weinreb, P. H., Violette, S. M., Alexandersen, S. & Jackson, T. (2005). The αVβ6 integrin receptor for Foot-and-mouth disease virus is expressed constitutively on the epithelial cells targeted in cattle. J Gen Virol 86, 2769-2780.
    • (2005) J Gen Virol , vol.86 , pp. 2769-2780
    • Monaghan, P.1    Gold, S.2    Simpson, J.3    Zhang, Z.4    Weinreb, P.H.5    Violette, S.M.6    Alexandersen, S.7    Jackson, T.8
  • 13
    • 2642681650 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus virulent for cattle utilizes the integrin αVβ3 as its receptor
    • Neff, S., Sá-Carvalho, D., Rieder, E., Mason, P. W., Blystone, S. D., Brown, E. J. & Baxt, B. (1998). Foot-and-mouth disease virus virulent for cattle utilizes the integrin αVβ3 as its receptor. J Virol 72, 3587-3594.
    • (1998) J Virol , vol.72 , pp. 3587-3594
    • Neff, S.1    Sá-Carvalho, D.2    Rieder, E.3    Mason, P.W.4    Blystone, S.D.5    Brown, E.J.6    Baxt, B.7
  • 14
    • 0037399855 scopus 로고    scopus 로고
    • Molecular and biological analysis of echovirus 9 strain isolated from a diabetic child
    • Paananen, A., Ylipaasto, P., Rieder, E., Hovi, T., Galama, J. & Roivainen, M. (2003). Molecular and biological analysis of echovirus 9 strain isolated from a diabetic child. J Med Virol 69, 529-537.
    • (2003) J Med Virol , vol.69 , pp. 529-537
    • Paananen, A.1    Ylipaasto, P.2    Rieder, E.3    Hovi, T.4    Galama, J.5    Roivainen, M.6
  • 15
    • 0026018224 scopus 로고
    • RGD-dependent entry of coxsackievirus A9 into host cells and its bypass after cleavage of VP1 protein by intestinal proteases
    • Roivainen, M., Hyypiä, T., Piirainen, L., Kalkkinen, N., Stanway, G. & Hovi, T. (1991). RGD-dependent entry of coxsackievirus A9 into host cells and its bypass after cleavage of VP1 protein by intestinal proteases. J Virol 65, 4735-4740.
    • (1991) J Virol , vol.65 , pp. 4735-4740
    • Roivainen, M.1    Hyypiä, T.2    Piirainen, L.3    Kalkkinen, N.4    Stanway, G.5    Hovi, T.6
  • 16
    • 0028167928 scopus 로고
    • Entry of coxsackievirus A9 into host cells: Specific interactions with αVβ3 integrin, the vitronectin receptor
    • Roivainen, M., Piirainen, L., Hovi, T., Virtanen, I., Riikonen, T., Heino, J. & Hyypiä, T. (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
  • 17
    • 0029825388 scopus 로고    scopus 로고
    • Efficient RGD-independent entry process of coxsackievirus A9
    • Roivainen, M., Piirainen, L. & Hovi, T. (1996). Efficient RGD-independent entry process of coxsackievirus A9. Arch Virol 141, 1909-1919.
    • (1996) Arch Virol , vol.141 , pp. 1909-1919
    • Roivainen, M.1    Piirainen, L.2    Hovi, T.3
  • 18
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti, E. & Pierschbacher, M. D. (1987). New perspectives in cell adhesion: RGD and integrins. Science 238, 491-497.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 19
    • 0034107811 scopus 로고    scopus 로고
    • Molecular epidemiology and evolution of coxsackievirus A9
    • Santti, J., Harvala, H., Kinnunen, L. & Hyypiä, T. (2000). Molecular epidemiology and evolution of coxsackievirus A9. J Gen Virol 81, 1361-1372.
    • (2000) J Gen Virol , vol.81 , pp. 1361-1372
    • Santti, J.1    Harvala, H.2    Kinnunen, L.3    Hyypiä, T.4
  • 20
    • 0346367067 scopus 로고    scopus 로고
    • Lipid raft microdomains: Key sites for Coxsackievirus A9 infectious cycle
    • Triantafilou, K. & Triantafilou, M. (2003). Lipid raft microdomains: key sites for Coxsackievirus A9 infectious cycle. Virology 317, 128-135.
    • (2003) Virology , vol.317 , pp. 128-135
    • Triantafilou, K.1    Triantafilou, M.2
  • 22
    • 0033784785 scopus 로고    scopus 로고
    • A 70 kDa MHC class I associated protein (MAP-70) identified as a receptor molecule for Coxsackievirus A9 cell attachment
    • Triantafilou, M., Triantafilou, K. & Wilson, K. M. (2000a). A 70 kDa MHC class I associated protein (MAP-70) identified as a receptor molecule for Coxsackievirus A9 cell attachment. Hum Immunol 61, 867-878.
    • (2000) Hum Immunol , vol.61 , pp. 867-878
    • Triantafilou, M.1    Triantafilou, K.2    Wilson, K.M.3
  • 23
    • 0034050359 scopus 로고    scopus 로고
    • High affinity interactions of Coxsackievirus A9 with integrin αVβ3 (CD51/61) require the CYDMKTTC sequence of β3, but do not require the RGD sequence of the CAV-9 VP1 protein
    • Triantafilou, M., Triantafilou, K., Wilson, K. M., Takada, Y. & Fernandez, N. (2000b). High affinity interactions of Coxsackievirus A9 with integrin αVβ3 (CD51/61) require the CYDMKTTC sequence of β3, but do not require the RGD sequence of the CAV-9 VP1 protein. Hum Immunol 61, 453-459.
    • (2000) Hum Immunol , vol.61 , pp. 453-459
    • Triantafilou, M.1    Triantafilou, K.2    Wilson, K.M.3    Takada, Y.4    Fernandez, N.5
  • 24
    • 0036139925 scopus 로고    scopus 로고
    • GRP78, a coreceptor for coxsackievirus A9, interacts with major histocompatibility complex class I molecules which mediate virus internalization
    • Triantafilou, K., Fradelizi, D., Wilson, K. & Triantafilou, M. (2002). GRP78, a coreceptor for coxsackievirus A9, interacts with major histocompatibility complex class I molecules which mediate virus internalization. J Virol 76, 633-643.
    • (2002) J Virol , vol.76 , pp. 633-643
    • Triantafilou, K.1    Fradelizi, D.2    Wilson, K.3    Triantafilou, M.4
  • 25
    • 31144465690 scopus 로고    scopus 로고
    • Quasispecies diversity determines pathogenesis through cooperative interactions in a viral population
    • Vignuzzi, M., Stone, J. K., Arnold, J. J., Cameron, C. E. & Andino, R. (2006). Quasispecies diversity determines pathogenesis through cooperative interactions in a viral population. Nature 439, 344-348.
    • (2006) Nature , vol.439 , pp. 344-348
    • Vignuzzi, M.1    Stone, J.K.2    Arnold, J.J.3    Cameron, C.E.4    Andino, R.5
  • 26
    • 0028173629 scopus 로고
    • Role of the integrin αVβ6 in cell attachment to fibronectin. Heterologous expression of intact and secreted forms of the receptor
    • Weinacker, A., Chen, A., Agrez, M., Cone, R. I., Nishimura, S., Wayner, E., Pytela, R. & Sheppard, D. (1994). Role of the integrin αVβ6 in cell attachment to fibronectin. Heterologous expression of intact and secreted forms of the receptor. J Biol Chem 269, 6940-6948.
    • (1994) J Biol Chem , vol.269 , pp. 6940-6948
    • Weinacker, A.1    Chen, A.2    Agrez, M.3    Cone, R.I.4    Nishimura, S.5    Wayner, E.6    Pytela, R.7    Sheppard, D.8
  • 28
    • 0030805087 scopus 로고    scopus 로고
    • Cell attachment and mouse virulence of echovirus 9 correlate with an RGD motif in the capsid protein VP1
    • Zimmermann, H., Eggers, H. J. & Nelsen-Salz, B. (1997). Cell attachment and mouse virulence of echovirus 9 correlate with an RGD motif in the capsid protein VP1. Virology 233, 149-156.
    • (1997) Virology , vol.233 , pp. 149-156
    • Zimmermann, H.1    Eggers, H.J.2    Nelsen-Salz, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.