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Volumn 82, Issue 13, 2008, Pages 6379-6394

Dendritic cell internalization of foot-and-mouth disease virus: Influence of heparan sulfate binding on virus uptake and induction of the immune response

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOHEXIMIDE; HEPARAN SULFATE; IMMUNOGLOBULIN G; INTEGRIN; VIRUS ANTIGEN; VIRUS RNA;

EID: 45749114579     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00021-08     Document Type: Article
Times cited : (23)

References (55)
  • 1
    • 0034012911 scopus 로고    scopus 로고
    • A porcine cell surface receptor identified by monoclonal antibodies to SWC3 is a member of the signal regulatory protein family and associates with protein-tyrosine phosphatase SHP-1
    • Alvarez, B., C. Sanchez, R. Bullido, A. Marina, J. Lunney, F. Alonso, A. Ezquerra, and J. Dominguez. 2000. A porcine cell surface receptor identified by monoclonal antibodies to SWC3 is a member of the signal regulatory protein family and associates with protein-tyrosine phosphatase SHP-1. Tissue Antigens 55:342-351.
    • (2000) Tissue Antigens , vol.55 , pp. 342-351
    • Alvarez, B.1    Sanchez, C.2    Bullido, R.3    Marina, A.4    Lunney, J.5    Alonso, F.6    Ezquerra, A.7    Dominguez, J.8
  • 2
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • Banchereau, J., and R. M. Steinman. 1998. Dendritic cells and the control of immunity. Nature 392:245-252.
    • (1998) Nature , vol.392 , pp. 245-252
    • Banchereau, J.1    Steinman, R.M.2
  • 3
    • 0141676531 scopus 로고    scopus 로고
    • Recovery of infectious foot-and-mouth disease virus from suckling mice after direct inoculation with in vitro-transcribed RNA
    • Baranowski, E., N. Molina, J. I. Nunez, F. Sobrino, and M. Saiz. 2003. Recovery of infectious foot-and-mouth disease virus from suckling mice after direct inoculation with in vitro-transcribed RNA. J.Virol. 77:11290-11295.
    • (2003) J.Virol , vol.77 , pp. 11290-11295
    • Baranowski, E.1    Molina, N.2    Nunez, J.I.3    Sobrino, F.4    Saiz, M.5
  • 4
    • 0033931398 scopus 로고    scopus 로고
    • Cell recognition by foot-and-mouth disease virus that lacks the RGD integrin-binding motif: Flexibility in aphthovirus receptor usage
    • Baranowski, E., C. M. Ruiz-Jarabo, N. Sevilla, D. Andreu, E. Beck, and E. Domingo. 2000. Cell recognition by foot-and-mouth disease virus that lacks the RGD integrin-binding motif: flexibility in aphthovirus receptor usage. J. Virol. 74:1641-1647.
    • (2000) J. Virol , vol.74 , pp. 1641-1647
    • Baranowski, E.1    Ruiz-Jarabo, C.M.2    Sevilla, N.3    Andreu, D.4    Beck, E.5    Domingo, E.6
  • 6
    • 16244372726 scopus 로고    scopus 로고
    • Constitutive expression of alpha interferon by skin dendritic cells confers resistance to infection by foot-and-mouth disease virus
    • Bautista, E. M., G. S. Ferman, D. Gregg, M. C. Brum, M. J. Grubman, and W. T. Golde. 2005. Constitutive expression of alpha interferon by skin dendritic cells confers resistance to infection by foot-and-mouth disease virus. J. Virol. 79:4838-4847.
    • (2005) J. Virol , vol.79 , pp. 4838-4847
    • Bautista, E.M.1    Ferman, G.S.2    Gregg, D.3    Brum, M.C.4    Grubman, M.J.5    Golde, W.T.6
  • 7
    • 0018826982 scopus 로고
    • Early interactions of foot-and-mouth disease virus with cultured cells
    • Baxt, B., and H. L. Bachrach. 1980. Early interactions of foot-and-mouth disease virus with cultured cells. Virology 104:42-55.
    • (1980) Virology , vol.104 , pp. 42-55
    • Baxt, B.1    Bachrach, H.L.2
  • 8
    • 0028913126 scopus 로고
    • Foot-and-mouth disease virus undergoes restricted replication in macrophage cell cultures following Fc receptor-mediated adsorption
    • Baxt, B., and P. W. Mason. 1995. Foot-and-mouth disease virus undergoes restricted replication in macrophage cell cultures following Fc receptor-mediated adsorption. Virology 207:503-509.
    • (1995) Virology , vol.207 , pp. 503-509
    • Baxt, B.1    Mason, P.W.2
  • 9
    • 35448950496 scopus 로고    scopus 로고
    • Porcine B-cell activating factor promotes anti-FMDV antibodies in vitro but not in vivo after DNA vaccination of pigs
    • Bergamin, F., L. Saurer, V. Neuhaus, K. C. McCullough, and A. Summerfield. 2007. Porcine B-cell activating factor promotes anti-FMDV antibodies in vitro but not in vivo after DNA vaccination of pigs. Vet. Immunol. Immunopathol. 120:115-123.
    • (2007) Vet. Immunol. Immunopathol , vol.120 , pp. 115-123
    • Bergamin, F.1    Saurer, L.2    Neuhaus, V.3    McCullough, K.C.4    Summerfield, A.5
  • 11
    • 18144398862 scopus 로고    scopus 로고
    • Human papillomavirus 16 virus-like particles use heparan sulfates to bind dendritic cells and colocalize with langerin in Langerhans cells
    • Bousarghin, L., P. Hubert, E. Franzen, N. Jacobs, J. Boniver, and P. Delvenne. 2005. Human papillomavirus 16 virus-like particles use heparan sulfates to bind dendritic cells and colocalize with langerin in Langerhans cells. J. Gen. Virol. 86:1297-1305.
    • (2005) J. Gen. Virol , vol.86 , pp. 1297-1305
    • Bousarghin, L.1    Hubert, P.2    Franzen, E.3    Jacobs, N.4    Boniver, J.5    Delvenne, P.6
  • 14
    • 17544382774 scopus 로고    scopus 로고
    • Double-stranded secondary structures on mRNA induce type I interferon (IFN alpha/beta) production and maturation of mRNA-transfected monocyte-derived dendritic cells
    • Ceppi, M., N. Ruggli, V. Tache, H. Gerber, K. C. McCullough, and A. Summerfield. 2005. Double-stranded secondary structures on mRNA induce type I interferon (IFN alpha/beta) production and maturation of mRNA-transfected monocyte-derived dendritic cells. J. Gene Med. 7:452-465.
    • (2005) J. Gene Med , vol.7 , pp. 452-465
    • Ceppi, M.1    Ruggli, N.2    Tache, V.3    Gerber, H.4    McCullough, K.C.5    Summerfield, A.6
  • 15
    • 0030245788 scopus 로고    scopus 로고
    • Long-term, large-population passage of aphthovirus can generate and amplify defective noninterfering particles deleted in the leader protease gene
    • Charpentier, N., M. Davila, E. Domingo, and C. Escarmis. 1996. Long-term, large-population passage of aphthovirus can generate and amplify defective noninterfering particles deleted in the leader protease gene. Virology 223:10-18.
    • (1996) Virology , vol.223 , pp. 10-18
    • Charpentier, N.1    Davila, M.2    Domingo, E.3    Escarmis, C.4
  • 16
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper, J. A. 1987. Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105:1473-1478.
    • (1987) J. Cell Biol , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 18
    • 0019186617 scopus 로고
    • Nucleotide sequence heterogeneity of the RNA from a natural population of foot-and-mouth-disease virus
    • Domingo, E., M. Davila, and J. Ortin. 1980. Nucleotide sequence heterogeneity of the RNA from a natural population of foot-and-mouth-disease virus. Gene 11:333-346.
    • (1980) Gene , vol.11 , pp. 333-346
    • Domingo, E.1    Davila, M.2    Ortin, J.3
  • 20
    • 0030042764 scopus 로고    scopus 로고
    • Actin filaments facilitate two steps of endocytosis
    • Durrbach, A., D. Louvard, and E. Coudrier. 1996. Actin filaments facilitate two steps of endocytosis. J. Cell Sci. 109:457-465.
    • (1996) J. Cell Sci , vol.109 , pp. 457-465
    • Durrbach, A.1    Louvard, D.2    Coudrier, E.3
  • 22
    • 0025273268 scopus 로고
    • Cell-induced conformational change in poliovirus: Externalization of the amino terminus of VP1 is responsible for liposome binding
    • Fricks, C. E., and J. M. Hogle. 1990. Cell-induced conformational change in poliovirus: externalization of the amino terminus of VP1 is responsible for liposome binding. J. Virol. 64:1934-1945.
    • (1990) J. Virol , vol.64 , pp. 1934-1945
    • Fricks, C.E.1    Hogle, J.M.2
  • 23
    • 0027422802 scopus 로고
    • Characterization of poliovirus conformational alteration mediated by soluble cell receptors
    • Gómez Yafal, A., G. Kaplan, V. R. Racaniello, and J. M. Hogle. 1993. Characterization of poliovirus conformational alteration mediated by soluble cell receptors. Virology 197:501-505.
    • (1993) Virology , vol.197 , pp. 501-505
    • Gómez Yafal, A.1    Kaplan, G.2    Racaniello, V.R.3    Hogle, J.M.4
  • 24
    • 33746256867 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cell activation by foot-and-mouth disease virus requires immune complexes
    • Guzylack-Piriou, L., F. Bergamin, M. Gerber, K. C. McCullough, and A. Summerfield. 2006. Plasmacytoid dendritic cell activation by foot-and-mouth disease virus requires immune complexes. Eur. J. Immunol. 36:1674-1683.
    • (2006) Eur. J. Immunol , vol.36 , pp. 1674-1683
    • Guzylack-Piriou, L.1    Bergamin, F.2    Gerber, M.3    McCullough, K.C.4    Summerfield, A.5
  • 28
    • 0033625053 scopus 로고    scopus 로고
    • The epithelial integrin αvβ6 is a receptor for foot-and-mouth disease virus
    • Jackson, T., D. Sheppard, M. Denyer, W. Blakemore, and A. M. Q. King. 2000. The epithelial integrin αvβ6 is a receptor for foot-and-mouth disease virus. J. Virol. 74:4949-4956.
    • (2000) J. Virol , vol.74 , pp. 4949-4956
    • Jackson, T.1    Sheppard, D.2    Denyer, M.3    Blakemore, W.4    King, A.M.Q.5
  • 30
    • 0032930766 scopus 로고    scopus 로고
    • Virus interactions with dendritic cells
    • Klagge, I. M., and S. Schneider-Schaulies. 1999. Virus interactions with dendritic cells. J. Gen. Virol. 80:823-833.
    • (1999) J. Gen. Virol , vol.80 , pp. 823-833
    • Klagge, I.M.1    Schneider-Schaulies, S.2
  • 31
    • 14744300849 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus replication sites form next to the nucleus and close to the Golgi apparatus, but exclude marker proteins associated with host membrane compartments
    • Knox, C., K. Moffat, S. Ali, M. Ryan, and T. Wileman. 2005. Foot-and-mouth disease virus replication sites form next to the nucleus and close to the Golgi apparatus, but exclude marker proteins associated with host membrane compartments. J. Gen. Virol. 86:687-696.
    • (2005) J. Gen. Virol , vol.86 , pp. 687-696
    • Knox, C.1    Moffat, K.2    Ali, S.3    Ryan, M.4    Wileman, T.5
  • 32
    • 0025325915 scopus 로고
    • A single amino acid substitution affects multiple overlapping epitopes in the major antigenic site of foot-and-mouth disease virus of serotype C
    • Mateu, M. G., M. A. Martinez, L. Capucci, D. Andren, E. Giralt, F. Sobrino, E. Brocchi, and E. Domingo. 1990. A single amino acid substitution affects multiple overlapping epitopes in the major antigenic site of foot-and-mouth disease virus of serotype C. J. Gen. Virol. 71:629-637.
    • (1990) J. Gen. Virol , vol.71 , pp. 629-637
    • Mateu, M.G.1    Martinez, M.A.2    Capucci, L.3    Andren, D.4    Giralt, E.5    Sobrino, F.6    Brocchi, E.7    Domingo, E.8
  • 33
    • 0020399806 scopus 로고
    • Monoclonal antibodies against foot-and-mouth disease virus 146S and 12S particles
    • McCullough, K. C., and R. Butcher. 1982. Monoclonal antibodies against foot-and-mouth disease virus 146S and 12S particles. Arch. Virol. 74:1-9.
    • (1982) Arch. Virol , vol.74 , pp. 1-9
    • McCullough, K.C.1    Butcher, R.2
  • 35
    • 0023680184 scopus 로고
    • Opsonization-enhanced phagocytosis of foot-and-mouth disease virus
    • McCullough, K. C., D. Parkinson, and J. R. Crowther. 1988. Opsonization-enhanced phagocytosis of foot-and-mouth disease virus. Immunology 65:187-191.
    • (1988) Immunology , vol.65 , pp. 187-191
    • McCullough, K.C.1    Parkinson, D.2    Crowther, J.R.3
  • 37
    • 0031683911 scopus 로고    scopus 로고
    • Macrophage cytoplasmic vesicle pH gradients and vacuolar H+-ATPase activities relative to virus infection
    • Natale, V. A., and K. C. McCullough. 1998. Macrophage cytoplasmic vesicle pH gradients and vacuolar H+-ATPase activities relative to virus infection. J. Leukoc. Biol. 64:302-310.
    • (1998) J. Leukoc. Biol , vol.64 , pp. 302-310
    • Natale, V.A.1    McCullough, K.C.2
  • 39
    • 20744438160 scopus 로고    scopus 로고
    • Analysis of foot-and-mouth disease virus internalization events in cultured cells
    • O'Donnell, V., M. LaRocco, H. Duque, and B. Baxt. 2005. Analysis of foot-and-mouth disease virus internalization events in cultured cells. J. Virol. 79:8506-8518.
    • (2005) J. Virol , vol.79 , pp. 8506-8518
    • O'Donnell, V.1    LaRocco, M.2    Duque, H.3    Baxt, B.4
  • 40
    • 24744455441 scopus 로고    scopus 로고
    • Impairment of thymus-dependent responses by murine dendritic cells infected with foot-and-mouth disease virus
    • Ostrowski, M., M. Vermeulen, O. Zabal, J. R. Geffner, A. M. Sadir, and O. J. Lopez. 2005. Impairment of thymus-dependent responses by murine dendritic cells infected with foot-and-mouth disease virus. J. Immunol. 175:3971-3979.
    • (2005) J. Immunol , vol.175 , pp. 3971-3979
    • Ostrowski, M.1    Vermeulen, M.2    Zabal, O.3    Geffner, J.R.4    Sadir, A.M.5    Lopez, O.J.6
  • 41
    • 4544291665 scopus 로고    scopus 로고
    • Ligand dependent and independent internalization and nuclear translocation of fibroblast growth factor (FGF) receptor 1
    • Reilly, J. F., E. Mizukoshi, and P. A. Maher. 2004. Ligand dependent and independent internalization and nuclear translocation of fibroblast growth factor (FGF) receptor 1. DNA Cell Biol. 23:538-548.
    • (2004) DNA Cell Biol , vol.23 , pp. 538-548
    • Reilly, J.F.1    Mizukoshi, E.2    Maher, P.A.3
  • 42
    • 0036037270 scopus 로고    scopus 로고
    • Macrophage phagocytosis of foot-and-mouth disease virus may create infectious carriers
    • Rigden, R. C., C. P. Carrasco, A. Summerfield, and K. C. McCullough. 2002. Macrophage phagocytosis of foot-and-mouth disease virus may create infectious carriers. Immunology 106:537-548.
    • (2002) Immunology , vol.106 , pp. 537-548
    • Rigden, R.C.1    Carrasco, C.P.2    Summerfield, A.3    McCullough, K.C.4
  • 43
    • 0030971779 scopus 로고    scopus 로고
    • Tissue culture adaptation of foot-and-mouth disease virus selects viruses that bind to heparin and are attenuated in cattle
    • Sa-Carvalho, D., E. Rieder, B. Baxt, R. Rodarte, A. Tanuri, and P. W. Mason. 1997. Tissue culture adaptation of foot-and-mouth disease virus selects viruses that bind to heparin and are attenuated in cattle. J. Virol. 71:5115-5123.
    • (1997) J. Virol , vol.71 , pp. 5115-5123
    • Sa-Carvalho, D.1    Rieder, E.2    Baxt, B.3    Rodarte, R.4    Tanuri, A.5    Mason, P.W.6
  • 44
    • 0020044056 scopus 로고
    • Action of cytochalasin D on cytoskeletal networks
    • Schliwa, M. 1982. Action of cytochalasin D on cytoskeletal networks. J. Cell Biol. 92:79-91.
    • (1982) J. Cell Biol , vol.92 , pp. 79-91
    • Schliwa, M.1
  • 45
    • 0038384133 scopus 로고    scopus 로고
    • Binding of a N,N′-bisheteryl derivative of dispirotripiperazine to heparan sulfate residues on the cell surface specifically prevents infection of viruses from different families
    • Schmidtke, M., A. Karger, A. Meerbach, R. Egerer, A. Stelzner, and V. Makarov. 2003. Binding of a N,N′-bisheteryl derivative of dispirotripiperazine to heparan sulfate residues on the cell surface specifically prevents infection of viruses from different families. Virology 311:134-143.
    • (2003) Virology , vol.311 , pp. 134-143
    • Schmidtke, M.1    Karger, A.2    Meerbach, A.3    Egerer, R.4    Stelzner, A.5    Makarov, V.6
  • 46
    • 0025855933 scopus 로고
    • Monoclonal antibodies to double-stranded RNA as probes of RNA structure in crude nucleic acid extracts
    • Schönborn, J., J. Oberstrass, E. Breyel, J. Tittgen, J. Schumacher, and N. Lukacs. 1991. Monoclonal antibodies to double-stranded RNA as probes of RNA structure in crude nucleic acid extracts. Nucleic Acids Res. 19:2993-3000.
    • (1991) Nucleic Acids Res , vol.19 , pp. 2993-3000
    • Schönborn, J.1    Oberstrass, J.2    Breyel, E.3    Tittgen, J.4    Schumacher, J.5    Lukacs, N.6
  • 47
    • 23744483354 scopus 로고    scopus 로고
    • TLR3 in antiviral immunity: Key player or bystander?
    • Schröder, M., and A. G. Bowie. 2005. TLR3 in antiviral immunity: key player or bystander? Trends Immunol. 26:462-468.
    • (2005) Trends Immunol , vol.26 , pp. 462-468
    • Schröder, M.1    Bowie, A.G.2
  • 48
    • 0029794374 scopus 로고    scopus 로고
    • Evolution of a persistent aphthovirus in cytolytic infections: Partial reversion of phenotypic traits accompanied by genetic diversification
    • Sevilla, N., and E. Domingo. 1996. Evolution of a persistent aphthovirus in cytolytic infections: partial reversion of phenotypic traits accompanied by genetic diversification. J. Virol. 70:6617-6624.
    • (1996) J. Virol , vol.70 , pp. 6617-6624
    • Sevilla, N.1    Domingo, E.2
  • 49
    • 18044365415 scopus 로고    scopus 로고
    • Induction of inflammatory cytokines and interferon responses by double-stranded and single-stranded siRNAs is sequence-dependent and requires endosomal localization
    • Sioud, M. 2005. Induction of inflammatory cytokines and interferon responses by double-stranded and single-stranded siRNAs is sequence-dependent and requires endosomal localization. J. Mol. Biol. 348:1079-1090.
    • (2005) J. Mol. Biol , vol.348 , pp. 1079-1090
    • Sioud, M.1
  • 50
    • 0020544508 scopus 로고
    • Multiple genetic variants arise in the course of replication of foot-and-mouth disease virus in cell culture
    • Sobrino, F., M. Davila, J. Ortin, and E. Domingo. 1983. Multiple genetic variants arise in the course of replication of foot-and-mouth disease virus in cell culture. Virology 128:310-318.
    • (1983) Virology , vol.128 , pp. 310-318
    • Sobrino, F.1    Davila, M.2    Ortin, J.3    Domingo, E.4
  • 51
    • 0022917448 scopus 로고
    • Fixation of mutations in the viral genome during an outbreak of foot-and-mouth disease: Heterogeneity and rate variations
    • Sobrino, F., E. L. Palma, E. Beck, M. Davila, J. C. de la Torre, P. Negro, N. Villanueva, J. Ortin, and E. Domingo. 1986. Fixation of mutations in the viral genome during an outbreak of foot-and-mouth disease: heterogeneity and rate variations. Gene 50:149-159.
    • (1986) Gene , vol.50 , pp. 149-159
    • Sobrino, F.1    Palma, E.L.2    Beck, E.3    Davila, M.4    de la Torre, J.C.5    Negro, P.6    Villanueva, N.7    Ortin, J.8    Domingo, E.9
  • 52
    • 20644463701 scopus 로고    scopus 로고
    • Role of clathrin-mediated endocytosis during vesicular stomatitis virus entry into host cells
    • Sun, X., V. K. Yau, B. J. Briggs, and G. R. Whittaker. 2005. Role of clathrin-mediated endocytosis during vesicular stomatitis virus entry into host cells. Virology. 338:53-60.
    • (2005) Virology , vol.338 , pp. 53-60
    • Sun, X.1    Yau, V.K.2    Briggs, B.J.3    Whittaker, G.R.4
  • 54
    • 0027520440 scopus 로고
    • Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation
    • Wang, L. H., K. G. Rothberg, and R. G. Anderson. 1993. Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation. J. Cell Biol. 123:1107-1117.
    • (1993) J. Cell Biol , vol.123 , pp. 1107-1117
    • Wang, L.H.1    Rothberg, K.G.2    Anderson, R.G.3
  • 55
    • 0033693858 scopus 로고    scopus 로고
    • Human spectrin Src homology 3 domain binding protein 1 regulates macropinocytosis in NIH 3T3 cells
    • Xu, J., D. Ziemnicka, G. S. Merz, and L. Kotula. 2000. Human spectrin Src homology 3 domain binding protein 1 regulates macropinocytosis in NIH 3T3 cells. J. Cell Sci. 113:3805-3814.
    • (2000) J. Cell Sci , vol.113 , pp. 3805-3814
    • Xu, J.1    Ziemnicka, D.2    Merz, G.S.3    Kotula, L.4


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