메뉴 건너뛰기




Volumn 73, Issue 9, 1999, Pages 7703-7709

Fish rhabdovirus cell entry is mediated by fibronectin

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; MONOCLONAL ANTIBODY;

EID: 0032854176     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.9.7703-7709.1999     Document Type: Article
Times cited : (78)

References (43)
  • 1
    • 0027944178 scopus 로고
    • Human cytomegalovirus interaction with platelets and adhesive glycoproteins: Significance in viral pathogenesis
    • Agbanyo, F. R., and S. Wasi. 1994. Human cytomegalovirus interaction with platelets and adhesive glycoproteins: significance in viral pathogenesis. J. Infect. Dis. 170:1120-1127.
    • (1994) J. Infect. Dis. , vol.170 , pp. 1120-1127
    • Agbanyo, F.R.1    Wasi, S.2
  • 2
    • 0026599667 scopus 로고
    • Strategies for the identification of icosahedral virus receptors
    • Bass, D. M., and H. B. Greenberg. 1992. Strategies for the identification of icosahedral virus receptors. J. Clin. Investig. 89:3-9.
    • (1992) J. Clin. Investig. , vol.89 , pp. 3-9
    • Bass, D.M.1    Greenberg, H.B.2
  • 3
    • 0030696504 scopus 로고    scopus 로고
    • Sequence variation of the glycoprotein gene identifies three distinct lineages within field isolates of viral haemorrhagic septicaemia virus, a fish rhabdovirus
    • Benmansour, A., B. Basurco, A. F. Monnier, P. Vende, J. R. Winton, and P. de Kinkelin. 1997. Sequence variation of the glycoprotein gene identifies three distinct lineages within field isolates of viral haemorrhagic septicaemia virus, a fish rhabdovirus. J. Gen. Virol. 78:2837-2846.
    • (1997) J. Gen. Virol. , vol.78 , pp. 2837-2846
    • Benmansour, A.1    Basurco, B.2    Monnier, A.F.3    Vende, P.4    Winton, J.R.5    De Kinkelin, P.6
  • 4
    • 17144445526 scopus 로고    scopus 로고
    • The glycoprotein genes and gene junctions of the fish rhabdoviruses spring viremia of carp virus and hirame rhabdovirus: Analysis of relationships with other rhabdoviruses
    • Bjorklund, H. V., K. H. Higman, and G. Kurath. 1996. The glycoprotein genes and gene junctions of the fish rhabdoviruses spring viremia of carp virus and hirame rhabdovirus: analysis of relationships with other rhabdoviruses. Virus Res. 42:65-80.
    • (1996) Virus Res. , vol.42 , pp. 65-80
    • Bjorklund, H.V.1    Higman, K.H.2    Kurath, G.3
  • 5
    • 0023755388 scopus 로고
    • Antipeptide monoclonal antibodies inhibit the binding of rabies virus glycoprotein and alpha-bungarotoxin to the nicotinic acetylcholine receptor
    • Bracci, L., G. Antoni, M. G. Cusi, L. Lozzi, N. Niccolai, S. Petreni, M. Rustici, A. Santucci, P. Soldani, and P. E. Valensin. 1988. Antipeptide monoclonal antibodies inhibit the binding of rabies virus glycoprotein and alpha-bungarotoxin to the nicotinic acetylcholine receptor. Mol. Immunol. 25:881-888.
    • (1988) Mol. Immunol. , vol.25 , pp. 881-888
    • Bracci, L.1    Antoni, G.2    Cusi, M.G.3    Lozzi, L.4    Niccolai, N.5    Petreni, S.6    Rustici, M.7    Santucci, A.8    Soldani, P.9    Valensin, P.E.10
  • 6
    • 0029139185 scopus 로고
    • Characterization of protein involvement in rabies virus binding to BHK-21 cells
    • Broughan, J. H., and W. H. Wunner. 1995. Characterization of protein involvement in rabies virus binding to BHK-21 cells. Arch. Virol. 140:75-93.
    • (1995) Arch. Virol. , vol.140 , pp. 75-93
    • Broughan, J.H.1    Wunner, W.H.2
  • 7
    • 0028873677 scopus 로고
    • Fibronectin of human liver sinusoids binds hepatitis B virus: Identification by an anti-idiotypic antibody bearing the internal image of the pre-S2 domain
    • Budkowska, A., P. Bedossa, F. Grob, A. Louise, and J. Pillot. 1995. Fibronectin of human liver sinusoids binds hepatitis B virus: identification by an anti-idiotypic antibody bearing the internal image of the pre-S2 domain. J. Virol. 69:840-848.
    • (1995) J. Virol. , vol.69 , pp. 840-848
    • Budkowska, A.1    Bedossa, P.2    Grob, F.3    Louise, A.4    Pillot, J.5
  • 9
    • 0018936427 scopus 로고
    • Rainbow trout gill pillar cells: Demonstration of inert particle phagocytosis and involvement in viral infection
    • Chilmonczyk, S., and D. Monge. 1980. Rainbow trout gill pillar cells: demonstration of inert particle phagocytosis and involvement in viral infection. J. Reticuloendothel. Soc. 28:327-332.
    • (1980) J. Reticuloendothel. Soc. , vol.28 , pp. 327-332
    • Chilmonczyk, S.1    Monge, D.2
  • 10
    • 0022990595 scopus 로고
    • Membrane carbohydrate requirement for rabies virus binding to chicken embryo related cells
    • Conti, C., F. Superti, and H. Tsiang. 1986. Membrane carbohydrate requirement for rabies virus binding to chicken embryo related cells. Intervirology 26:164-168.
    • (1986) Intervirology , vol.26 , pp. 164-168
    • Conti, C.1    Superti, F.2    Tsiang, H.3
  • 11
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. 1988. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16:10881-10890.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 12
    • 0025352589 scopus 로고
    • Extracellular glycoproteins at acetylcholine receptor clusters of rat myotubes are organized into domains
    • Dmytrenko, G. M., M. G. Scher, G. Poiana, M. Baetscher, and R. J. Bloch. 1990. Extracellular glycoproteins at acetylcholine receptor clusters of rat myotubes are organized into domains. Exp. Cell Res. 189:41-50.
    • (1990) Exp. Cell Res. , vol.189 , pp. 41-50
    • Dmytrenko, G.M.1    Scher, M.G.2    Poiana, G.3    Baetscher, M.4    Bloch, R.J.5
  • 13
    • 0027240666 scopus 로고
    • Evidence for transmembrane anchoring of extracellular matrix at acetylcholine receptor clusters
    • Dmytrenko, G. M., and R. J. Bloch. 1993. Evidence for transmembrane anchoring of extracellular matrix at acetylcholine receptor clusters. Exp. Cell Res. 206:323-334.
    • (1993) Exp. Cell Res. , vol.206 , pp. 323-334
    • Dmytrenko, G.M.1    Bloch, R.J.2
  • 14
    • 0029913917 scopus 로고    scopus 로고
    • Pepscan mapping and fusion related properties of the major phosphatidylserine-binding domain of the glycoprotein of VHSV, a salmonid rhabdovirus
    • Estepa, A., and J. M. Coll. 1996. Pepscan mapping and fusion related properties of the major phosphatidylserine-binding domain of the glycoprotein of VHSV, a salmonid rhabdovirus. Virology 216:60-70.
    • (1996) Virology , vol.216 , pp. 60-70
    • Estepa, A.1    Coll, J.M.2
  • 16
    • 0029909548 scopus 로고    scopus 로고
    • Rabies virus binding to the nicotinic acetylcholine receptor alpha subunit demonstrated by virus overlay protein binding assay
    • Gastka, M., J. Horvath, and T. L. Lentz. 1996. Rabies virus binding to the nicotinic acetylcholine receptor alpha subunit demonstrated by virus overlay protein binding assay. J. Gen. Virol. 77:2437-2440.
    • (1996) J. Gen. Virol. , vol.77 , pp. 2437-2440
    • Gastka, M.1    Horvath, J.2    Lentz, T.L.3
  • 17
    • 0028078572 scopus 로고
    • Virus receptors: Binding, adhesion strengthening, and changes in viral structure
    • Haywood, A. M. 1994. Virus receptors: binding, adhesion strengthening, and changes in viral structure. J. Virol. 68:1-5.
    • (1994) J. Virol. , vol.68 , pp. 1-5
    • Haywood, A.M.1
  • 18
    • 0029187341 scopus 로고
    • The esophagus/cardiac stomach region: Site of attachment and internalization of infectious hematopoietic necrosis virus in challenged juvenile rainbow trout Oncorhynchus mykiss and coho salmon O. kisutch
    • Helmick, C. M., J. F. Bailey, S. LaPatra, and S. Ristow. 1995. The esophagus/cardiac stomach region: site of attachment and internalization of infectious hematopoietic necrosis virus in challenged juvenile rainbow trout Oncorhynchus mykiss and coho salmon O. kisutch. Dis. Aquat. Org. 23:189-199.
    • (1995) Dis. Aquat. Org. , vol.23 , pp. 189-199
    • Helmick, C.M.1    Bailey, J.F.2    LaPatra, S.3    Ristow, S.4
  • 19
    • 0027292986 scopus 로고
    • Bacterial proteins binding to the mammalian extracellular matrix
    • Korhonen, T. K. 1993. Bacterial proteins binding to the mammalian extracellular matrix. Mol. Microbiol. 9:687-694.
    • (1993) Mol. Microbiol. , vol.9 , pp. 687-694
    • Korhonen, T.K.1
  • 22
    • 0025349746 scopus 로고
    • Neutralization of Egtved virus pathogenicity to cell cultures and fish by monoclonal antibodies to the viral G protein
    • Lorenzen, N., N. J. Olesen, and P. E. Jorgensen. 1990. Neutralization of Egtved virus pathogenicity to cell cultures and fish by monoclonal antibodies to the viral G protein. J. Gen. Virol. 71:561-567.
    • (1990) J. Gen. Virol. , vol.71 , pp. 561-567
    • Lorenzen, N.1    Olesen, N.J.2    Jorgensen, P.E.3
  • 23
    • 0028882375 scopus 로고
    • The complete genome structure and phylogenetic relationship of infectious hematopoietic necrosis virus
    • Morzunov, S. P., J. R., Winton, and S. T. Nichol. 1995. The complete genome structure and phylogenetic relationship of infectious hematopoietic necrosis virus. Virus Res. 38:175-192.
    • (1995) Virus Res. , vol.38 , pp. 175-192
    • Morzunov, S.P.1    Winton, J.R.2    Nichol, S.T.3
  • 25
    • 0023182351 scopus 로고
    • Vesicular stomatitis virus membrane proteins and their interaction with lipid bilayers
    • Pal, R., Y. Barenholz, and R. R. Wagner. 1987. Vesicular stomatitis virus membrane proteins and their interaction with lipid bilayers. Biochim. Biophys. Acta 906:175-193.
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 175-193
    • Pal, R.1    Barenholz, Y.2    Wagner, R.R.3
  • 26
    • 0023367927 scopus 로고
    • Fibronectin: A brief overview of its structure, function, and physiology
    • Proctor, R. A. 1987. Fibronectin: a brief overview of its structure, function, and physiology. Rev. Infect. Dis. 9(Suppl. 4):S317-S321.
    • (1987) Rev. Infect. Dis. , vol.9 , Issue.SUPPL. 4
    • Proctor, R.A.1
  • 28
    • 0027263014 scopus 로고
    • Purification of a mycobacterial adhesin for fibronectin
    • Ratliff, T. L., R. McCarthy, W. B. Telle, and E. J. Brown. 1993. Purification of a mycobacterial adhesin for fibronectin. Infect. Immun. 61:1889-1894.
    • (1993) Infect. Immun. , vol.61 , pp. 1889-1894
    • Ratliff, T.L.1    McCarthy, R.2    Telle, W.B.3    Brown, E.J.4
  • 29
    • 0028896143 scopus 로고
    • Cellular actin-binding ezrin-radixin-moesin (ERM) family proteins are incorporated into the rabies virion and closely associated with viral envelope proteins in the cell
    • Sagara, J., S. Tsukita, S. Yonemura, S. Tsukita, and A. Kawai. 1995. Cellular actin-binding ezrin-radixin-moesin (ERM) family proteins are incorporated into the rabies virion and closely associated with viral envelope proteins in the cell. Virology 206:485-494.
    • (1995) Virology , vol.206 , pp. 485-494
    • Sagara, J.1    Tsukita, S.2    Yonemura, S.3    Tsukita, S.4    Kawai, A.5
  • 30
    • 0025173021 scopus 로고
    • Molecular characterization of a rotaviruslike virus isolated from striped bass (Morone saxatilis)
    • Samal, S. K., C. P. Dopazo, T. H. McPhillips, A. Baya, S. B. Mohanty, and F. M. Hetrick. 1990. Molecular characterization of a rotaviruslike virus isolated from striped bass (Morone saxatilis). J. Virol. 64:5235-5240.
    • (1990) J. Virol. , vol.64 , pp. 5235-5240
    • Samal, S.K.1    Dopazo, C.P.2    McPhillips, T.H.3    Baya, A.4    Mohanty, S.B.5    Hetrick, F.M.6
  • 31
    • 0020712445 scopus 로고
    • Inhibition of VSV binding and infectivity by phosphatidylserine: Is phosphatidylserine a VSV-binding site?
    • Schiegel, R., T. S. Tralka, M. C. Willingham, I. Pastan. 1983. Inhibition of VSV binding and infectivity by phosphatidylserine: is phosphatidylserine a VSV-binding site? Cell 32:639-646.
    • (1983) Cell , vol.32 , pp. 639-646
    • Schiegel, R.1    Tralka, T.S.2    Willingham, M.C.3    Pastan, I.4
  • 32
    • 0029070194 scopus 로고
    • A Mycobacterium leprae gene encoding a fibronectin binding protein is used for efficient invasion of epithelial cells and Schwann cells
    • Schorey, J. S., Q. Li, D. W. McCourt, M. Bong-Mastek, J. E. Clark-Curtiss, T. L. Ratliff, and E. J. Brown. 1995. A Mycobacterium leprae gene encoding a fibronectin binding protein is used for efficient invasion of epithelial cells and Schwann cells. Infect. Immun. 63:2652-2657.
    • (1995) Infect. Immun. , vol.63 , pp. 2652-2657
    • Schorey, J.S.1    Li, Q.2    McCourt, D.W.3    Bong-Mastek, M.4    Clark-Curtiss, J.E.5    Ratliff, T.L.6    Brown, E.J.7
  • 33
    • 0029784779 scopus 로고    scopus 로고
    • Characterization of the fibronectin-attachment protein of Mycobacterium avium reveals a fibronectin-binding motif conserved among mycobacteria
    • Schorey, J. S., M. A. Holsti, T. L. Ratliff, P. M. Allen, and E. J. Brown. 1996. Characterization of the fibronectin-attachment protein of Mycobacterium avium reveals a fibronectin-binding motif conserved among mycobacteria. Mol. Microbiol. 21:321-329.
    • (1996) Mol. Microbiol. , vol.21 , pp. 321-329
    • Schorey, J.S.1    Holsti, M.A.2    Ratliff, T.L.3    Allen, P.M.4    Brown, E.J.5
  • 35
    • 0020627950 scopus 로고
    • Attachment of Rous sarcoma virus to the fibronectin of infected chick embryo fibroblasts
    • Stanislawski, L. 1983. Attachment of Rous sarcoma virus to the fibronectin of infected chick embryo fibroblasts. J. Ultrastruct. Res. 82:134-142.
    • (1983) J. Ultrastruct. Res. , vol.82 , pp. 134-142
    • Stanislawski, L.1
  • 36
    • 0021277638 scopus 로고
    • Role of phospholipids in rhabdovirus attachment to CER cells. Brief report
    • Superti, F., L. Seganti, H. Tsiang, and N. Orsi. 1984. Role of phospholipids in rhabdovirus attachment to CER cells. Brief report. Arch. Virol. 81:321-328.
    • (1984) Arch. Virol. , vol.81 , pp. 321-328
    • Superti, F.1    Seganti, L.2    Tsiang, H.3    Orsi, N.4
  • 39
    • 0031882105 scopus 로고    scopus 로고
    • Neuronal cell surface molecules mediate specific binding to rabies virus glycoprotein expressed by a recombinant baculovirus on the surfaces of lepidopteran cells
    • Tuffereau, C., J. Benejean, A. M. Alfonso, A. Flamand, and M. C. Fishman. 1998. Neuronal cell surface molecules mediate specific binding to rabies virus glycoprotein expressed by a recombinant baculovirus on the surfaces of lepidopteran cells. J. Virol. 72:1085-1091.
    • (1998) J. Virol. , vol.72 , pp. 1085-1091
    • Tuffereau, C.1    Benejean, J.2    Alfonso, A.M.3    Flamand, A.4    Fishman, M.C.5
  • 40
    • 0032535485 scopus 로고    scopus 로고
    • Low-affinity nerve-growth factor receptor (P75NTR) can serve as a receptor for rabies virus
    • Tuffereau, C., J. Benejean, D. Blondel, B. Kieffer, and A. Flamand. 1998. Low-affinity nerve-growth factor receptor (P75NTR) can serve as a receptor for rabies virus. EMBO J. 17:7250-7259.
    • (1998) EMBO J. , vol.17 , pp. 7250-7259
    • Tuffereau, C.1    Benejean, J.2    Blondel, D.3    Kieffer, B.4    Flamand, A.5
  • 41
    • 0008438621 scopus 로고
    • Binding of microbial pathogen to connective tissue fibronectin: An early step in localized and invasive infections
    • G. J. Jackson (ed.). Springer-Verlag KG, Berlin, Germany
    • Wadström, T., L. M. Switalski, P. Speziale, K. Rubin, C. Ryden, G. Fröman, A. Faris, M. Lindberg, and M. Höök. 1985. Binding of microbial pathogen to connective tissue fibronectin: an early step in localized and invasive infections, p. 193-200. In G. J. Jackson (ed.), Pathogenesis of infection. Springer-Verlag KG, Berlin, Germany.
    • (1985) Pathogenesis of Infection , pp. 193-200
    • Wadström, T.1    Switalski, L.M.2    Speziale, P.3    Rubin, K.4    Ryden, C.5    Fröman, G.6    Faris, A.7    Lindberg, M.8    Höök, M.9
  • 42
    • 0004162696 scopus 로고
    • Comstock Publishing Associates, Cornell University Press, Ithaca, N.Y.
    • Wolf, K. 1988. Fish viruses and fish viral diseases. Comstock Publishing Associates, Cornell University Press, Ithaca, N.Y.
    • (1988) Fish Viruses and Fish Viral Diseases
    • Wolf, K.1
  • 43
    • 0021244469 scopus 로고
    • Characterization of saturable binding sites for rabies virus
    • Wunner, W. H., K. J. Reagan, and H. Koprowski. 1984. Characterization of saturable binding sites for rabies virus. J. Virol. 50:691-697.
    • (1984) J. Virol. , vol.50 , pp. 691-697
    • Wunner, W.H.1    Reagan, K.J.2    Koprowski, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.