메뉴 건너뛰기




Volumn 72, Issue 2, 1998, Pages 1577-1585

A27L protein mediates vaccinia virus interaction with cell surface heparan sulfate

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; CHONDROITIN SULFATE; DERMATAN SULFATE; GENE PRODUCT; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; HEPARIN;

EID: 0031906150     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.2.1577-1585.1998     Document Type: Article
Times cited : (281)

References (52)
  • 1
    • 0022897789 scopus 로고
    • Chlorate - A potent inhibitor of protein sulfation in intact cells
    • Baeuerle, P. A., and W. B. Huttner. 1986. Chlorate - a potent inhibitor of protein sulfation in intact cells. Biochem. Biophys. Res. Commun. 141:870-877.
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 870-877
    • Baeuerle, P.A.1    Huttner, W.B.2
  • 2
    • 0029013579 scopus 로고
    • Sequential isolation of proteoglycan synthesis mutants by using herpes simplex virus as a selective agent: Evidence for a proteoglycan-independent virus entry pathway
    • Banfield, B. W., Y. Leduc, L. Esford, K. Schubert, and F. Tufaro. 1995. Sequential isolation of proteoglycan synthesis mutants by using herpes simplex virus as a selective agent: evidence for a proteoglycan-independent virus entry pathway. J. Virol. 69:3290-8.
    • (1995) J. Virol. , vol.69 , pp. 3290-3298
    • Banfield, B.W.1    Leduc, Y.2    Esford, L.3    Schubert, K.4    Tufaro, F.5
  • 3
    • 0025219217 scopus 로고
    • Acid pH induced fusion of cells by herpes simplex virus glycoproteins gB and gD
    • Butcher, M., K. Raviprakash, and H. P. Ghosh. 1990. Acid pH induced fusion of cells by herpes simplex virus glycoproteins gB and gD. J. Biol. Chem. 265:5862-5868.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5862-5868
    • Butcher, M.1    Raviprakash, K.2    Ghosh, H.P.3
  • 4
    • 0028938550 scopus 로고
    • Isolation of a monoclonal antibody which blocks vaccinia virus infection
    • Chang, W., J.-C. Hsiao, C.-S. Chung, and C.-H. Bair. 1995. Isolation of a monoclonal antibody which blocks vaccinia virus infection. J. Virol. 69:517-522.
    • (1995) J. Virol. , vol.69 , pp. 517-522
    • Chang, W.1    Hsiao, J.-C.2    Chung, C.-S.3    Bair, C.-H.4
  • 5
    • 0023389797 scopus 로고
    • A 14K. envelope protein of vaccinia virus with an important role in virus-host cell interactions is altered during virus persistence and determines the plaque size phenotype of the virus
    • Dallo, S., J. F. Rodriguez, and M. Esteban. 1987. A 14K. envelope protein of vaccinia virus with an important role in virus-host cell interactions is altered during virus persistence and determines the plaque size phenotype of the virus. Virology 159:423-32.
    • (1987) Virology , vol.159 , pp. 423-432
    • Dallo, S.1    Rodriguez, J.F.2    Esteban, M.3
  • 6
    • 0024791519 scopus 로고
    • Structure of vaccinia virus early promoters
    • Davison, A. J., and B. Moss. 1989. Structure of vaccinia virus early promoters. J. Mol. Biol. 210:749-769.
    • (1989) J. Mol. Biol. , vol.210 , pp. 749-769
    • Davison, A.J.1    Moss, B.2
  • 8
    • 0025151572 scopus 로고
    • Fusion of intra- and extracellular forms of vaccinia virus with the cell membrane
    • Doms, R. W., R. Blumenthal, and B. Moss. 1990. Fusion of intra-and extracellular forms of vaccinia virus with the cell membrane. J. Virol. 64:4884-4892.
    • (1990) J. Virol. , vol.64 , pp. 4884-4892
    • Doms, R.W.1    Blumenthal, R.2    Moss, B.3
  • 9
    • 0027980117 scopus 로고
    • Structure of intracellular mature vaccinia virus observed by cryoelectron microscopy
    • Dubochet, J., M. Adrian, K. Richter, J. Garces, and R. Wittek. 1994. Structure of intracellular mature vaccinia virus observed by cryoelectron microscopy. J. Virol. 68:1935-1941.
    • (1994) J. Virol. , vol.68 , pp. 1935-1941
    • Dubochet, J.1    Adrian, M.2    Richter, K.3    Garces, J.4    Wittek, R.5
  • 10
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng, Y., C. C. Broder, P. E. Kennedy, and E. A. Berger. 1996. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272:872-877.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 11
    • 0027422802 scopus 로고
    • Characterization of poliovirus conformational alteration mediated by soluble cell receptors
    • Gomez 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
    • Gomez Yafal, A.1    Kaplan, G.2    Racaniello, V.R.3    Hogle, J.M.4
  • 12
    • 0024446496 scopus 로고
    • r envelope protein of vaccinia virus induces a size change that leads to the small plaque size phenotype of the virus
    • r envelope protein of vaccinia virus induces a size change that leads to the small plaque size phenotype of the virus. J. Virol. 63:4507-4514.
    • (1989) J. Virol. , vol.63 , pp. 4507-4514
    • Gong, S.C.1    Lai, C.F.2    Dallo, S.3    Esteban, M.4
  • 13
    • 0025193184 scopus 로고
    • Vaccinia virus induces cell fusion at acid pH and this activity is mediated by the N-terminus of the 14-kDa virus envelope protein
    • Gong, S. C., C. F. Lai, and M. Esteban. 1990. Vaccinia virus induces cell fusion at acid pH and this activity is mediated by the N-terminus of the 14-kDa virus envelope protein. Virology 178:81-91.
    • (1990) Virology , vol.178 , pp. 81-91
    • Gong, S.C.1    Lai, C.F.2    Esteban, M.3
  • 14
    • 0023681294 scopus 로고
    • Influence of chlorate on proteoglycan biosynthesis by cultured human fibroblasts
    • Greve, H., Z. Cully, P. Blumberg, and H. Kresse. 1988. Influence of chlorate on proteoglycan biosynthesis by cultured human fibroblasts. J. Biol. Chem. 263:12886-12892.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12886-12892
    • Greve, H.1    Cully, Z.2    Blumberg, P.3    Kresse, H.4
  • 15
    • 0027473606 scopus 로고
    • Herpes simplex virus infection and propagation in a mouse L cell mutant lacking heparan sulfate proteoglycans
    • Gruenheid, S., L. Gatzke, H. Meadows, and F. Tufaro. 1993. Herpes simplex virus infection and propagation in a mouse L cell mutant lacking heparan sulfate proteoglycans. J. Virol. 67:93-100.
    • (1993) J. Virol. , vol.67 , pp. 93-100
    • Gruenheid, S.1    Gatzke, L.2    Meadows, H.3    Tufaro, F.4
  • 16
    • 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
    • 0028876742 scopus 로고
    • Identification of structural features of heparin required for inhibition of herpes simplex virus type 1 binding
    • Herold, B. C., S. I. Gerber, T. Polonsky, B. J. Belval, P. N. Shaklee, and K. Holme. 1995. Identification of structural features of heparin required for inhibition of herpes simplex virus type 1 binding. Virology 206:1108-1116.
    • (1995) Virology , vol.206 , pp. 1108-1116
    • Herold, B.C.1    Gerber, S.I.2    Polonsky, T.3    Belval, B.J.4    Shaklee, P.N.5    Holme, K.6
  • 19
    • 0026026623 scopus 로고
    • Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity
    • Herold, B. C., D. WuDunn, N. Soltys, and P. G. Spear. 1991. Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity. J. Virol. 65:1090-1098.
    • (1991) J. Virol. , vol.65 , pp. 1090-1098
    • Herold, B.C.1    WuDunn, D.2    Soltys, N.3    Spear, P.G.4
  • 21
    • 0002796345 scopus 로고
    • The purification of four strains of poxvirus
    • Joklik, W. K. 1962. The purification of four strains of poxvirus. Virology 18:9-18.
    • (1962) Virology , vol.18 , pp. 9-18
    • Joklik, W.K.1
  • 22
    • 0025001939 scopus 로고
    • Neutralization of poliovirus by cell receptors expressed in insect cells
    • Kaplan, G., M. S. Freistadt, and V. R. Racaniello. 1990. Neutralization of poliovirus by cell receptors expressed in insect cells. J. Virol. 64:4697-4702.
    • (1990) J. Virol. , vol.64 , pp. 4697-4702
    • Kaplan, G.1    Freistadt, M.S.2    Racaniello, V.R.3
  • 23
    • 0024423373 scopus 로고
    • Modulation of cell surface heparan sulfate structure by growth of cells in the presence of chlorate
    • Keller, K. M., P. B. Brauer, and J. M. Keller. 1989. Modulation of cell surface heparan sulfate structure by growth of cells in the presence of chlorate. Biochemistry 28:8100-8107.
    • (1989) Biochemistry , vol.28 , pp. 8100-8107
    • Keller, K.M.1    Brauer, P.B.2    Keller, J.M.3
  • 24
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellen, L., and U. Lindahl. 1991. Proteoglycans: structures and interactions. Annu. Rev. Biochem. 60:443-475.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellen, L.1    Lindahl, U.2
  • 25
    • 0025687379 scopus 로고
    • Structural and functional properties of the 14-kDa envelope protein of vaccinia virus synthesized in Escherichia coli
    • Lai, C., S. Gong, and M. Esteban. 1990. Structural and functional properties of the 14-kDa envelope protein of vaccinia virus synthesized in Escherichia coli. J. Biol. Chem. 265:22174-22180.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22174-22180
    • Lai, C.1    Gong, S.2    Esteban, M.3
  • 28
    • 0027360382 scopus 로고
    • A heparin-binding activity on Leishmania amastigotes which mediates adhesion to cellular proteoglycans
    • Love, D. C., J. D. Esko, and D. M. Mosser. 1993. A heparin-binding activity on Leishmania amastigotes which mediates adhesion to cellular proteoglycans. J. Cell Biol. 123:759-766.
    • (1993) J. Cell Biol. , vol.123 , pp. 759-766
    • Love, D.C.1    Esko, J.D.2    Mosser, D.M.3
  • 29
    • 0024519677 scopus 로고
    • Cellular receptor for poliovirus: Molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily
    • Mendelsohn, C. L., E. Wimmer, and V. R. Racaniello. 1989. Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily. Cell 56:855-865.
    • (1989) Cell , vol.56 , pp. 855-865
    • Mendelsohn, C.L.1    Wimmer, E.2    Racaniello, V.R.3
  • 30
    • 0028316256 scopus 로고
    • Identification of binding sites for neutralizing monoclonal antibodies on the 14-kDa fusion protein of orthopox viruses
    • Meyer, H., N. Osterrieder, and C.-P. Czerny. 1994. Identification of binding sites for neutralizing monoclonal antibodies on the 14-kDa fusion protein of orthopox viruses. Virology 200:778-783.
    • (1994) Virology , vol.200 , pp. 778-783
    • Meyer, H.1    Osterrieder, N.2    Czerny, C.-P.3
  • 31
    • 0030298375 scopus 로고    scopus 로고
    • Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/ NGF receptor family
    • Montgomery, R. I., M. S. Warner, B. J. Lum, and P. G. Spear. 1996. Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/ NGF receptor family. Cell 87:427-36.
    • (1996) Cell , vol.87 , pp. 427-436
    • Montgomery, R.I.1    Warner, M.S.2    Lum, B.J.3    Spear, P.G.4
  • 33
    • 0023181906 scopus 로고
    • Virus attenuation and identification of structural proteins of vaccinia virus that are selectively modified during virus persistence
    • Paez, E., S. Dallo, and M. Esteban. 1987. Virus attenuation and identification of structural proteins of vaccinia virus that are selectively modified during virus persistence. J. Virol. 61:2642-2647.
    • (1987) J. Virol. , vol.61 , pp. 2642-2647
    • Paez, E.1    Dallo, S.2    Esteban, M.3
  • 35
    • 0029858908 scopus 로고    scopus 로고
    • Early events in poliovirus infection: Virus-receptor interactions
    • Racaniello, V. R. 1996. Early events in poliovirus infection: virus-receptor interactions. Proc. Natl. Acad. Sci. USA 93:11378-11381.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11378-11381
    • Racaniello, V.R.1
  • 36
    • 0026360861 scopus 로고
    • Virus-receptor interaction in poliovirus entry and pathogenesis
    • Racaniello, V. R. 1991. Virus-receptor interaction in poliovirus entry and pathogenesis. Harvey Lect. 87:1-16.
    • (1991) Harvey Lect. , vol.87 , pp. 1-16
    • Racaniello, V.R.1
  • 37
    • 0028319952 scopus 로고
    • Transgenic mice and the pathogenesis of poliomyelitis
    • Racaniello, V. R., and R. Ren. 1994. Transgenic mice and the pathogenesis of poliomyelitis. Arch. Virol. Suppl. 9:79-86.
    • (1994) Arch. Virol. Suppl. , vol.9 , pp. 79-86
    • Racaniello, V.R.1    Ren, R.2
  • 38
    • 0023162118 scopus 로고
    • Mapping and nucleotide sequence of the vaccinia virus gene that encodes a 14-kilodalton fusion protein
    • Rodriguez, J. F., and M. Esteban. 1987. Mapping and nucleotide sequence of the vaccinia virus gene that encodes a 14-kilodalton fusion protein. J. Virol. 61:3550-3554.
    • (1987) J. Virol. , vol.61 , pp. 3550-3554
    • Rodriguez, J.F.1    Esteban, M.2
  • 39
    • 0023164849 scopus 로고
    • r enveloped protein of vaccinia virus is involved in cell fusion and forms covalently linked trimers
    • r enveloped protein of vaccinia virus is involved in cell fusion and forms covalently linked trimers. J. Virol. 61:395-404.
    • (1987) J. Virol. , vol.61 , pp. 395-404
    • Rodriguez, J.F.1    Paez, E.2    Esteban, M.3
  • 41
    • 0024402592 scopus 로고
    • Proteoglycans in cell regulation
    • Ruoslahti, E. 1989. Proteoglycans in cell regulation. J. Biol. Chem. 264:13369-13372.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13369-13372
    • Ruoslahti, E.1
  • 42
    • 0028008650 scopus 로고
    • Herpesvirus-induced cell fusion that is dependent on cell surface heparan sulfate or soluble heparin
    • Shieh, M.-T., and P. G. Spear. 1994. Herpesvirus-induced cell fusion that is dependent on cell surface heparan sulfate or soluble heparin. J. Virol. 68:1224-1228.
    • (1994) J. Virol. , vol.68 , pp. 1224-1228
    • Shieh, M.-T.1    Spear, P.G.2
  • 43
    • 0026551062 scopus 로고
    • Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans
    • Shieh, M. T., D. WuDunn, R. I. Montgomery, J. D. Esko, and P. G. Spear. 1992. Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans. J. Cell Biol. 116:1273-1281.
    • (1992) J. Cell Biol. , vol.116 , pp. 1273-1281
    • Shieh, M.T.1    WuDunn, D.2    Montgomery, R.I.3    Esko, J.D.4    Spear, P.G.5
  • 44
    • 0029019920 scopus 로고
    • Assembly of vaccinia virus: Incorporalion of p14 and p32 into the membrane of the intracellular mature virus
    • Sodeik, B., S. Cudmore, M. Ericsson, M. Esteban, E. G. Niles, and G. Griffiths. 1995. Assembly of vaccinia virus: incorporalion of p14 and p32 into the membrane of the intracellular mature virus. J. Virol. 69:3560-3574.
    • (1995) J. Virol. , vol.69 , pp. 3560-3574
    • Sodeik, B.1    Cudmore, S.2    Ericsson, M.3    Esteban, M.4    Niles, E.G.5    Griffiths, G.6
  • 45
    • 0000929553 scopus 로고
    • Entry of alphaherpesviruses into cells
    • Spear, P. G. 1993. Entry of alphaherpesviruses into cells. Semin. Virol. 4:167-180.
    • (1993) Semin. Virol. , vol.4 , pp. 167-180
    • Spear, P.G.1
  • 46
    • 0026778580 scopus 로고
    • Heparan sulfate glycosaminoglycans as primary cell surface receptors for herpes simplex virus
    • Spear, P. G., M. T. Shieh, B. C. Herold, D. WuDunn, and T. I. Koshy. 1992. Heparan sulfate glycosaminoglycans as primary cell surface receptors for herpes simplex virus. Adv. Exp. Med. Biol. 313:341-353.
    • (1992) Adv. Exp. Med. Biol. , vol.313 , pp. 341-353
    • Spear, P.G.1    Shieh, M.T.2    Herold, B.C.3    WuDunn, D.4    Koshy, T.I.5
  • 47
    • 0028067316 scopus 로고
    • Swine testis cells contain functional heparan sulfate but are defective in entry of herpes simplex virus
    • Subramanian, G., D. S. McClain, A. Perez, and A. O. Fuller. 1994. Swine testis cells contain functional heparan sulfate but are defective in entry of herpes simplex virus. J. Virol. 68:5667-5676.
    • (1994) J. Virol. , vol.68 , pp. 5667-5676
    • Subramanian, G.1    McClain, D.S.2    Perez, A.3    Fuller, A.O.4
  • 48
    • 0030984273 scopus 로고    scopus 로고
    • A novel virus binding assay using confocal microscopy: Demonstration that the intracellular and extracellular vaccinia virions bind to different cellular receptors
    • Vanderplasschen, A., and G. L. Smith. 1997. A novel virus binding assay using confocal microscopy: demonstration that the intracellular and extracellular vaccinia virions bind to different cellular receptors. J. Virol. 71:4032-4041.
    • (1997) J. Virol. , vol.71 , pp. 4032-4041
    • Vanderplasschen, A.1    Smith, G.L.2
  • 49
    • 0029027169 scopus 로고
    • Binding of syndecan-like cell surface proteoglycan receptor is required for Neisseria gonorrhoeae entry into human mucosal cells
    • van Putten, J. P. M., and S. M. Paul. 1995. Binding of syndecan-like cell surface proteoglycan receptor is required for Neisseria gonorrhoeae entry into human mucosal cells. EMBO J. 14:2144-2154.
    • (1995) EMBO J. , vol.14 , pp. 2144-2154
    • Van Putten, J.P.M.1    Paul, S.M.2
  • 50
    • 0003600512 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Wimmer, E. 1994. Cellular receptors for animal viruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1994) Cellular Receptors for Animal Viruses
    • Wimmer, E.1
  • 51
    • 0024497174 scopus 로고
    • Initial interaction of herpes simplex virus with cells is binding to heparan sulfate
    • WuDunn, D., and P. G. Spear. 1989. Initial interaction of herpes simplex virus with cells is binding to heparan sulfate. J. Virol. 63:52-8.
    • (1989) J. Virol. , vol.63 , pp. 52-58
    • WuDunn, D.1    Spear, P.G.2
  • 52
    • 0029090119 scopus 로고
    • Sulfated polyanions block Chlamydia trachomatis infection of cervix-derived human epithelia
    • Zaretzky, F. R., R. Pearce-Pratt, and D. M. Phillips. 1995. Sulfated polyanions block Chlamydia trachomatis infection of cervix-derived human epithelia. Infect. Immun. 63:3520-3526.
    • (1995) Infect. Immun. , vol.63 , pp. 3520-3526
    • Zaretzky, F.R.1    Pearce-Pratt, R.2    Phillips, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.