메뉴 건너뛰기




Volumn 73, Issue 10, 1999, Pages 8127-8137

The first immunoglobulin-like domain of HveC is sufficient to bind herpes simplex virus gD with full affinity, while the third domain is involved in oligomerization of HveC

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN; MUTANT PROTEIN; PROTEIN C; VIRUS GLYCOPROTEIN;

EID: 0032826768     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.10.8127-8137.1999     Document Type: Article
Times cited : (116)

References (61)
  • 1
    • 0031572294 scopus 로고    scopus 로고
    • Mouse homolog of poliovirus receptor-related gene 2 product, mPRR2, mediates homophilic cell aggregation
    • Aoki, J., S. Koike, H. Asou, I, Ise, H. Suwa, T. Tanaka, M. Miyasaka, and A. Nomoto. 1997. Mouse homolog of poliovirus receptor-related gene 2 product, mPRR2, mediates homophilic cell aggregation. Exp. Cell Res. 235:374-384.
    • (1997) Exp. Cell Res. , vol.235 , pp. 374-384
    • Aoki, J.1    Koike, S.2    Asou, H.3    Ise, I.4    Suwa, H.5    Tanaka, T.6    Miyasaka, M.7    Nomoto, A.8
  • 2
    • 0031958412 scopus 로고    scopus 로고
    • Interaction of poliovirus with its purified receptor and conformational alteration in the virion
    • Arita, M., S. Koike, J. Aoki, H. Horie, and A. Nomoto. 1998. Interaction of poliovirus with its purified receptor and conformational alteration in the virion. J. Virol. 72:3578-3586.
    • (1998) J. Virol. , vol.72 , pp. 3578-3586
    • Arita, M.1    Koike, S.2    Aoki, J.3    Horie, H.4    Nomoto, A.5
  • 3
    • 0032516070 scopus 로고    scopus 로고
    • The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as LFA-1 integrin ligand
    • Bella, J., P. R. Kolatkar, C. W. Marlor, J. M. Greve, and M. G. Rossmann. 1998. The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as LFA-1 integrin ligand. Proc. Natl. Acad. Sci. USA 95:4140-4145.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4140-4145
    • Bella, J.1    Kolatkar, P.R.2    Marlor, C.W.3    Greve, J.M.4    Rossmann, M.G.5
  • 6
    • 0023878260 scopus 로고
    • Entry of herpes simplex virus 1 in BJ cells that constitutively express viral glycoprotein D is by endocytosis and results in degradation of the virus
    • Campadelli-Fiume, G., M. Arsenakis, F. Farabegoli, and B. Roizman. 1988. Entry of herpes simplex virus 1 in BJ cells that constitutively express viral glycoprotein D is by endocytosis and results in degradation of the virus. J. Virol. 62:159-167.
    • (1988) J. Virol. , vol.62 , pp. 159-167
    • Campadelli-Fiume, G.1    Arsenakis, M.2    Farabegoli, F.3    Roizman, B.4
  • 7
    • 0031747204 scopus 로고    scopus 로고
    • The domain structure of ICAM-1 and the kinetics of binding to rhinovirus
    • Casasnovas, J. M., J. K. Bickford, and T. A. Springer. 1998. The domain structure of ICAM-1 and the kinetics of binding to rhinovirus. J. Virol. 72:6244-6246.
    • (1998) J. Virol. , vol.72 , pp. 6244-6246
    • Casasnovas, J.M.1    Bickford, J.K.2    Springer, T.A.3
  • 8
    • 0032516060 scopus 로고    scopus 로고
    • A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1
    • Casasnovas, J. M., T. Stehle, J. H. Liu, J. H. Wang, and T. A. Springer. 1998. A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1. Proc. Natl. Acad. Sci. USA 95:4134-4139.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4134-4139
    • Casasnovas, J.M.1    Stehle, T.2    Liu, J.H.3    Wang, J.H.4    Springer, T.A.5
  • 9
    • 0032446355 scopus 로고    scopus 로고
    • The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein D
    • Cocchi, F., M. Lopez, L. Menotti, M. Aoubala, P. Dubreuil, and G. Campadelli-Fiume. 1998. The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein D. Proc. Natl. Acad. Sci. USA 95:15700-15705.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15700-15705
    • Cocchi, F.1    Lopez, M.2    Menotti, L.3    Aoubala, M.4    Dubreuil, P.5    Campadelli-Fiume, G.6
  • 10
    • 0031797729 scopus 로고    scopus 로고
    • The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attribute of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells
    • Cocchi, F., L. Menotti, P. Mirandola, M. Lopez, and G. Campadelli-Fiume. 1998. The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attribute of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells. J. Virol. 72:9992-10002.
    • (1998) J. Virol. , vol.72 , pp. 9992-10002
    • Cocchi, F.1    Menotti, L.2    Mirandola, P.3    Lopez, M.4    Campadelli-Fiume, G.5
  • 11
    • 0022498630 scopus 로고
    • Localization of discontinuous epitopes of herpes simplex virus glycoprotein D: Use of a nondenaturing ("native" gel) system of polyacrylamide gel electrophoresis coupled with Western blotting
    • Cohen, G. H., V. J. Isola, J. Kuhns, P. W. Berman, and R. J. Eisenberg. 1986. Localization of discontinuous epitopes of herpes simplex virus glycoprotein D: use of a nondenaturing ("native" gel) system of polyacrylamide gel electrophoresis coupled with Western blotting. J. Virol. 60:157-166.
    • (1986) J. Virol. , vol.60 , pp. 157-166
    • Cohen, G.H.1    Isola, V.J.2    Kuhns, J.3    Berman, P.W.4    Eisenberg, R.J.5
  • 12
  • 13
    • 0028245995 scopus 로고
    • Single amino acid substitutions in gD of herpes simplex virus 1 confer resistance to gD-mediated interference and cause cell-type-dependent alterations in infectivity
    • Dean, H. J., S. S. Terhune, M. Shieh, N. Susmarski, and P. G. Spear. 1994. Single amino acid substitutions in gD of herpes simplex virus 1 confer resistance to gD-mediated interference and cause cell-type-dependent alterations in infectivity. Virology 199:67-80.
    • (1994) Virology , vol.199 , pp. 67-80
    • Dean, H.J.1    Terhune, S.S.2    Shieh, M.3    Susmarski, N.4    Spear, P.G.5
  • 15
    • 0029048729 scopus 로고
    • The human PRR2 gene, related to the poliovirus receptor gene (PVR), is the true homolog of the murine MPH gene
    • Eberlé, F., P. Dubreuil, M.-G. Mattei, E. Devilard, and M. Lopez. 1995. The human PRR2 gene, related to the poliovirus receptor gene (PVR), is the true homolog of the murine MPH gene. Gene 159:267-272.
    • (1995) Gene , vol.159 , pp. 267-272
    • Eberlé, F.1    Dubreuil, P.2    Mattei, M.-G.3    Devilard, E.4    Lopez, M.5
  • 16
    • 0032902878 scopus 로고    scopus 로고
    • Coxsackievirus and adenovirus receptor amino-terminal immunoglobulin V-related domain binds adenovirus type 2 and fiber knob from adenovirus type 12
    • Freimuth, P., K. Springer, C. Berard, J. Hainfeld, M. Bewley, and J. Fianagan. 1999. Coxsackievirus and adenovirus receptor amino-terminal immunoglobulin V-related domain binds adenovirus type 2 and fiber knob from adenovirus type 12. J. Virol. 73:1392-1398.
    • (1999) J. Virol. , vol.73 , pp. 1392-1398
    • Freimuth, P.1    Springer, K.2    Berard, C.3    Hainfeld, J.4    Bewley, M.5    Fianagan, J.6
  • 17
    • 0026772030 scopus 로고
    • Herpes simplex virus type 1 entry through a cascade of virus-cell interactions requires different roles of gD and gH in penetration
    • Fuller, A. O., and W. C. Lee. 1992. Herpes simplex virus type 1 entry through a cascade of virus-cell interactions requires different roles of gD and gH in penetration. J. Virol. 66:5002-12.
    • (1992) J. Virol. , vol.66 , pp. 5002-5012
    • Fuller, A.O.1    Lee, W.C.2
  • 18
    • 0032486317 scopus 로고    scopus 로고
    • Entry of alphaherpesviruses mediated by poliovirus receptor related protein 1 and poliovirus receptor
    • Geraghty, R. J., C. Krummenacher, R. J. Eisenberg, G. H. Cohen, and P. G. Spear. 1998. Entry of alphaherpesviruses mediated by poliovirus receptor related protein 1 and poliovirus receptor. Science 280:1618-1620.
    • (1998) Science , vol.280 , pp. 1618-1620
    • Geraghty, R.J.1    Krummenacher, C.2    Eisenberg, R.J.3    Cohen, G.H.4    Spear, P.G.5
  • 21
    • 0029817292 scopus 로고    scopus 로고
    • Crosslinking of glycoprotein oligomers during herpes simplex virus type 1 entry
    • Handler, C. G., G. H. Cohen, and R. J. Eisenberg. 1996. Crosslinking of glycoprotein oligomers during herpes simplex virus type 1 entry. J. Virol. 70:6076-6082.
    • (1996) J. Virol. , vol.70 , pp. 6076-6082
    • Handler, C.G.1    Cohen, G.H.2    Eisenberg, R.J.3
  • 22
    • 0029841218 scopus 로고    scopus 로고
    • Oligomeric structure of glycoproteins in herpes simplex virus type 1
    • Handler, C. G., R. J. Eisenberg, and G. H. Cohen. 1996. Oligomeric structure of glycoproteins in herpes simplex virus type 1. J. Virol. 70:6067-6075.
    • (1996) J. Virol. , vol.70 , pp. 6067-6075
    • Handler, C.G.1    Eisenberg, R.J.2    Cohen, G.H.3
  • 23
    • 0028236443 scopus 로고
    • Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulfate and glycoprotein B
    • Herold, B. C., R. J. Visalli, N. Sumarski, C. Brandt, and P. G. Spear. 1994 Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulfate and glycoprotein B. J. Gen. Virol. 75:1211-1222.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1211-1222
    • Herold, B.C.1    Visalli, R.J.2    Sumarski, N.3    Brandt, C.4    Spear, P.G.5
  • 24
    • 0030920262 scopus 로고    scopus 로고
    • ATAR, a novel tumor necrosis factor receptor family member, signals through TRAF2 and TRAF5
    • Hsu, S., I. Solovyev, A. Colombero, R. Elliott, M. Kelley, and W, J. Boyle. 1997. ATAR, a novel tumor necrosis factor receptor family member, signals through TRAF2 and TRAF5. J. Biol. Chem. 272:13471-13474.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13471-13474
    • Hsu, S.1    Solovyev, I.2    Colombero, A.3    Elliott, R.4    Kelley, M.5    Boyle, W.J.6
  • 26
    • 0025294236 scopus 로고
    • Soluble forms of herpes simplex virus glycoprotein D bind to a limited number of cell surface receptors and inhibit virus entry into cells
    • Johnson, D. C., R. L. Burke, and T. Gregory. 1990. Soluble forms of herpes simplex virus glycoprotein D bind to a limited number of cell surface receptors and inhibit virus entry into cells. J. Virol. 64:2569-2576.
    • (1990) J. Virol. , vol.64 , pp. 2569-2576
    • Johnson, D.C.1    Burke, R.L.2    Gregory, T.3
  • 27
    • 0024502639 scopus 로고
    • Herpes simplex virus glycoprotein D mediates interference with herpes simplex virus infection
    • Johnson, R. M., and P. G. Spear. 1989. Herpes simplex virus glycoprotein D mediates interference with herpes simplex virus infection. J. Virol. 63:819-827.
    • (1989) J. Virol. , vol.63 , pp. 819-827
    • Johnson, R.M.1    Spear, P.G.2
  • 29
    • 0031820802 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry
    • Krummenacher, C., A. V. Nicola, J. C. Whitbeck, H. Lou, W. Hou, J. D. Lambris, R. J. Geraghry, P. G. Spear, G. H. Cohen, and R. J. Eisenberg. 1998. Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry. J. Virol. 72:7064-7074.
    • (1998) J. Virol. , vol.72 , pp. 7064-7074
    • Krummenacher, C.1    Nicola, A.V.2    Whitbeck, J.C.3    Lou, H.4    Hou, W.5    Lambris, J.D.6    Geraghry, R.J.7    Spear, P.G.8    Cohen, G.H.9    Eisenberg, R.J.10
  • 30
    • 0025193736 scopus 로고
    • The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector
    • Kuroda, K., H. Geyer, R. Geyer, W. Doerfler, and H.-D. Klenk. 1990. The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector. Virology 174:418-429.
    • (1990) Virology , vol.174 , pp. 418-429
    • Kuroda, K.1    Geyer, H.2    Geyer, R.3    Doerfler, W.4    Klenk, H.-D.5
  • 32
    • 0023878973 scopus 로고
    • The envelope glycoprotein of the human immunodeficiency virus binds to the immunoglobulin-like domain of CD4
    • Landau, N. R., M. Warton, and D. R. Littman. 1988. The envelope glycoprotein of the human immunodeficiency virus binds to the immunoglobulin-like domain of CD4. Nature 334:159-162.
    • (1988) Nature , vol.334 , pp. 159-162
    • Landau, N.R.1    Warton, M.2    Littman, D.R.3
  • 33
    • 0032534991 scopus 로고    scopus 로고
    • The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule
    • Lopez, M., M. Aoubala, F. Jordier, D. Isnardon, S. Gomez, and P. Dubreuil. 1998. The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule. Blood 92:4602-4611.
    • (1998) Blood , vol.92 , pp. 4602-4611
    • Lopez, M.1    Aoubala, M.2    Jordier, F.3    Isnardon, D.4    Gomez, S.5    Dubreuil, P.6
  • 34
    • 0028925875 scopus 로고
    • Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene
    • Lopez, M., F. Eberlé, M.-G. Mattei, J. Gabert, F. Birg, F. Bardin, C. Maroc, and P. Dubreuil. 1995. Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene. Gene 155:261-265.
    • (1995) Gene , vol.155 , pp. 261-265
    • Lopez, M.1    Eberlé, F.2    Mattei, M.-G.3    Gabert, J.4    Birg, F.5    Bardin, F.6    Maroc, C.7    Dubreuil, P.8
  • 35
    • 0001939434 scopus 로고    scopus 로고
    • CD 155 workshop: Identification of a new class of IgG superfamily antigens expressed in hematopoiesis
    • I. Garland Publishing (ed.). Garland Publishing, London, England
    • Lopez, M., F. Eberlé, M. G. Mattei, J. Gabert, F. Birg, F. Bardin, C. Maroc, and P. Dubreuil. 1997. CD 155 Workshop: identification of a new class of IgG superfamily antigens expressed in hematopoiesis, p. 1081-1083. In I. Garland Publishing (ed.), Leukocyte typing VI, white cells differentiation antigens. I. Garland Publishing, London, England.
    • (1997) Leukocyte Typing VI, White Cells Differentiation Antigens , vol.1 , pp. 1081-1083
    • Lopez, M.1    Eberlé, F.2    Mattei, M.G.3    Gabert, J.4    Birg, F.5    Bardin, F.6    Maroc, C.7    Dubreuil, P.8
  • 36
    • 0027211815 scopus 로고
    • Efficient neutralization and disruption of rhinovirus by chimeric ICAM-1/immunoglobulin molecules
    • Martin, S., J. M. Casasnovas, D. E. Staunton, and T. A. Springer. 1993. Efficient neutralization and disruption of rhinovirus by chimeric ICAM-1/immunoglobulin molecules. J. Virol. 67:3561-3568.
    • (1993) J. Virol. , vol.67 , pp. 3561-3568
    • Martin, S.1    Casasnovas, J.M.2    Staunton, D.E.3    Springer, T.A.4
  • 38
    • 0025887767 scopus 로고
    • Identification of monoclonal antibody epitopes and critical residues for rhinovirus binding in domain 1 of intercellular adhesion molecule 1
    • McClelland, A., J. DeBear, S. C. Yost, A. M. Meyer, C. W. Marlor, and J. M. Greve. 1991. Identification of monoclonal antibody epitopes and critical residues for rhinovirus binding in domain 1 of intercellular adhesion molecule 1. Proc. Natl. Acad. Sci. USA 88:7993-7997.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7993-7997
    • McClelland, A.1    DeBear, J.2    Yost, S.C.3    Meyer, A.M.4    Marlor, C.W.5    Greve, J.M.6
  • 39
    • 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
  • 40
    • 0024273639 scopus 로고
    • Binding region for human immunodeficiency virus (HIV) and epitopes for HIV-blocking monoclonal antibodies of the CD4 molecule defined by site-directed mutagenesis
    • Mizukami, T., T. R. Fuerst, E. A, Berger, and B. Moss. 1988. Binding region for human immunodeficiency virus (HIV) and epitopes for HIV-blocking monoclonal antibodies of the CD4 molecule defined by site-directed mutagenesis. Proc. Natl. Acad. Sci. USA 85:9273-9277.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9273-9277
    • Mizukami, T.1    Fuerst, T.R.2    Berger, E.A.3    Moss, B.4
  • 41
    • 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 87:427-436.
    • (1996) Cell , vol.87 , pp. 427-436
    • Montgomery, R.I.1    Warner, M.S.2    Lum, B.J.3    Spear, P.G.4
  • 42
    • 0028214691 scopus 로고
    • Homolog-scanning mutagenesis reveals poliovirus receptor residues important for virus binding and replication
    • Morrison, M. E., Y.-J. He, M. W. Wien, J. M. Hogle, and V. Racaniello. 1994. Homolog-scanning mutagenesis reveals poliovirus receptor residues important for virus binding and replication. J. Virol. 68:2578-2588.
    • (1994) J. Virol. , vol.68 , pp. 2578-2588
    • Morrison, M.E.1    He, Y.-J.2    Wien, M.W.3    Hogle, J.M.4    Racaniello, V.5
  • 43
    • 0030945466 scopus 로고    scopus 로고
    • Antigenic structure of soluble herpes simplex virus glycoprotein D correlates with inhibition of HSV infection
    • Nicola, A. V., C. Peng, H. Lou, G. H. Cohen, and R. J. Eisenberg. 1997. Antigenic structure of soluble herpes simplex virus glycoprotein D correlates with inhibition of HSV infection. J. Virol. 71:2940-2946.
    • (1997) J. Virol. , vol.71 , pp. 2940-2946
    • Nicola, A.V.1    Peng, C.2    Lou, H.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 45
    • 0030007655 scopus 로고    scopus 로고
    • Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D
    • Nicola, A. V., S. H. Willis, N. N. Naidoo, R. J. Eisenberg, and G. H. Cohen. 1996. Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D. J. Virol. 70:3815-3822.
    • (1996) J. Virol. , vol.70 , pp. 3815-3822
    • Nicola, A.V.1    Willis, S.H.2    Naidoo, N.N.3    Eisenberg, R.J.4    Cohen, G.H.5
  • 46
    • 0029945538 scopus 로고    scopus 로고
    • Disulfide bond structure determination and biochemical analysis of glycoprotein C from herpes simplex virus
    • Rux, A. H., W. T. Moore, J. D. Lambris, W. R. Abrams, C. Peng, H. M. Friedman, G. H. Cohen, and R. J. Eisenberg. 1996. Disulfide bond structure determination and biochemical analysis of glycoprotein C from herpes simplex virus. J. Virol. 70:5455-5465.
    • (1996) J. Virol. , vol.70 , pp. 5455-5465
    • Rux, A.H.1    Moore, W.T.2    Lambris, J.D.3    Abrams, W.R.4    Peng, C.5    Friedman, H.M.6    Cohen, G.H.7    Eisenberg, R.J.8
  • 47
    • 0031868961 scopus 로고    scopus 로고
    • Functional region IV of glycoprotein D from herpes simplex virus modulates glycoprotein binding to the herpes virus entry mediator
    • Rux, A. H., S. H. Willis, A. V. Nicola, W. Hou, C. Peng, H. Lou, G. H. Cohen, and R. J. Eisenberg. 1998. Functional region IV of glycoprotein D from herpes simplex virus modulates glycoprotein binding to the herpes virus entry mediator. J. Virol. 72:7091-7098.
    • (1998) J. Virol. , vol.72 , pp. 7091-7098
    • Rux, A.H.1    Willis, S.H.2    Nicola, A.V.3    Hou, W.4    Peng, C.5    Lou, H.6    Cohen, G.H.7    Eisenberg, R.J.8
  • 48
    • 0027954404 scopus 로고
    • High-level expression and purification of secreted forms of herpes simplex virus type 1 glycoprotein gD synthesized by baculovirus-infected insect cells
    • Sisk, W. P., J. D. Bradley, R. J. Leipold, A. M. Stoltzfus, M. Ponce de Leon, M. Hilf, C. Peng, G. H. Cohen, and R. J. Eisenberg. 1994. High-level expression and purification of secreted forms of herpes simplex virus type 1 glycoprotein gD synthesized by baculovirus-infected insect cells. J. Virol. 68:766-775.
    • (1994) J. Virol. , vol.68 , pp. 766-775
    • Sisk, W.P.1    Bradley, J.D.2    Leipold, R.J.3    Stoltzfus, A.M.4    Ponce De Leon, M.5    Hilf, M.6    Peng, C.7    Cohen, G.H.8    Eisenberg, R.J.9
  • 49
    • 0002109061 scopus 로고
    • Membrane fusion induced by herpes simplex virus
    • In J. Bentz (ed.). CRC Press, Inc., Boca Raton, Fla.
    • Spear, P. G. 1993. Membrane fusion induced by herpes simplex virus, p. 201-232. In J. Bentz (ed.), Viral fusion mechanisms. CRC Press, Inc., Boca Raton, Fla.
    • (1993) Viral Fusion Mechanisms , pp. 201-232
    • Spear, P.G.1
  • 50
    • 0025269047 scopus 로고
    • The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus
    • Staunton, D. E., M. L. Dustin, H. P. Erickson, and T. A. Springer. 1990. The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus. Cell 61:243-254.
    • (1990) Cell , vol.61 , pp. 243-254
    • Staunton, D.E.1    Dustin, M.L.2    Erickson, H.P.3    Springer, T.A.4
  • 52
    • 0033519211 scopus 로고    scopus 로고
    • Nectin/PRR: An immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with afadin, a PDZ domain-containing protein
    • Takahashi, K., H. Nakanishi, M. Miyahara, K. Mandai, K. Satoh, A. Satoh, H. Nishioka, J. Aoki, A. Nomoto, A. Mizoguchi, and Y. Takai. 1999. Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with afadin, a PDZ domain-containing protein. J. Cell Biol. 145:539-549.
    • (1999) J. Cell Biol. , vol.145 , pp. 539-549
    • Takahashi, K.1    Nakanishi, H.2    Miyahara, M.3    Mandai, K.4    Satoh, K.5    Satoh, A.6    Nishioka, H.7    Aoki, J.8    Nomoto, A.9    Mizoguchi, A.10    Takai, Y.11
  • 53
    • 0031776458 scopus 로고    scopus 로고
    • HveA (herpesvirus entry mediator A), a coreceptor for herpes simplex virus entry, also participates in virus-induced cell fusion
    • Terry-Allison, T., R. I. Montgomery, J. C. Whitbeck, R. Xu, G. H. Cohen, R. J. Eisenberg, and P. G. Spear. 1998. HveA (herpesvirus entry mediator A), a coreceptor for herpes simplex virus entry, also participates in virus-induced cell fusion. J. Virol. 72:5802-5810.
    • (1998) J. Virol. , vol.72 , pp. 5802-5810
    • Terry-Allison, T.1    Montgomery, R.I.2    Whitbeck, J.C.3    Xu, R.4    Cohen, G.H.5    Eisenberg, R.J.6    Spear, P.G.7
  • 55
    • 0032551272 scopus 로고    scopus 로고
    • A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by herpes simplex virus type 2, mutants of herpes simplex virus type 1 and pseudorabies virus
    • Warner, M. S., W. Martinez, R. J. Geraghty, R. I. Montgomery, J. C. Whitbeck, R. Xu, R. J. Eisenberg, G. H. Cohen, and P. G. Spear. 1998. A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by herpes simplex virus type 2, mutants of herpes simplex virus type 1 and pseudorabies virus. Virology 246:179-189.
    • (1998) Virology , vol.246 , pp. 179-189
    • Warner, M.S.1    Martinez, W.2    Geraghty, R.J.3    Montgomery, R.I.4    Whitbeck, J.C.5    Xu, R.6    Eisenberg, R.J.7    Cohen, G.H.8    Spear, P.G.9
  • 57
    • 0025352657 scopus 로고
    • Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a non-functional, homologous protein in MHV-resistant SJL/J mice
    • Williams, R. K., G.-S. Jiang, S. W. Snyder, M. F. Frana, and K. V. Holmes. 1990. Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a non-functional, homologous protein in MHV-resistant SJL/J mice. J. Virol. 64: 3817-3823.
    • (1990) J. Virol. , vol.64 , pp. 3817-3823
    • Williams, R.K.1    Jiang, G.-S.2    Snyder, S.W.3    Frana, M.F.4    Holmes, K.V.5
  • 58
    • 0001205935 scopus 로고    scopus 로고
    • Expression and purification of secreted forms of HSV glycoproteins from baculovirus-infected insect cells
    • S. M. Brown and A. R. MacLean (ed.). Herpes simplex virus protocols. Humana Press, Inc., Totowa, N.J.
    • Willis, S. H., C. Peng, M. Ponce de Leon, A. V. Nicola, A. H. Rux, G. H. Cohen, and R. J. Eisenberg. 1998. Expression and purification of secreted forms of HSV glycoproteins from baculovirus-infected insect cells, p. 131-156. In S. M. Brown and A. R. MacLean (ed.), Methods in molecular medicine, vol. 10. Herpes simplex virus protocols. Humana Press, Inc., Totowa, N.J.
    • (1998) Methods in Molecular Medicine , vol.10 , pp. 131-156
    • Willis, S.H.1    Peng, C.2    Ponce De Leon, M.3    Nicola, A.V.4    Rux, A.H.5    Cohen, G.H.6    Eisenberg, R.J.7
  • 59
    • 0031777344 scopus 로고    scopus 로고
    • Examination of the kinetics of herpes simplex virus glycoprotein D binding to the herpesvirus entry mediator, using surface plasmon resonance
    • Willis, S. H., A. H. Rux, C. Peng, J. C. Whitbeck, A. V. Nicola, H. Lou, W. Hou, L. Salvador, G. H. Cohen, and R. J. Eisenberg. 1998. Examination of the kinetics of herpes simplex virus glycoprotein D binding to the herpesvirus entry mediator, using surface plasmon resonance. J. Virol. 72:5937-5947.
    • (1998) J. Virol. , vol.72 , pp. 5937-5947
    • Willis, S.H.1    Rux, A.H.2    Peng, C.3    Whitbeck, J.C.4    Nicola, A.V.5    Lou, H.6    Hou, W.7    Salvador, L.8    Cohen, G.H.9    Eisenberg, R.J.10
  • 60
    • 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. 63:52-58.
    • (1989) J. Virol. , vol.63 , pp. 52-58
    • WuDunn, D.1    Spear, P.G.2
  • 61
    • 0031816799 scopus 로고    scopus 로고
    • Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1b, and Bgp2 murine coronavirus receptors differ in mouse hepatitis binding and neutralizing activities
    • Zelus, B. D., D. R. Wessner, R. K. Williams, M. N. Pensiero, F. T. Phibbs, M. DeSouza, G. D. Dveksler, and K. V. Holmes. 1998 Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1b, and Bgp2 murine coronavirus receptors differ in mouse hepatitis binding and neutralizing activities. J. Virol. 72:7237-7244.
    • (1998) J. Virol. , vol.72 , pp. 7237-7244
    • Zelus, B.D.1    Wessner, D.R.2    Williams, R.K.3    Pensiero, M.N.4    Phibbs, F.T.5    DeSouza, M.6    Dveksler, G.D.7    Holmes, K.V.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.