메뉴 건너뛰기




Volumn 89, Issue 8, 2008, Pages 2011-2019

Binding of equine infectious anemia virus to the equine lentivirus receptor-1 is mediated by complex discontinuous sequences in the viral envelope gp90 protein

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; EQUINE LENTIVIRUS RECEPTOR 1; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; MUTANT PROTEIN; PEPTIDE; TUMOR NECROSIS FACTOR RECEPTOR; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; GLYCOPROTEIN; HERPESVIRUS ENTRY MEDIATOR; SU PROTEIN, EQUINE INFECTIOUS ANEMIA VIRUS; VIRUS RECEPTOR;

EID: 50549101569     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.83646-0     Document Type: Article
Times cited : (12)

References (46)
  • 2
    • 0034108828 scopus 로고    scopus 로고
    • Identification and characterization of a shared TNFR-related receptor for subgroup B, D, and E avian leukosis viruses reveal cysteine residues required specifically for subgroup E viral entry
    • Adkins, H. B., Brojatsch, J. & Young, J. A. (2000). Identification and characterization of a shared TNFR-related receptor for subgroup B, D, and E avian leukosis viruses reveal cysteine residues required specifically for subgroup E viral entry. J Virol 74, 3572-3578.
    • (2000) J Virol , vol.74 , pp. 3572-3578
    • Adkins, H.B.1    Brojatsch, J.2    Young, J.A.3
  • 3
    • 0026584749 scopus 로고
    • Detailed mapping of the antigenicity of the surface unit glycoprotein of equine infectious anemia virus by using synthetic peptide strategies
    • Ball, J. M., Rushlow, K. E., Issel, C. J. & Montelaro, R. C. (1992). Detailed mapping of the antigenicity of the surface unit glycoprotein of equine infectious anemia virus by using synthetic peptide strategies. J Virol 66, 732-74.
    • (1992) J Virol , vol.66 , pp. 732-774
    • Ball, J.M.1    Rushlow, K.E.2    Issel, C.J.3    Montelaro, R.C.4
  • 4
    • 29144449872 scopus 로고    scopus 로고
    • Avian sarcoma and leukosis virus-receptor interactions: From classical genetics to novel insights into virus-cell membrane fusion
    • Barnard, R. J., Elleder, D. & Young, J. A. (2006). Avian sarcoma and leukosis virus-receptor interactions: from classical genetics to novel insights into virus-cell membrane fusion. Virology 344, 25-29.
    • (2006) Virology , vol.344 , pp. 25-29
    • Barnard, R.J.1    Elleder, D.2    Young, J.A.3
  • 5
    • 0026608630 scopus 로고
    • Receptor choice determinants in the envelope glycoproteins of amphotropic, xenotropic, and polytropic murine leukemia viruses
    • Battini, J. L. Heard, J. M. & Danos. O. (1992). Receptor choice determinants in the envelope glycoproteins of amphotropic, xenotropic, and polytropic murine leukemia viruses. J Virol 66, 1468-1475.
    • (1992) J Virol , vol.66 , pp. 1468-1475
    • Battini, J.L.1    Heard, J.M.2    Danos, O.3
  • 6
    • 0028853990 scopus 로고
    • Receptor-binding domain of murine leukemia virus envelope glycoproteins
    • Battini, J. L., Danos, O. & Heard, J. M. (1995). Receptor-binding domain of murine leukemia virus envelope glycoproteins. J. Virol 69, 713-719.
    • (1995) J. Virol , vol.69 , pp. 713-719
    • Battini, J.L.1    Danos, O.2    Heard, J.M.3
  • 7
    • 0031985781 scopus 로고    scopus 로고
    • Definition of a 14-amino-acid peptide essential for the interaction between the murine leukemia virus amphotropic envelope glycoprotein and its receptor
    • Battini, J. L., Danos, O. & Heard, J. M. (1998). Definition of a 14-amino-acid peptide essential for the interaction between the murine leukemia virus amphotropic envelope glycoprotein and its receptor, J Virol 72, 428-435.
    • (1998) J Virol , vol.72 , pp. 428-435
    • Battini, J.L.1    Danos, O.2    Heard, J.M.3
  • 8
    • 0030606315 scopus 로고    scopus 로고
    • CAR1, a TNFR-related protein, is a cellular receptor for cytopathic avian leukosis-sarcoma viruses and mediates apoptosis
    • Brojatsch, J., Naughton, J, Rolls, M. M., Zingler, K. & Young, J. A. (1996). CAR1, a TNFR-related protein, is a cellular receptor for cytopathic avian leukosis-sarcoma viruses and mediates apoptosis. Cell 87, 845-855.
    • (1996) Cell , vol.87 , pp. 845-855
    • Brojatsch, J.1    Naughton, J.2    Rolls, M.M.3    Zingler, K.4    Young, J.A.5
  • 9
    • 0028212250 scopus 로고
    • Identification of functional regions of herpes simplex virus glycoprotein gD by using linker-insertion mutagenesis
    • Chiang, H. Y., Cohen, G. H. & Eisenberg, R. J. (1994). Identification of functional regions of herpes simplex virus glycoprotein gD by using linker-insertion mutagenesis. J Virol 68, 2529-2543.
    • (1994) J Virol , vol.68 , pp. 2529-2543
    • Chiang, H.Y.1    Cohen, G.H.2    Eisenberg, R.J.3
  • 10
    • 0036839118 scopus 로고    scopus 로고
    • Structure-based analysis of the herpes simplex virus glycoprotein D binding site present on herpesvirus entry mediator HveA (HVEM)
    • Connolly, S. A., Landsburg, D. J., Carfi, A., Wiley, D. C., Eisenberg, R. J. & Cohen, G. H. (2002). Structure-based analysis of the herpes simplex virus glycoprotein D binding site present on herpesvirus entry mediator HveA (HVEM). J. Virol 76, 10894-10904.
    • (2002) J. Virol , vol.76 , pp. 10894-10904
    • Connolly, S.A.1    Landsburg, D.J.2    Carfi, A.3    Wiley, D.C.4    Eisenberg, R.J.5    Cohen, G.H.6
  • 11
    • 0038758772 scopus 로고    scopus 로고
    • Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface
    • Connolly, S. A., Landsburg, D. J., Carfi, A., Wiley, D. C., Cohen, G. H. & Eisenberg, R. J. (2003). Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface. J Virol 77, 8127-8140.
    • (2003) J Virol , vol.77 , pp. 8127-8140
    • Connolly, S.A.1    Landsburg, D.J.2    Carfi, A.3    Wiley, D.C.4    Cohen, G.H.5    Eisenberg, R.J.6
  • 12
    • 0024416330 scopus 로고
    • Effects of mutations in hyperconserved regions of the extracellular glycoprotein of human immunodeficiency virus type 1 on receptor binding
    • Cordonnier, A., Riviere, Y., Montagnier, L. & Emerman, M. (1989). Effects of mutations in hyperconserved regions of the extracellular glycoprotein of human immunodeficiency virus type 1 on receptor binding. J Virol 63, 4464-4468.
    • (1989) J Virol , vol.63 , pp. 4464-4468
    • Cordonnier, A.1    Riviere, Y.2    Montagnier, L.3    Emerman, M.4
  • 14
    • 11444269806 scopus 로고    scopus 로고
    • Structural mapping of CD134 residues critical for interaction with feline immunodeficiency virus
    • de Parseval, A., Chatterji, U., Morris, G., Sun, P., Olson, A. J. & Elder, J. H. (2005). Structural mapping of CD134 residues critical for interaction with feline immunodeficiency virus. Nat Struct Mol Biol 12, 60-66.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 60-66
    • de Parseval, A.1    Chatterji, U.2    Morris, G.3    Sun, P.4    Olson, A.J.5    Elder, J.H.6
  • 15
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms, R. W., Lamb, R. A., Rose, J. K. & Helenius, A. (1993). Folding and assembly of viral membrane proteins. Virology 193, 545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 16
    • 0031576346 scopus 로고    scopus 로고
    • HIV/SIV glycoproteins: Structure-function relationships
    • Douglas, N. W., Munro, G. H. & Daniels, R. S. (1997). HIV/SIV glycoproteins: structure-function relationships. J Mol Biol 273, 122-149.
    • (1997) J Mol Biol , vol.273 , pp. 122-149
    • Douglas, N.W.1    Munro, G.H.2    Daniels, R.S.3
  • 17
    • 0027195996 scopus 로고
    • Characterization of a naturally occurring ecotropic receptor that does not facilitate entry of all ecotropic murine retroviruses
    • Eiden, M. V., Farrell, K., Warsowe, J., Mahan, L. C. & Wilson, C. A. (1993). Characterization of a naturally occurring ecotropic receptor that does not facilitate entry of all ecotropic murine retroviruses. J Virol 67, 4056-4061.
    • (1993) J Virol , vol.67 , pp. 4056-4061
    • Eiden, M.V.1    Farrell, K.2    Warsowe, J.3    Mahan, L.C.4    Wilson, C.A.5
  • 18
    • 0030820095 scopus 로고    scopus 로고
    • Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 Å resolution
    • Fass, D., Davey, R. A., Harrison, C. A., Kim, P. S., Cunningham, J. M. & Berger, J. M. (1997). Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 Å resolution. Science 277, 1662-1666.
    • (1997) Science , vol.277 , pp. 1662-1666
    • Fass, D.1    Davey, R.A.2    Harrison, C.A.3    Kim, P.S.4    Cunningham, J.M.5    Berger, J.M.6
  • 21
    • 17844392654 scopus 로고    scopus 로고
    • The ins and outs of HIV replication
    • Gomez, C. & Hope, T. J. (2005). The ins and outs of HIV replication. Cell Microbiol 7, 621-626.
    • (2005) Cell Microbiol , vol.7 , pp. 621-626
    • Gomez, C.1    Hope, T.J.2
  • 22
    • 0025861667 scopus 로고
    • An amino-terminal fragment of the Friend murine leukemia virus envelope glycoprotein binds the ecotropic receptor
    • Heard, J. M. & Danos, O. (1991). An amino-terminal fragment of the Friend murine leukemia virus envelope glycoprotein binds the ecotropic receptor. J Virol 65, 4026-4032.
    • (1991) J Virol , vol.65 , pp. 4026-4032
    • Heard, J.M.1    Danos, O.2
  • 23
    • 0023265817 scopus 로고
    • Antigenic analysis of equine infectious anemia virus (EIAV) variants by using monoclonal antibodies: Epitopes of glycoprotein gp90 of EIAV stimulate neutralizing antibodies
    • Hussain, K. A., Issel, C. J., Schnorr, K. L., Rwambo, P. M. & Montelaro, R. C. (1987). Antigenic analysis of equine infectious anemia virus (EIAV) variants by using monoclonal antibodies: epitopes of glycoprotein gp90 of EIAV stimulate neutralizing antibodies. J Virol 61, 2956-2961.
    • (1987) J Virol , vol.61 , pp. 2956-2961
    • Hussain, K.A.1    Issel, C.J.2    Schnorr, K.L.3    Rwambo, P.M.4    Montelaro, R.C.5
  • 24
    • 0023797230 scopus 로고
    • Antigenic mapping of the envelope proteins of equine infectious anemia virus: Identification of a neutralization domain and a conserved region on glycoprotein 90
    • Hussain, K. A., Issel, C. J., Schnorr, K. L., Rwambo, P. M., West, M. & Montelaro, R. C. (1988). Antigenic mapping of the envelope proteins of equine infectious anemia virus: identification of a neutralization domain and a conserved region on glycoprotein 90. Arch Virol 98, 213-224.
    • (1988) Arch Virol , vol.98 , pp. 213-224
    • Hussain, K.A.1    Issel, C.J.2    Schnorr, K.L.3    Rwambo, P.M.4    West, M.5    Montelaro, R.C.6
  • 25
    • 27744512883 scopus 로고    scopus 로고
    • Receptor-mediated entry by equine infectious anemia virus utilizes a pH-dependent endocytic pathway
    • Jin, S., Zhang, B. Weisz, O. A. & Montelaro, R. C. (2005). Receptor-mediated entry by equine infectious anemia virus utilizes a pH-dependent endocytic pathway. J Virol 79, 14489-14497.
    • (2005) J Virol , vol.79 , pp. 14489-14497
    • Jin, S.1    Zhang, B.2    Weisz, O.A.3    Montelaro, R.C.4
  • 26
    • 0022721628 scopus 로고
    • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface
    • Kreis, T. E. (1986). Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface. EMBO J 5, 931-941.
    • (1986) EMBO J , vol.5 , pp. 931-941
    • Kreis, T.E.1
  • 27
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, P. D., Wyatt, R., Robinson, J., Sweet, R. W., Sodroski, J. & Hendrickson, W. A. (1998). Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 28
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard, C. K., Spellman, M. W., Riddle, L., Harris, R. J., Thomas, J. N. & Gregory, T. J. (1990). Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J Biol Chem 265, 10373-10382.
    • (1990) J Biol Chem , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 29
    • 0030807901 scopus 로고    scopus 로고
    • Novel and dynamic evolution of equine infectious anemia virus genomic quasispecies associated with sequential disease cycles in an experimentally infected pony
    • Leroux, C., Issel, C. J. & Montelaro, R. C. (1997). Novel and dynamic evolution of equine infectious anemia virus genomic quasispecies associated with sequential disease cycles in an experimentally infected pony. J Virol 71, 9627-9639.
    • (1997) J Virol , vol.71 , pp. 9627-9639
    • Leroux, C.1    Issel, C.J.2    Montelaro, R.C.3
  • 30
    • 0035027217 scopus 로고    scopus 로고
    • Equine infectious anemia virus genomic evolution in progressor and nonprogressor ponies
    • Leroux, C., Craigo, J. K., Issel, C. J. & Montelaro, R. C. (2001). Equine infectious anemia virus genomic evolution in progressor and nonprogressor ponies. J Virol 75, 4570-4583.
    • (2001) J Virol , vol.75 , pp. 4570-4583
    • Leroux, C.1    Craigo, J.K.2    Issel, C.J.3    Montelaro, R.C.4
  • 31
    • 0023107134 scopus 로고
    • Computer-assisted analysis of envelope protein sequences of seven human immunodeficiency virus isolates: Prediction of antigenic epitopes in conserved and variable regions
    • Modrow, S., Hahn, B. H., Shaw, G. M., Gallo, R. C., Wong-Staal, F. & Wolf, H. (1987). Computer-assisted analysis of envelope protein sequences of seven human immunodeficiency virus isolates: prediction of antigenic epitopes in conserved and variable regions. J Virol 61, 570-578.
    • (1987) J Virol , vol.61 , pp. 570-578
    • Modrow, S.1    Hahn, B.H.2    Shaw, G.M.3    Gallo, R.C.4    Wong-Staal, F.5    Wolf, H.6
  • 32
    • 0021236382 scopus 로고
    • Antigenic variation during persistent infection by equine infectious anemia virus, a retrovirus
    • Montelaro, R. C., Parekh, B., Orrego, A. & Issel, C. J. (1984). Antigenic variation during persistent infection by equine infectious anemia virus, a retrovirus. J Biol Chem 259, 10539-10544.
    • (1984) J Biol Chem , vol.259 , pp. 10539-10544
    • Montelaro, R.C.1    Parekh, B.2    Orrego, A.3    Issel, C.J.4
  • 33
    • 0028107685 scopus 로고
    • Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies
    • Moore, J. P., Satkentau, O. J., Wyatt, R. & Sodroski, J. (1994). Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies. J Virol 68, 469-484.
    • (1994) J Virol , vol.68 , pp. 469-484
    • Moore, J.P.1    Satkentau, O.J.2    Wyatt, R.3    Sodroski, J.4
  • 34
    • 0027301667 scopus 로고
    • Analysis of the functional and host range-determining regions of the murine ecotropic and amphotropic retrovirus envelope proteins
    • Morgan, R. A., Nussbaum, O., Muenchau, D. D., Shu, L., Couture, L. & Anderson, W. F. (1993). Analysis of the functional and host range-determining regions of the murine ecotropic and amphotropic retrovirus envelope proteins. J Virol 67, 4712-4721.
    • (1993) J Virol , vol.67 , pp. 4712-4721
    • Morgan, R.A.1    Nussbaum, O.2    Muenchau, D.D.3    Shu, L.4    Couture, L.5    Anderson, W.F.6
  • 35
    • 0026627849 scopus 로고
    • Basis for receptor specificity of nonecotropic murine leukemia virus surface glycoprotein gp70SU
    • Ott D. & Rein, A. (1992). Basis for receptor specificity of nonecotropic murine leukemia virus surface glycoprotein gp70SU. J Virol 66, 4632-4638.
    • (1992) J Virol , vol.66 , pp. 4632-4638
    • Ott, D.1    Rein, A.2
  • 38
    • 0019415608 scopus 로고
    • Nucleotide sequences of the mRNAs encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions
    • Rose, J. K. & Gallione, C. J. (1981). Nucleotide sequences of the mRNAs encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions. J Virol 39, 519-528.
    • (1981) J Virol , vol.39 , pp. 519-528
    • Rose, J.K.1    Gallione, C.J.2
  • 40
    • 0037333420 scopus 로고    scopus 로고
    • Effect of amino acid substitution of the V3 and bridging sheet residues in human immunodeficiency virus type 1 subtype C gp120 on CCR5 utilization
    • Suphaphiphat, P., Thitithanyanont, A., Paca-Uccaralertkun, S., Essex, M. & Lee, T. H. (2003). Effect of amino acid substitution of the V3 and bridging sheet residues in human immunodeficiency virus type 1 subtype C gp120 on CCR5 utilization. J Virol 77, 3832-3837.
    • (2003) J Virol , vol.77 , pp. 3832-3837
    • Suphaphiphat, P.1    Thitithanyanont, A.2    Paca-Uccaralertkun, S.3    Essex, M.4    Lee, T.H.5
  • 41
    • 33847272713 scopus 로고    scopus 로고
    • Mutations in the V3 stem versus the V3 crown and C4 region have different effects on the binding and fusion steps of human immunodeficiency virus type 1 gp120 interaction with the CCR5 coreceptor
    • Suphaphiphat, P., Essex, M. & Lee, T. H. (2007). Mutations in the V3 stem versus the V3 crown and C4 region have different effects on the binding and fusion steps of human immunodeficiency virus type 1 gp120 interaction with the CCR5 coreceptor. Virology 360, 182-190.
    • (2007) Virology , vol.360 , pp. 182-190
    • Suphaphiphat, P.1    Essex, M.2    Lee, T.H.3
  • 42
    • 0029119783 scopus 로고
    • Involvement ofthe V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding
    • Wyatt, R., Moore, J., Accola, M., Desjardin, E., Robinson, J. & Sodroski, J. (1995). Involvement ofthe V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding. J Virol 69, 5723-5733.
    • (1995) J Virol , vol.69 , pp. 5723-5733
    • Wyatt, R.1    Moore, J.2    Accola, M.3    Desjardin, E.4    Robinson, J.5    Sodroski, J.6
  • 44
    • 22244474314 scopus 로고    scopus 로고
    • A tumor necrosis factor receptor family protein serves as a cellular receptor for the macrophage-tropic equine lentivirus
    • Zhang, B., Jin, S., Jin, J., Li, F. & Montelaro, R. C. (2005). A tumor necrosis factor receptor family protein serves as a cellular receptor for the macrophage-tropic equine lentivirus. Proc Natl Acad Sci U S A 102, 9918-9923.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 9918-9923
    • Zhang, B.1    Jin, S.2    Jin, J.3    Li, F.4    Montelaro, R.C.5
  • 45
    • 38349133685 scopus 로고    scopus 로고
    • Mapping of equine lentivirus receptor-1 residues critical for EIAV envelope binding
    • Zhang, B., Sun, C., Jin, S., Cascio, M. & Montelaro, R. C. (2008). Mapping of equine lentivirus receptor-1 residues critical for EIAV envelope binding. J Virol 82, 1204-1213.
    • (2008) J Virol , vol.82 , pp. 1204-1213
    • Zhang, B.1    Sun, C.2    Jin, S.3    Cascio, M.4    Montelaro, R.C.5
  • 46
    • 0030932629 scopus 로고    scopus 로고
    • Insertions, duplications and substitutions in restricted gp90 regions of equine infectious anaemia virus during febrile episodes in an experimentally infected horse
    • Zheng, Y. H., Nakaya, T., Sentsui, H., Kameoka, M., Kishi, M., Hagiwara, K., Takahashi, H., Kono, Y. & Ikuta, K. (1997). Insertions, duplications and substitutions in restricted gp90 regions of equine infectious anaemia virus during febrile episodes in an experimentally infected horse. J Gen Virol 78, 807-820.
    • (1997) J Gen Virol , vol.78 , pp. 807-820
    • Zheng, Y.H.1    Nakaya, T.2    Sentsui, H.3    Kameoka, M.4    Kishi, M.5    Hagiwara, K.6    Takahashi, H.7    Kono, Y.8    Ikuta, K.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.