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Volumn 87, Issue 19, 2013, Pages 10855-10873

Isolate-specific differences in the conformational dynamics and antigenicity of HIV-1 gp120

Author keywords

[No Author keywords available]

Indexed keywords

CD4 RECEPTOR; EPITOPE; GLYCOPROTEIN GP 120; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; LYMPHOCYTE ANTIGEN RECEPTOR; MONOCLONAL ANTIBODY; MONOMER; UNCLASSIFIED DRUG; VIRUS ANTIBODY; VIRUS ANTIGEN;

EID: 84886011849     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01535-13     Document Type: Article
Times cited : (28)

References (104)
  • 3
    • 0021924655 scopus 로고
    • Virus envelope protein of HTLV-III represents major target antigen for antibodies in AIDS patients
    • Barin F, McLane MF, Allan JS, Lee TH, Groopman JE, Essex M. 1985. Virus envelope protein of HTLV-III represents major target antigen for antibodies in AIDS patients. Science 228:1094-1096.
    • (1985) Science , vol.228 , pp. 1094-1096
    • Barin, F.1    McLane, M.F.2    Allan, J.S.3    Lee, T.H.4    Groopman, J.E.5    Essex, M.6
  • 4
    • 77951882041 scopus 로고    scopus 로고
    • Toward an antibody-based HIV-1 vaccine
    • Hoxie JA. 2010. Toward an antibody-based HIV-1 vaccine. Annu. Rev. Med. 61:135-152.
    • (2010) Annu. Rev. Med. , vol.61 , pp. 135-152
    • Hoxie, J.A.1
  • 6
    • 49149118421 scopus 로고    scopus 로고
    • Autologous neutralizing humoral immunity and evolution of the viral envelope in the course of subtype B human immunodeficiency virus type 1 infection
    • Bunnik EM, Pisas L, van Nuenen AC, Schuitemaker H. 2008. Autologous neutralizing humoral immunity and evolution of the viral envelope in the course of subtype B human immunodeficiency virus type 1 infection. J. Virol. 82:7932-7941.
    • (2008) J. Virol. , vol.82 , pp. 7932-7941
    • Bunnik, E.M.1    Pisas, L.2    van Nuenen, A.C.3    Schuitemaker, H.4
  • 7
    • 75849146082 scopus 로고    scopus 로고
    • Temporal analysis of HIV envelope sequence evolution and antibody escape in a subtype A-infected individual with a broad neutralizing antibody response
    • Bosch KA, Rainwater S, Jaoko W, Overbaugh J. 2010. Temporal analysis of HIV envelope sequence evolution and antibody escape in a subtype A-infected individual with a broad neutralizing antibody response. Virology 398:115-124.
    • (2010) Virology , vol.398 , pp. 115-124
    • Bosch, K.A.1    Rainwater, S.2    Jaoko, W.3    Overbaugh, J.4
  • 15
    • 0028073184 scopus 로고
    • Exploration of antigenic variation in gp120 from clades A through F of human immunodeficiency virus type 1 by using monoclonal antibodies
    • Moore JP, McCutchan FE, Poon SW, Mascola J, Liu J, Cao Y, Ho DD. 1994. Exploration of antigenic variation in gp120 from clades A through F of human immunodeficiency virus type 1 by using monoclonal antibodies. J. Virol. 68:8350-8364.
    • (1994) J. Virol. , vol.68 , pp. 8350-8364
    • Moore, J.P.1    McCutchan, F.E.2    Poon, S.W.3    Mascola, J.4    Liu, J.5    Cao, Y.6    Ho, D.D.7
  • 18
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. 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
  • 20
    • 27744597054 scopus 로고    scopus 로고
    • Structure of a V3-containing HIV-1 gp120 core
    • Huang CC. 2005. Structure of a V3-containing HIV-1 gp120 core. Science 310:1025-1028.
    • (2005) Science , vol.310 , pp. 1025-1028
    • Huang, C.C.1
  • 25
    • 77951939875 scopus 로고    scopus 로고
    • Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity
    • Diskin R, Marcovecchio PM, Bjorkman PJ. 2010. Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity. Nat. Struct. Mol. Biol. 17:608-613.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 608-613
    • Diskin, R.1    Marcovecchio, P.M.2    Bjorkman, P.J.3
  • 29
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease
    • Berger EA, Murphy PM, Farber JM. 1999. Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. Annu. Rev. Immunol. 17:657-700.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 31
    • 0035100868 scopus 로고    scopus 로고
    • Loss of a single N-linked glycan allows CD4-independent human immunodeficiency virus type 1 infection by altering the position of the gp120 V1/V2 variable loops
    • Kolchinsky P, Kiprilov E, Bartley P, Rubinstein R, Sodroski J. 2001. Loss of a single N-linked glycan allows CD4-independent human immunodeficiency virus type 1 infection by altering the position of the gp120 V1/V2 variable loops. J. Virol. 75:3435-3443.
    • (2001) J. Virol. , vol.75 , pp. 3435-3443
    • Kolchinsky, P.1    Kiprilov, E.2    Bartley, P.3    Rubinstein, R.4    Sodroski, J.5
  • 35
    • 0029119783 scopus 로고
    • Involvement of the 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 of the 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
  • 36
    • 33846552274 scopus 로고    scopus 로고
    • Role of V1V2 and other human immunodeficiency virus type 1 envelope domains in resistance to autologous neutralization during clade C infection
    • Rong R, Bibollet-Ruche F, Mulenga J, Allen S, Blackwell JL, Derdeyn CA. 2007. Role of V1V2 and other human immunodeficiency virus type 1 envelope domains in resistance to autologous neutralization during clade C infection. J. Virol. 81:1350-1359.
    • (2007) J. Virol. , vol.81 , pp. 1350-1359
    • Rong, R.1    Bibollet-Ruche, F.2    Mulenga, J.3    Allen, S.4    Blackwell, J.L.5    Derdeyn, C.A.6
  • 37
    • 2342644898 scopus 로고    scopus 로고
    • The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection
    • Pinter A, Honnen WJ, He Y, Gorny MK, Zolla-Pazner S, Kayman SC. 2004. The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection. J. Virol. 78:5205-5215.
    • (2004) J. Virol. , vol.78 , pp. 5205-5215
    • Pinter, A.1    Honnen, W.J.2    He, Y.3    Gorny, M.K.4    Zolla-Pazner, S.5    Kayman, S.C.6
  • 39
    • 77956819789 scopus 로고    scopus 로고
    • Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/ deuterium exchange
    • Kong L, Huang CC, Coales SJ, Molnar KS, Skinner J, Hamuro Y, Kwong PD. 2010. Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/ deuterium exchange. J. Virol. 84:10311-10321.
    • (2010) J. Virol. , vol.84 , pp. 10311-10321
    • Kong, L.1    Huang, C.C.2    Coales, S.J.3    Molnar, K.S.4    Skinner, J.5    Hamuro, Y.6    Kwong, P.D.7
  • 40
    • 84865066445 scopus 로고    scopus 로고
    • Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120
    • Guttman M, Kahn M, Garcia NK, Hu S-L, Lee KK. 2012. Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120. J. Virol. 86:8750-8764.
    • (2012) J. Virol. , vol.86 , pp. 8750-8764
    • Guttman, M.1    Kahn, M.2    Garcia, N.K.3    Hu, S.-L.4    Lee, K.K.5
  • 41
    • 84878477071 scopus 로고    scopus 로고
    • A mechanistic understanding of allosteric immune escape pathways in the HIV-1 envelope glycoprotein
    • Sethi A, Tian J, Derdeyn CA, Korber B, Gnanakaran S. 2013. A mechanistic understanding of allosteric immune escape pathways in the HIV-1 envelope glycoprotein. PLoS Comput. Biol. 9(5):e1003046.
    • (2013) PLoS Comput. Biol. , vol.9 , Issue.5
    • Sethi, A.1    Tian, J.2    Derdeyn, C.A.3    Korber, B.4    Gnanakaran, S.5
  • 42
    • 0012041487 scopus 로고
    • Isolates of human immunodeficiency virus type 1 from the brain may constitute a special group of the AIDS virus
    • Cheng-Mayer C, Weiss C, Seto D, Levy JA. 1989. Isolates of human immunodeficiency virus type 1 from the brain may constitute a special group of the AIDS virus. Proc. Natl. Acad. Sci. U.S.A. 86:8575-8579.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 8575-8579
    • Cheng-Mayer, C.1    Weiss, C.2    Seto, D.3    Levy, J.A.4
  • 43
    • 0021717961 scopus 로고
    • Molecular characterization of human T-cell leukemia (lymphotropic) virus type III in the acquired immune deficiency syndrome
    • Shaw GM, Hahn BH, Arya SK, Groopman JE, Gallo RC, Wong-Staal F. 1984. Molecular characterization of human T-cell leukemia (lymphotropic) virus type III in the acquired immune deficiency syndrome. Science 226:1165-1171.
    • (1984) Science , vol.226 , pp. 1165-1171
    • Shaw, G.M.1    Hahn, B.H.2    Arya, S.K.3    Groopman, J.E.4    Gallo, R.C.5    Wong-Staal, F.6
  • 44
    • 10044223604 scopus 로고    scopus 로고
    • Infectious molecular clone of a recently transmitted pediatric human immunodeficiency virus clade C isolate from Africa: evidence of intraclade recombination
    • Grisson RD, Chenine A-L, Yeh L-Y, He J, Wood C, Bhat GJ, Xu W, Kankasa C, Ruprecht RM. 2004. Infectious molecular clone of a recently transmitted pediatric human immunodeficiency virus clade C isolate from Africa: evidence of intraclade recombination. J. Virol. 78:14066-14069.
    • (2004) J. Virol. , vol.78 , pp. 14066-14069
    • Grisson, R.D.1    Chenine, A.-L.2    Yeh, L.-Y.3    He, J.4    Wood, C.5    Bhat, G.J.6    Xu, W.7    Kankasa, C.8    Ruprecht, R.M.9
  • 46
    • 77749311718 scopus 로고    scopus 로고
    • Bridging the solution divide: comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering
    • Rambo RP, Tainer JA. 2010. Bridging the solution divide: comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering. Curr. Opin. Struct. Biol. 20:128-137.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 128-137
    • Rambo, R.P.1    Tainer, J.A.2
  • 47
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution
    • Putnam CD, Hammel M, Hura GL, Tainer JA. 2007. X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q. Rev. Biophys. 40:191-285.
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 48
    • 0036816606 scopus 로고    scopus 로고
    • Advances in structure analysis using small-angle scattering in solution
    • Svergun DI, Koch MHJ. 2002. Advances in structure analysis using small-angle scattering in solution. Curr. Opin. Struct. Biol. 12:654-660.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 654-660
    • Svergun, D.I.1    Koch, M.H.J.2
  • 49
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: a historical perspective
    • Englander SW. 2006. Hydrogen exchange and mass spectrometry: a historical perspective. J. Am. Soc. Mass Spectrom. 17:1481-1489.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1481-1489
    • Englander, S.W.1
  • 50
    • 75749148378 scopus 로고    scopus 로고
    • Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry
    • Chapter:Unit-17.617. doi:10.1002/0471140864 .ps170s58.
    • Morgan CR, Engen JR. 2009. Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry. Curr. Protoc. Protein Sci. Chapter:Unit-17.617. doi:10.1002/0471140864 .ps170s58.
    • (2009) Curr. Protoc. Protein Sci.
    • Morgan, C.R.1    Engen, J.R.2
  • 51
    • 0025838698 scopus 로고
    • A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals
    • Burton DR, Barbas CF, Persson MA, Koenig S, Chanock RM, Lerner RA. 1991. A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals. Proc. Natl. Acad. Sci. U.S.A. 88: 10134-10137.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10134-10137
    • Burton, D.R.1    Barbas, C.F.2    Persson, M.A.3    Koenig, S.4    Chanock, R.M.5    Lerner, R.A.6
  • 53
    • 0028291731 scopus 로고
    • Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1
    • Roben P, Moore JP, Thali M, Sodroski J, Barbas CF, Burton DR. 1994. Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1. J. Virol. 68:4821-4828.
    • (1994) J. Virol. , vol.68 , pp. 4821-4828
    • Roben, P.1    Moore, J.P.2    Thali, M.3    Sodroski, J.4    Barbas, C.F.5    Burton, D.R.6
  • 55
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali M, Moore JP, Furman C, Charles M, Ho DD, Robinson J, Sodroski J. 1993. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67:3978-3988.
    • (1993) J. Virol. , vol.67 , pp. 3978-3988
    • Thali, M.1    Moore, J.P.2    Furman, C.3    Charles, M.4    Ho, D.D.5    Robinson, J.6    Sodroski, J.7
  • 59
    • 0027301670 scopus 로고
    • Immunochemical analysis of the gp120 surface glycoprotein of human immunodeficiency virus type 1: probing the structure of the C4 and V4 domains and the interaction of the C4 domain with the V3 loop
    • Moore JP, Thali M, Jameson BA, Vignaux F, Lewis GK, Poon SW, Charles M, Fung MS, Sun B, Durda PJ. 1993. Immunochemical analysis of the gp120 surface glycoprotein of human immunodeficiency virus type 1: probing the structure of the C4 and V4 domains and the interaction of the C4 domain with the V3 loop. J. Virol. 67:4785-4796.
    • (1993) J. Virol. , vol.67 , pp. 4785-4796
    • Moore, J.P.1    Thali, M.2    Jameson, B.A.3    Vignaux, F.4    Lewis, G.K.5    Poon, S.W.6    Charles, M.7    Fung, M.S.8    Sun, B.9    Durda, P.J.10
  • 64
    • 84878255015 scopus 로고    scopus 로고
    • Purification of recombinant vaccinia virus-expressed monomeric HIV-1 gp120 to apparent homogeneity
    • Guo W, Cleveland B, Davenport TM, Lee KK, Hu S-L. 2013. Purification of recombinant vaccinia virus-expressed monomeric HIV-1 gp120 to apparent homogeneity. Protein Expr. Purif. 90:34-39.
    • (2013) Protein Expr. Purif. , vol.90 , pp. 34-39
    • Guo, W.1    Cleveland, B.2    Davenport, T.M.3    Lee, K.K.4    Hu, S.-L.5
  • 65
    • 79954631167 scopus 로고    scopus 로고
    • False EX1 signatures caused by sample carryover during HX MS analyses
    • Fang J, Rand KD, Beuning PJ, Engen JR. 2011. False EX1 signatures caused by sample carryover during HX MS analyses. Int. J. Mass Spectrom. 302:19-25.
    • (2011) Int. J. Mass Spectrom. , vol.302 , pp. 19-25
    • Fang, J.1    Rand, K.D.2    Beuning, P.J.3    Engen, J.R.4
  • 66
    • 33751337111 scopus 로고    scopus 로고
    • Semi-automated data processing of hydrogen exchange mass spectra using HX-Express
    • Weis DD, Engen JR, Kass IJ. 2006. Semi-automated data processing of hydrogen exchange mass spectra using HX-Express. J. Am. Soc. Mass Spectrom. 17:1700-1703.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1700-1703
    • Weis, D.D.1    Engen, J.R.2    Kass, I.J.3
  • 67
    • 84862832993 scopus 로고    scopus 로고
    • Tracking hydrogen/deuterium exchange at glycan sites in glycoproteins by mass spectrometry
    • Guttman M, Scian M, Lee KK. 2011. Tracking hydrogen/deuterium exchange at glycan sites in glycoproteins by mass spectrometry. Anal. Chem. 83:7492-7499.
    • (2011) Anal. Chem. , vol.83 , pp. 7492-7499
    • Guttman, M.1    Scian, M.2    Lee, K.K.3
  • 69
    • 34248369857 scopus 로고    scopus 로고
    • Biological small-angle X-ray scattering facility at the Stanford Synchrotron Radiation Laboratory
    • Smolsky IL, Liu P, Niebuhr M, Ito K, Weiss TM, Tsuruta H. 2007. Biological small-angle X-ray scattering facility at the Stanford Synchrotron Radiation Laboratory. J. Appl. Crystallogr. 40:s453-s458.
    • (2007) J. Appl. Crystallogr. , vol.40
    • Smolsky, I.L.1    Liu, P.2    Niebuhr, M.3    Ito, K.4    Weiss, T.M.5    Tsuruta, H.6
  • 72
    • 35748982423 scopus 로고    scopus 로고
    • Analysis of X-ray and neutron scattering from biomacromolecular solutions
    • Petoukhov MV, Svergun DI. 2007. Analysis of X-ray and neutron scattering from biomacromolecular solutions. Curr. Opin. Struct. Biol. 17: 562-571.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 562-571
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 73
    • 0026243243 scopus 로고
    • Mathematical methods in small-angle scattering data analysis
    • Svergun DI. 1991. Mathematical methods in small-angle scattering data analysis. J. Appl. Crystallogr. 24:485-492.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 485-492
    • Svergun, D.I.1
  • 74
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI. 1992. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25:495-503.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 75
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun DI. 1999. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76:2879-2886.
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 76
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI. 2003. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36:860-864.
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 77
    • 77956190770 scopus 로고    scopus 로고
    • Structural characterization of proteins and complexes using small-angle X-ray solution scattering
    • Mertens HDT, Svergun DI. 2010. Structural characterization of proteins and complexes using small-angle X-ray solution scattering. J. Struct. Biol. 172:128-141.
    • (2010) J. Struct. Biol. , vol.172 , pp. 128-141
    • Mertens, H.D.T.1    Svergun, D.I.2
  • 78
    • 79958045453 scopus 로고    scopus 로고
    • Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law
    • Rambo RP, Tainer JA. 2011. Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law. Biopolymers 95:559-571.
    • (2011) Biopolymers , vol.95 , pp. 559-571
    • Rambo, R.P.1    Tainer, J.A.2
  • 81
    • 0016734961 scopus 로고
    • Antigenic structure of myoglobin: the complete immunochemical anatomy of a protein and conclusions relating to antigenic structures of proteins
    • Atassi MZ. 1975. Antigenic structure of myoglobin: the complete immunochemical anatomy of a protein and conclusions relating to antigenic structures of proteins. Immunochemistry 12:423-438.
    • (1975) Immunochemistry , vol.12 , pp. 423-438
    • Atassi, M.Z.1
  • 82
    • 1242338175 scopus 로고    scopus 로고
    • Expression and characterisation of recombinant oligomeric envelope glycoproteins derived from primary isolates of HIV-1
    • Jeffs SA, Goriup S, Kebble B, Crane D, Bolgiano B, Sattentau Q, Jones S, Holmes H. 2004. Expression and characterisation of recombinant oligomeric envelope glycoproteins derived from primary isolates of HIV-1. Vaccine 22:1032-1046.
    • (2004) Vaccine , vol.22 , pp. 1032-1046
    • Jeffs, S.A.1    Goriup, S.2    Kebble, B.3    Crane, D.4    Bolgiano, B.5    Sattentau, Q.6    Jones, S.7    Holmes, H.8
  • 86
    • 0030730243 scopus 로고    scopus 로고
    • Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein
    • Wyatt R, Desjardin E, Olshevsky U, Nixon C, Binley J, Olshevsky V, Sodroski J. 1997. Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein. J. Virol. 71:9722-9731.
    • (1997) J. Virol. , vol.71 , pp. 9722-9731
    • Wyatt, R.1    Desjardin, E.2    Olshevsky, U.3    Nixon, C.4    Binley, J.5    Olshevsky, V.6    Sodroski, J.7
  • 87
    • 0036436313 scopus 로고    scopus 로고
    • Characterization of CD4-induced epitopes on the HIV type 1 gp120 envelope glycoprotein recognized by neutralizing human monoclonal antibodies
    • Xiang S-H, Doka N, Choudhary RK, Sodroski J, Robinson JE. 2002. Characterization of CD4-induced epitopes on the HIV type 1 gp120 envelope glycoprotein recognized by neutralizing human monoclonal antibodies. AIDS Res. Hum. Retroviruses 18:1207-1217.
    • (2002) AIDS Res. Hum. Retroviruses , vol.18 , pp. 1207-1217
    • Xiang, S.-H.1    Doka, N.2    Choudhary, R.K.3    Sodroski, J.4    Robinson, J.E.5
  • 88
    • 84876862575 scopus 로고    scopus 로고
    • Allosteric modulation of the HIV-1 gp120-gp41 association site by adjacent gp120 variable region 1 (V1) N-glycans linked to neutralization sensitivity
    • doi:10 .1371/journal.ppat.1003218
    • Drummer HE, Hill MK, Maerz AL, Wood S, Ramsland PA, Mak J, Poumbourios P. 2013. Allosteric modulation of the HIV-1 gp120-gp41 association site by adjacent gp120 variable region 1 (V1) N-glycans linked to neutralization sensitivity. PLoS Pathog. 9(4):e1003218. doi:10 .1371/journal.ppat.1003218.
    • (2013) PLoS Pathog. , vol.9 , Issue.4
    • Drummer, H.E.1    Hill, M.K.2    Maerz, A.L.3    Wood, S.4    Ramsland, P.A.5    Mak, J.6    Poumbourios, P.7
  • 89
    • 84871641830 scopus 로고    scopus 로고
    • Structural plasticity and conformational transitions of HIV envelope glycoprotein gp120
    • doi:10.1371/journal.pone.0052170
    • Korkut A, Hendrickson WA. 2012. Structural plasticity and conformational transitions of HIV envelope glycoprotein gp120. PLoS One 7(12): e52170. doi:10.1371/journal.pone.0052170.
    • (2012) PLoS One , vol.7 , Issue.12
    • Korkut, A.1    Hendrickson, W.A.2
  • 96
    • 69549091679 scopus 로고    scopus 로고
    • Immunogenicity of HIV-1 envelope glycoprotein oligomers
    • Forsell MN, Schief WR, Wyatt RT. 2009. Immunogenicity of HIV-1 envelope glycoprotein oligomers. Curr. Opin. HIV AIDS 4:380-387.
    • (2009) Curr. Opin. HIV AIDS , vol.4 , pp. 380-387
    • Forsell, M.N.1    Schief, W.R.2    Wyatt, R.T.3
  • 97
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 virions induced by soluble CD4
    • Moore JP, McKeating JA, Weiss RA, Sattentau QJ. 1990. Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 250:1139-1142.
    • (1990) Science , vol.250 , pp. 1139-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 100
    • 37849026069 scopus 로고    scopus 로고
    • Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses
    • Li Y, Cleveland B, Klots I, Travis B, Richardson BA, Anderson D, Montefiori D, Polacino P, Hu SL. 2008. Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses. J. Virol. 82: 638-651.
    • (2008) J. Virol. , vol.82 , pp. 638-651
    • Li, Y.1    Cleveland, B.2    Klots, I.3    Travis, B.4    Richardson, B.A.5    Anderson, D.6    Montefiori, D.7    Polacino, P.8    Hu, S.L.9
  • 101
    • 0031025113 scopus 로고    scopus 로고
    • Macrophage tropism of human immunodeficiency virus type 1 and utilization of the CC-CKR5 coreceptor
    • Cheng-Mayer C, Liu R, Landau NR, Stamatatos L. 1997. Macrophage tropism of human immunodeficiency virus type 1 and utilization of the CC-CKR5 coreceptor. J. Virol. 71:1657-1661.
    • (1997) J. Virol. , vol.71 , pp. 1657-1661
    • Cheng-Mayer, C.1    Liu, R.2    Landau, N.R.3    Stamatatos, L.4
  • 103
    • 77949571338 scopus 로고    scopus 로고
    • Functional properties of the HIV-1 subtype C envelope glycoprotein associated with mother-to-child transmission
    • Zhang H, Rola M, West JT, Tully DC, Kubis P, He J, Kankasa C, Wood C. 2010. Functional properties of the HIV-1 subtype C envelope glycoprotein associated with mother-to-child transmission. Virology 400:164-174.
    • (2010) Virology , vol.400 , pp. 164-174
    • Zhang, H.1    Rola, M.2    West, J.T.3    Tully, D.C.4    Kubis, P.5    He, J.6    Kankasa, C.7    Wood, C.8
  • 104
    • 37848999666 scopus 로고    scopus 로고
    • The first hypervariable region of the gp120 Env glycoprotein defines the neutralizing susceptibility of heterologous human immunodeficiency virus type 1 isolates to neutralizing antibodies elicited by the SF162gp140 immunogen
    • Ching LK, Vlachogiannis G, Bosch KA, Stamatatos L. 2008. The first hypervariable region of the gp120 Env glycoprotein defines the neutralizing susceptibility of heterologous human immunodeficiency virus type 1 isolates to neutralizing antibodies elicited by the SF162gp140 immunogen. J. Virol. 82:949-956.
    • (2008) J. Virol. , vol.82 , pp. 949-956
    • Ching, L.K.1    Vlachogiannis, G.2    Bosch, K.A.3    Stamatatos, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.