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Volumn 11, Issue 1, 2014, Pages

Differential glycosylation of envelope gp120 is associated with differential recognition of HIV-1 by virus-specific antibodies and cell infection

Author keywords

Deglycosylation resistance; Glycan specific antibody; gp120 glycosylation; Neutralization inhibition

Indexed keywords

CD4 ANTIGEN; EPITOPE; GLYCAN; GLYCOPROTEIN GP 120; MANNOSE OLIGOSACCHARIDE; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; POLYCLONAL ANTIBODY; RECOMBINANT GLYCOPROTEIN GP 120; VIRUS ANTIBODY;

EID: 84905817200     PISSN: None     EISSN: 17426405     Source Type: Journal    
DOI: 10.1186/1742-6405-11-23     Document Type: Article
Times cited : (30)

References (106)
  • 1
    • 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. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998, 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
  • 3
    • 33646146379 scopus 로고    scopus 로고
    • Gp120: target for neutralizing HIV-1 antibodies
    • Pantophlet R, Burton DR. gp120: target for neutralizing HIV-1 antibodies. Annu Rev Immunol 2006, 24:739-769.
    • (2006) Annu Rev Immunol , vol.24 , pp. 739-769
    • Pantophlet, R.1    Burton, D.R.2
  • 7
    • 0031790121 scopus 로고    scopus 로고
    • Role of cellular adhesion molecules in HIV type 1 infection and their impact on virus neutralization
    • Hioe CE, Bastiani L, Hildreth JE, Zolla-Pazner S. Role of cellular adhesion molecules in HIV type 1 infection and their impact on virus neutralization. AIDS Res Hum Retroviruses 1998, 14(Suppl 3):S247-S254.
    • (1998) AIDS Res Hum Retroviruses , vol.14 , pp. S247-S254
    • Hioe, C.E.1    Bastiani, L.2    Hildreth, J.E.3    Zolla-Pazner, S.4
  • 8
    • 0033541477 scopus 로고    scopus 로고
    • Enhanced HIV type 1 neutralization by human anti-glycoprotein 120 monoclonal antibodies in the presence of monoclonal antibodies to lymphocyte function-associated molecule 1
    • Hioe CE, Hildreth JE, Zolla-Pazner S. Enhanced HIV type 1 neutralization by human anti-glycoprotein 120 monoclonal antibodies in the presence of monoclonal antibodies to lymphocyte function-associated molecule 1. AIDS Res Hum Retroviruses 1999, 15:523-531.
    • (1999) AIDS Res Hum Retroviruses , vol.15 , pp. 523-531
    • Hioe, C.E.1    Hildreth, J.E.2    Zolla-Pazner, S.3
  • 12
    • 69149083668 scopus 로고    scopus 로고
    • Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine?
    • Stamatatos L, Morris L, Burton DR, Mascola JR. Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine?. Nat Med 2009, 15:866-870.
    • (2009) Nat Med , vol.15 , pp. 866-870
    • Stamatatos, L.1    Morris, L.2    Burton, D.R.3    Mascola, J.R.4
  • 13
    • 43749123908 scopus 로고    scopus 로고
    • 25 years of HIV
    • Fauci AS. 25 years of HIV. Nature 2008, 453:289-290.
    • (2008) Nature , vol.453 , pp. 289-290
    • Fauci, A.S.1
  • 14
    • 27144525215 scopus 로고    scopus 로고
    • Targeting the glycans of gp120: a novel approach aimed at the Achilles heel of HIV
    • Balzarini J. Targeting the glycans of gp120: a novel approach aimed at the Achilles heel of HIV. Lancet Infect Dis 2005, 5:726-731.
    • (2005) Lancet Infect Dis , vol.5 , pp. 726-731
    • Balzarini, J.1
  • 16
    • 36148973173 scopus 로고    scopus 로고
    • HIV/AIDS vaccines: 2007
    • Robinson HL. HIV/AIDS vaccines: 2007. Clin Pharmacol Ther 2007, 82:686-693.
    • (2007) Clin Pharmacol Ther , vol.82 , pp. 686-693
    • Robinson, H.L.1
  • 17
    • 0034687168 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells
    • Zhu X, Borchers C, Bienstock RJ, Tomer KB. Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells. Biochemistry 2000, 39:11194-11204.
    • (2000) Biochemistry , vol.39 , pp. 11194-11204
    • Zhu, X.1    Borchers, C.2    Bienstock, R.J.3    Tomer, K.B.4
  • 20
    • 77953028154 scopus 로고    scopus 로고
    • Involvement of envelope-glycoprotein glycans in HIV-1 biology and infection
    • Raska M, Novak J. Involvement of envelope-glycoprotein glycans in HIV-1 biology and infection. Arch Immunol Ther Exp (Warsz) 2010, 58:191-208.
    • (2010) Arch Immunol Ther Exp (Warsz) , vol.58 , pp. 191-208
    • Raska, M.1    Novak, J.2
  • 22
    • 0025374887 scopus 로고
    • Diversity of oligosaccharide structures on the envelope glycoprotein gp120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N-acetylglucosamine residues
    • Mizuochi T, Matthews TJ, Kato M, Hamako J, Titani K, Solomon J, Feizi T. Diversity of oligosaccharide structures on the envelope glycoprotein gp120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N-acetylglucosamine residues. J Biol Chem 1990, 265:8519-8524.
    • (1990) J Biol Chem , vol.265 , pp. 8519-8524
    • Mizuochi, T.1    Matthews, T.J.2    Kato, M.3    Hamako, J.4    Titani, K.5    Solomon, J.6    Feizi, T.7
  • 23
    • 0024232268 scopus 로고
    • Structural characterization by chromatographic profiling of the oligosaccharides of human immunodeficiency virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese hamster ovary cells
    • Mizuochi T, Spellman MW, Larkin M, Solomon J, Basa LJ, Feizi T. Structural characterization by chromatographic profiling of the oligosaccharides of human immunodeficiency virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese hamster ovary cells. Biomed Chromatogr 1988, 2:260-270.
    • (1988) Biomed Chromatogr , vol.2 , pp. 260-270
    • Mizuochi, T.1    Spellman, M.W.2    Larkin, M.3    Solomon, J.4    Basa, L.J.5    Feizi, T.6
  • 24
    • 0023807495 scopus 로고
    • Carbohydrate structures of the human-immunodeficiency-virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese-hamster ovary cells
    • Mizuochi T, Spellman MW, Larkin M, Solomon J, Basa LJ, Feizi T. Carbohydrate structures of the human-immunodeficiency-virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese-hamster ovary cells. Biochem J 1988, 254:599-603.
    • (1988) Biochem J , vol.254 , pp. 599-603
    • Mizuochi, T.1    Spellman, M.W.2    Larkin, M.3    Solomon, J.4    Basa, L.J.5    Feizi, T.6
  • 25
    • 0031749469 scopus 로고    scopus 로고
    • A role for carbohydrates in immune evasion in AIDS
    • Reitter JN, Means RE, Desrosiers RC. A role for carbohydrates in immune evasion in AIDS. Nat Med 1998, 4:679-684.
    • (1998) Nat Med , vol.4 , pp. 679-684
    • Reitter, J.N.1    Means, R.E.2    Desrosiers, R.C.3
  • 26
    • 0031748799 scopus 로고    scopus 로고
    • Identification of replication-competent strains of simian immunodeficiency virus lacking multiple attachment sites for N-linked carbohydrates in variable regions 1 and 2 of the surface envelope protein
    • Reitter JN, Desrosiers RC. Identification of replication-competent strains of simian immunodeficiency virus lacking multiple attachment sites for N-linked carbohydrates in variable regions 1 and 2 of the surface envelope protein. J Virol 1998, 72:5399-5407.
    • (1998) J Virol , vol.72 , pp. 5399-5407
    • Reitter, J.N.1    Desrosiers, R.C.2
  • 28
    • 45549101708 scopus 로고    scopus 로고
    • Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility
    • Go EP, Irungu J, Zhang Y, Dalpathado DS, Liao HX, Sutherland LL, Alam SM, Haynes BF, Desaire H. Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility. J Proteome Res 2008, 7:1660-1674.
    • (2008) J Proteome Res , vol.7 , pp. 1660-1674
    • Go, E.P.1    Irungu, J.2    Zhang, Y.3    Dalpathado, D.S.4    Liao, H.X.5    Sutherland, L.L.6    Alam, S.M.7    Haynes, B.F.8    Desaire, H.9
  • 29
    • 0035173908 scopus 로고    scopus 로고
    • HIV-1 receptors and cell tropism
    • Clapham PR, McKnight A. HIV-1 receptors and cell tropism. Br Med Bull 2001, 58:43-59.
    • (2001) Br Med Bull , vol.58 , pp. 43-59
    • Clapham, P.R.1    McKnight, A.2
  • 30
    • 79251526530 scopus 로고    scopus 로고
    • HIV-1 envelope, integrins and co-receptor use in mucosal transmission of HIV
    • Cicala C, Arthos J, Fauci AS. HIV-1 envelope, integrins and co-receptor use in mucosal transmission of HIV. J Transl Med 2011, 9(Suppl 1):S2.
    • (2011) J Transl Med , vol.9 , pp. S2
    • Cicala, C.1    Arthos, J.2    Fauci, A.S.3
  • 33
    • 0035918220 scopus 로고    scopus 로고
    • N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization
    • Pollakis G, Kang S, Kliphuis A, Chalaby MI, Goudsmit J, Paxton WA. N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization. J Biol Chem 2001, 276:13433-13441.
    • (2001) J Biol Chem , vol.276 , pp. 13433-13441
    • Pollakis, G.1    Kang, S.2    Kliphuis, A.3    Chalaby, M.I.4    Goudsmit, J.5    Paxton, W.A.6
  • 34
    • 1842562419 scopus 로고    scopus 로고
    • N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies
    • McCaffrey RA, Saunders C, Hensel M, Stamatatos L. N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies. J Virol 2004, 78:3279-3295.
    • (2004) J Virol , vol.78 , pp. 3279-3295
    • McCaffrey, R.A.1    Saunders, C.2    Hensel, M.3    Stamatatos, L.4
  • 35
    • 33644609596 scopus 로고    scopus 로고
    • CCR5 use by human immunodeficiency virus type 1 is associated closely with the gp120 V3 loop N-linked glycosylation site
    • Clevestig P, Pramanik L, Leitner T, Ehrnst A. CCR5 use by human immunodeficiency virus type 1 is associated closely with the gp120 V3 loop N-linked glycosylation site. J Gen Virol 2006, 87:607-612.
    • (2006) J Gen Virol , vol.87 , pp. 607-612
    • Clevestig, P.1    Pramanik, L.2    Leitner, T.3    Ehrnst, A.4
  • 36
    • 33748881797 scopus 로고    scopus 로고
    • N-Glycans in the gp120 V1/V2 domain of the HIV-1 strain NL4-3 are indispensable for viral infectivity and resistance against antibody neutralization
    • Wolk T, Schreiber M. N-Glycans in the gp120 V1/V2 domain of the HIV-1 strain NL4-3 are indispensable for viral infectivity and resistance against antibody neutralization. Med Microbiol Immunol 2006, 195:165-172.
    • (2006) Med Microbiol Immunol , vol.195 , pp. 165-172
    • Wolk, T.1    Schreiber, M.2
  • 37
    • 84855343161 scopus 로고    scopus 로고
    • Highly conserved HIV-1 gp120 glycans proximal to CD4-binding region affect viral infectivity and neutralizing antibody induction
    • Huang X, Jin W, Hu K, Luo S, Du T, Griffin GE, Shattock RJ, Hu Q. Highly conserved HIV-1 gp120 glycans proximal to CD4-binding region affect viral infectivity and neutralizing antibody induction. Virology 2012, 423:97-106.
    • (2012) Virology , vol.423 , pp. 97-106
    • Huang, X.1    Jin, W.2    Hu, K.3    Luo, S.4    Du, T.5    Griffin, G.E.6    Shattock, R.J.7    Hu, Q.8
  • 40
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • Doores KJ, Burton DR. Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. J Virol 2010, 84:10510-10521.
    • (2010) J Virol , vol.84 , pp. 10510-10521
    • Doores, K.J.1    Burton, D.R.2
  • 43
    • 84861208332 scopus 로고    scopus 로고
    • Kinetic mechanism for HIV-1 neutralization by antibody 2G12 entails reversible glycan binding that slows cell entry
    • Platt EJ, Gomes MM, Kabat D. Kinetic mechanism for HIV-1 neutralization by antibody 2G12 entails reversible glycan binding that slows cell entry. Proc Natl Acad Sci U S A 2012, 109:7829-7834.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 7829-7834
    • Platt, E.J.1    Gomes, M.M.2    Kabat, D.3
  • 51
    • 0026356679 scopus 로고
    • Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the human immunodeficiency virus type 1 envelope glycoprotein
    • Gorny MK, Xu JY, Gianakakos V, Karwowska S, Williams C, Sheppard HW, Hanson CV, Zolla-Pazner S. Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the human immunodeficiency virus type 1 envelope glycoprotein. Proc Natl Acad Sci U S A 1991, 88:3238-3242.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3238-3242
    • Gorny, M.K.1    Xu, J.Y.2    Gianakakos, V.3    Karwowska, S.4    Williams, C.5    Sheppard, H.W.6    Hanson, C.V.7    Zolla-Pazner, S.8
  • 52
    • 34250027638 scopus 로고    scopus 로고
    • Analysis of the neutralization breadth of the anti-V3 antibody F425-B4e8 and re-assessment of its epitope fine specificity by scanning mutagenesis
    • Pantophlet R, Aguilar-Sino RO, Wrin T, Cavacini LA, Burton DR. Analysis of the neutralization breadth of the anti-V3 antibody F425-B4e8 and re-assessment of its epitope fine specificity by scanning mutagenesis. Virology 2007, 364:441-453.
    • (2007) Virology , vol.364 , pp. 441-453
    • Pantophlet, R.1    Aguilar-Sino, R.O.2    Wrin, T.3    Cavacini, L.A.4    Burton, D.R.5
  • 54
    • 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. 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 1991, 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
  • 55
    • 59649125573 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 envelope spike of primary viruses can suppress antibody access to variable regions
    • Pantophlet R, Wang M, Aguilar-Sino RO, Burton DR. The human immunodeficiency virus type 1 envelope spike of primary viruses can suppress antibody access to variable regions. J Virol 2009, 83:1649-1659.
    • (2009) J Virol , vol.83 , pp. 1649-1659
    • Pantophlet, R.1    Wang, M.2    Aguilar-Sino, R.O.3    Burton, D.R.4
  • 57
    • 84867427047 scopus 로고    scopus 로고
    • Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA
    • Julien JP, Lee PS, Wilson IA. Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA. Immunol Rev 2012, 250:180-198.
    • (2012) Immunol Rev , vol.250 , pp. 180-198
    • Julien, J.P.1    Lee, P.S.2    Wilson, I.A.3
  • 59
    • 44849108137 scopus 로고    scopus 로고
    • Identification of an N-linked glycosylation in the C4 region of HIV-1 envelope gp120 that is critical for recognition of neighboring CD4 T cell epitopes
    • Li H, Chien PC, Tuen M, Visciano ML, Cohen S, Blais S, Xu CF, Zhang HT, Hioe CE. Identification of an N-linked glycosylation in the C4 region of HIV-1 envelope gp120 that is critical for recognition of neighboring CD4 T cell epitopes. J Immunol 2008, 180:4011-4021.
    • (2008) J Immunol , vol.180 , pp. 4011-4021
    • Li, H.1    Chien, P.C.2    Tuen, M.3    Visciano, M.L.4    Cohen, S.5    Blais, S.6    Xu, C.F.7    Zhang, H.T.8    Hioe, C.E.9
  • 61
    • 0030804546 scopus 로고    scopus 로고
    • Glycosylation affects both the three-dimensional structure and antibody binding properties of the HIV-1IIIB GP120 peptide RP135
    • Huang X, Barchi JJ, Lung FD, Roller PP, Nara PL, Muschik J, Garrity RR. Glycosylation affects both the three-dimensional structure and antibody binding properties of the HIV-1IIIB GP120 peptide RP135. Biochemistry 1997, 36:10846-10856.
    • (1997) Biochemistry , vol.36 , pp. 10846-10856
    • Huang, X.1    Barchi, J.J.2    Lung, F.D.3    Roller, P.P.4    Nara, P.L.5    Muschik, J.6    Garrity, R.R.7
  • 67
    • 84861986980 scopus 로고    scopus 로고
    • HIV vaccine development: challenges and opportunities towards solving the HIV vaccine-neutralizing antibody problem
    • Koff WC. HIV vaccine development: challenges and opportunities towards solving the HIV vaccine-neutralizing antibody problem. Vaccine 2012, 30:4310-4315.
    • (2012) Vaccine , vol.30 , pp. 4310-4315
    • Koff, W.C.1
  • 69
    • 84873255997 scopus 로고    scopus 로고
    • A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization
    • Wang W, Nie J, Prochnow C, Truong C, Jia Z, Wang S, Chen XS, Wang Y. A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization. Retrovirology 2013, 10:14.
    • (2013) Retrovirology , vol.10 , pp. 14
    • Wang, W.1    Nie, J.2    Prochnow, C.3    Truong, C.4    Jia, Z.5    Wang, S.6    Chen, X.S.7    Wang, Y.8
  • 70
    • 0027311936 scopus 로고
    • Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120
    • Gorny MK, Xu JY, Karwowska S, Buchbinder A, Zolla-Pazner S. Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120. J Immunol 1993, 150:635-643.
    • (1993) J Immunol , vol.150 , pp. 635-643
    • Gorny, M.K.1    Xu, J.Y.2    Karwowska, S.3    Buchbinder, A.4    Zolla-Pazner, S.5
  • 72
    • 1242351232 scopus 로고    scopus 로고
    • Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D
    • Stanfield RL, Gorny MK, Williams C, Zolla-Pazner S, Wilson IA. Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D. Structure 2004, 12:193-204.
    • (2004) Structure , vol.12 , pp. 193-204
    • Stanfield, R.L.1    Gorny, M.K.2    Williams, C.3    Zolla-Pazner, S.4    Wilson, I.A.5
  • 73
    • 70350714115 scopus 로고    scopus 로고
    • Structural basis of the cross-reactivity of genetically related human anti-HIV-1 mAbs: implications for design of V3-based immunogens
    • Burke V, Williams C, Sukumaran M, Kim SS, Li H, Wang XH, Gorny MK, Zolla-Pazner S, Kong XP. Structural basis of the cross-reactivity of genetically related human anti-HIV-1 mAbs: implications for design of V3-based immunogens. Structure 2009, 17:1538-1546.
    • (2009) Structure , vol.17 , pp. 1538-1546
    • Burke, V.1    Williams, C.2    Sukumaran, M.3    Kim, S.S.4    Li, H.5    Wang, X.H.6    Gorny, M.K.7    Zolla-Pazner, S.8    Kong, X.P.9
  • 74
    • 0028908782 scopus 로고
    • A human monoclonal antibody to a complex epitope in the V3 region of gp120 of human immunodeficiency virus type 1 has broad reactivity within and outside clade B
    • Moore JP, Trkola A, Korber B, Boots LJ, Kessler JA, McCutchan FE, Mascola J, Ho DD, Robinson J, Conley AJ. A human monoclonal antibody to a complex epitope in the V3 region of gp120 of human immunodeficiency virus type 1 has broad reactivity within and outside clade B. J Virol 1995, 69:122-130.
    • (1995) J Virol , vol.69 , pp. 122-130
    • Moore, J.P.1    Trkola, A.2    Korber, B.3    Boots, L.J.4    Kessler, J.A.5    McCutchan, F.E.6    Mascola, J.7    Ho, D.D.8    Robinson, J.9    Conley, A.J.10
  • 80
    • 70350320690 scopus 로고    scopus 로고
    • Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment
    • Wu X, Zhou T, O'Dell S, Wyatt RT, Kwong PD, Mascola JR. Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment. J Virol 2009, 83:10892-10907.
    • (2009) J Virol , vol.83 , pp. 10892-10907
    • Wu, X.1    Zhou, T.2    O'Dell, S.3    Wyatt, R.T.4    Kwong, P.D.5    Mascola, J.R.6
  • 83
    • 77957189612 scopus 로고    scopus 로고
    • Antibody 2G12 recognizes di-mannose equivalently in domain- and nondomain-exchanged forms but only binds the HIV-1 glycan shield if domain exchanged
    • Doores KJ, Fulton Z, Huber M, Wilson IA, Burton DR. Antibody 2G12 recognizes di-mannose equivalently in domain- and nondomain-exchanged forms but only binds the HIV-1 glycan shield if domain exchanged. J Virol 2010, 84:10690-10699.
    • (2010) J Virol , vol.84 , pp. 10690-10699
    • Doores, K.J.1    Fulton, Z.2    Huber, M.3    Wilson, I.A.4    Burton, D.R.5
  • 84
    • 79958086672 scopus 로고    scopus 로고
    • Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected
    • Crooks ET, Tong T, Osawa K, Binley JM. Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected. J Virol 2011, 85:5825-5839.
    • (2011) J Virol , vol.85 , pp. 5825-5839
    • Crooks, E.T.1    Tong, T.2    Osawa, K.3    Binley, J.M.4
  • 85
    • 0034469405 scopus 로고    scopus 로고
    • Resistance of native, oligomeric envelope on simian immunodeficiency virus to digestion by glycosidases
    • Means RE, Desrosiers RC. Resistance of native, oligomeric envelope on simian immunodeficiency virus to digestion by glycosidases. J Virol 2000, 74:11181-11190.
    • (2000) J Virol , vol.74 , pp. 11181-11190
    • Means, R.E.1    Desrosiers, R.C.2
  • 87
    • 0027535672 scopus 로고
    • Glycosylation is necessary for the correct folding of human immunodeficiency virus gp120 in CD4 binding
    • Li Y, Luo L, Rasool N, Kang CY. Glycosylation is necessary for the correct folding of human immunodeficiency virus gp120 in CD4 binding. J Virol 1993, 67:584-588.
    • (1993) J Virol , vol.67 , pp. 584-588
    • Li, Y.1    Luo, L.2    Rasool, N.3    Kang, C.Y.4
  • 89
    • 0030450295 scopus 로고    scopus 로고
    • Conserved N-linked oligosaccharides of the C-terminal portion of human immunodeficiency virus type 1 gp120 and viral susceptibility to neutralizing antibodies
    • Hemming A, Gram GJ, Bolmstedt A, Losman B, Hansen JE, Ricksten A, Olofsson S. Conserved N-linked oligosaccharides of the C-terminal portion of human immunodeficiency virus type 1 gp120 and viral susceptibility to neutralizing antibodies. Arch Virol 1996, 141:2139-2151.
    • (1996) Arch Virol , vol.141 , pp. 2139-2151
    • Hemming, A.1    Gram, G.J.2    Bolmstedt, A.3    Losman, B.4    Hansen, J.E.5    Ricksten, A.6    Olofsson, S.7
  • 94
    • 13944254982 scopus 로고    scopus 로고
    • Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection
    • Flynn NM, Forthal DN, Harro CD, Judson FN, Mayer KH, Para MF. Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection. J Infect Dis 2005, 191:654-665.
    • (2005) J Infect Dis , vol.191 , pp. 654-665
    • Flynn, N.M.1    Forthal, D.N.2    Harro, C.D.3    Judson, F.N.4    Mayer, K.H.5    Para, M.F.6
  • 98
    • 33645381510 scopus 로고    scopus 로고
    • Decline in sexually transmitted infection prevalence and HIV incidence in female barworkers attending prevention and care services in Mbeya Region, Tanzania
    • Riedner G, Hoffmann O, Rusizoka M, Mmbando D, Maboko L, Grosskurth H, Todd J, Hayes R, Hoelscher M. Decline in sexually transmitted infection prevalence and HIV incidence in female barworkers attending prevention and care services in Mbeya Region, Tanzania. Aids 2006, 20:609-615.
    • (2006) Aids , vol.20 , pp. 609-615
    • Riedner, G.1    Hoffmann, O.2    Rusizoka, M.3    Mmbando, D.4    Maboko, L.5    Grosskurth, H.6    Todd, J.7    Hayes, R.8    Hoelscher, M.9
  • 102
    • 38949115679 scopus 로고    scopus 로고
    • Neutralizing antibodies in mucosal secretions: IgG or IgA?
    • Alexander R, Mestecky J. Neutralizing antibodies in mucosal secretions: IgG or IgA?. Curr HIV Res 2007, 5:588-593.
    • (2007) Curr HIV Res , vol.5 , pp. 588-593
    • Alexander, R.1    Mestecky, J.2
  • 104
    • 60349089294 scopus 로고    scopus 로고
    • Measuring HIV neutralization in a luciferase reporter gene assay
    • Montefiori DC. Measuring HIV neutralization in a luciferase reporter gene assay. Methods Mol Biol 2009, 485:395-405.
    • (2009) Methods Mol Biol , vol.485 , pp. 395-405
    • Montefiori, D.C.1
  • 105
    • 69549105767 scopus 로고    scopus 로고
    • New virologic reagents for neutralizing antibody assays
    • Ochsenbauer C, Kappes JC. New virologic reagents for neutralizing antibody assays. Curr Opin HIV AIDS 2009, 4:418-425.
    • (2009) Curr Opin HIV AIDS , vol.4 , pp. 418-425
    • Ochsenbauer, C.1    Kappes, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.