메뉴 건너뛰기




Volumn 423, Issue 1, 2012, Pages 97-106

Highly conserved HIV-1 gp120 glycans proximal to CD4-binding region affect viral infectivity and neutralizing antibody induction

Author keywords

Deglycosylation; Envelope glycoprotein; HIV 1; Immune response; Immunization; Infectivity; Neutralizing activity

Indexed keywords

CD4 ANTIGEN; GLYCOPROTEIN GP 120; NEUTRALIZING ANTIBODY;

EID: 84855343161     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2011.11.023     Document Type: Article
Times cited : (44)

References (72)
  • 1
    • 0031753867 scopus 로고    scopus 로고
    • Gene transfer into muscle by electroporation in vivo
    • Aihara H., Miyazaki J. Gene transfer into muscle by electroporation in vivo. Nat. Biotechnol. 1998, 16(9):867-870.
    • (1998) Nat. Biotechnol. , vol.16 , Issue.9 , pp. 867-870
    • Aihara, H.1    Miyazaki, J.2
  • 3
    • 34447523910 scopus 로고    scopus 로고
    • Targeting the glycans of glycoproteins: a novel paradigm for antiviral therapy
    • Balzarini J. Targeting the glycans of glycoproteins: a novel paradigm for antiviral therapy. Nat. Rev. Microbiol. 2007, 5(8):583-597.
    • (2007) Nat. Rev. Microbiol. , vol.5 , Issue.8 , pp. 583-597
    • Balzarini, J.1
  • 4
    • 33748650569 scopus 로고    scopus 로고
    • Mutational pathways, resistance profile, and side effects of cyanovirin relative to human immunodeficiency virus type 1 strains with N-glycan deletions in their gp120 envelopes
    • Balzarini J., Van Laethem K., Peumans W.J., Van Damme E.J., Bolmstedt A., Gago F., Schols D. Mutational pathways, resistance profile, and side effects of cyanovirin relative to human immunodeficiency virus type 1 strains with N-glycan deletions in their gp120 envelopes. J. Virol. 2006, 80(17):8411-8421.
    • (2006) J. Virol. , vol.80 , Issue.17 , pp. 8411-8421
    • Balzarini, J.1    Van Laethem, K.2    Peumans, W.J.3    Van Damme, E.J.4    Bolmstedt, A.5    Gago, F.6    Schols, D.7
  • 5
    • 33947590277 scopus 로고    scopus 로고
    • A comparative immunogenicity study in rabbits of disulfide-stabilized, proteolytically cleaved, soluble trimeric human immunodeficiency virus type 1 gp140, trimeric cleavage-defective gp140 and monomeric gp120
    • Beddows S., Franti M., Dey A.K., Kirschner M., Iyer S.P., Fisch D.C., Ketas T., Yuste E., Desrosiers R.C., Klasse P.J., Maddon P.J., Olson W.C., Moore J.P. A comparative immunogenicity study in rabbits of disulfide-stabilized, proteolytically cleaved, soluble trimeric human immunodeficiency virus type 1 gp140, trimeric cleavage-defective gp140 and monomeric gp120. Virology 2007, 360(2):329-340.
    • (2007) Virology , vol.360 , Issue.2 , pp. 329-340
    • Beddows, S.1    Franti, M.2    Dey, A.K.3    Kirschner, M.4    Iyer, S.P.5    Fisch, D.C.6    Ketas, T.7    Yuste, E.8    Desrosiers, R.C.9    Klasse, P.J.10    Maddon, P.J.11    Olson, W.C.12    Moore, J.P.13
  • 10
    • 0345742562 scopus 로고    scopus 로고
    • Removal of N-linked glycosylation sites in the V1 region of simian immunodeficiency virus gp120 results in redirection of B-cell responses to V3
    • Cole K.S., Steckbeck J.D., Rowles J.L., Desrosiers R.C., Montelaro R.C. Removal of N-linked glycosylation sites in the V1 region of simian immunodeficiency virus gp120 results in redirection of B-cell responses to V3. J. Virol. 2004, 78(3):1525-1539.
    • (2004) J. Virol. , vol.78 , Issue.3 , pp. 1525-1539
    • Cole, K.S.1    Steckbeck, J.D.2    Rowles, J.L.3    Desrosiers, R.C.4    Montelaro, R.C.5
  • 12
    • 0027462887 scopus 로고
    • Enhanced immunity to human immunodeficiency virus (HIV) envelope elicited by a combined vaccine regimen consisting of priming with a vaccinia recombinant expressing HIV envelope and boosting with gp160 protein
    • Cooney E.L., McElrath M.J., Corey L., Hu S.L., Collier A.C., Arditti D., Hoffman M., Coombs R.W., Smith G.E., Greenberg P.D. Enhanced immunity to human immunodeficiency virus (HIV) envelope elicited by a combined vaccine regimen consisting of priming with a vaccinia recombinant expressing HIV envelope and boosting with gp160 protein. Proc. Natl. Acad. Sci. U. S. A. 1993, 90(5):1882-1886.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , Issue.5 , pp. 1882-1886
    • Cooney, E.L.1    McElrath, M.J.2    Corey, L.3    Hu, S.L.4    Collier, A.C.5    Arditti, D.6    Hoffman, M.7    Coombs, R.W.8    Smith, G.E.9    Greenberg, P.D.10
  • 13
    • 79960391233 scopus 로고    scopus 로고
    • Binding interactions between soluble HIV envelope glycoproteins and quaternary-structure-specific monoclonal antibodies PG9 and PG16
    • Davenport T.M., Friend D., Ellingson K., Xu H., Caldwell Z., Sellhorn G., Kraft Z., Strong R.K., Stamatatos L. Binding interactions between soluble HIV envelope glycoproteins and quaternary-structure-specific monoclonal antibodies PG9 and PG16. J. Virol. 2011, 85(14):7095-7107.
    • (2011) J. Virol. , vol.85 , Issue.14 , pp. 7095-7107
    • Davenport, T.M.1    Friend, D.2    Ellingson, K.3    Xu, H.4    Caldwell, Z.5    Sellhorn, G.6    Kraft, Z.7    Strong, R.K.8    Stamatatos, L.9
  • 14
    • 9144244280 scopus 로고    scopus 로고
    • Intranasal HIV-1-gp160-DNA/gp41 peptide prime-boost immunization regimen in mice results in long-term HIV-1 neutralizing humoral mucosal and systemic immunity
    • Devito C., Zuber B., Schroder U., Benthin R., Okuda K., Broliden K., Wahren B., Hinkula J. Intranasal HIV-1-gp160-DNA/gp41 peptide prime-boost immunization regimen in mice results in long-term HIV-1 neutralizing humoral mucosal and systemic immunity. J. Immunol. 2004, 173(11):7078-7089.
    • (2004) J. Immunol. , vol.173 , Issue.11 , pp. 7078-7089
    • Devito, C.1    Zuber, B.2    Schroder, U.3    Benthin, R.4    Okuda, K.5    Broliden, K.6    Wahren, B.7    Hinkula, J.8
  • 15
    • 34249827906 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 monomeric and trimeric gp120 glycoproteins stabilized in the CD4-bound state: antigenicity, biophysics, and immunogenicity
    • Dey B., Pancera M., Svehla K., Shu Y., Xiang S.H., Vainshtein J., Li Y., Sodroski J., Kwong P.D., Mascola J.R., Wyatt R. Characterization of human immunodeficiency virus type 1 monomeric and trimeric gp120 glycoproteins stabilized in the CD4-bound state: antigenicity, biophysics, and immunogenicity. J. Virol. 2007, 81(11):5579-5593.
    • (2007) J. Virol. , vol.81 , Issue.11 , pp. 5579-5593
    • Dey, B.1    Pancera, M.2    Svehla, K.3    Shu, Y.4    Xiang, S.H.5    Vainshtein, J.6    Li, Y.7    Sodroski, J.8    Kwong, P.D.9    Mascola, J.R.10    Wyatt, R.11
  • 16
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • Doores K.J., Burton D.R. Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. J. Virol. 2010, 84(20):10510-10521.
    • (2010) J. Virol. , vol.84 , Issue.20 , pp. 10510-10521
    • Doores, K.J.1    Burton, D.R.2
  • 17
    • 44949125679 scopus 로고    scopus 로고
    • Natural resistance of human immunodeficiency virus type 1 to the CD4bs antibody b12 conferred by a glycan and an arginine residue close to the CD4 binding loop
    • Duenas-Decamp M.J., Peters P., Burton D., Clapham P.R. Natural resistance of human immunodeficiency virus type 1 to the CD4bs antibody b12 conferred by a glycan and an arginine residue close to the CD4 binding loop. J. Virol. 2008, 82(12):5807-5814.
    • (2008) J. Virol. , vol.82 , Issue.12 , pp. 5807-5814
    • Duenas-Decamp, M.J.1    Peters, P.2    Burton, D.3    Clapham, P.R.4
  • 18
    • 0035038932 scopus 로고    scopus 로고
    • Determination of essential amino acids involved in the CD4-independent tropism of the X4 human immunodeficiency virus type 1 m7NDK isolate: role of potential N glycosylations in the C2 and V3 regions of gp120
    • Dumonceaux J., Goujon C., Joliot V., Briand P., Hazan U. Determination of essential amino acids involved in the CD4-independent tropism of the X4 human immunodeficiency virus type 1 m7NDK isolate: role of potential N glycosylations in the C2 and V3 regions of gp120. J. Virol. 2001, 75(11):5425-5428.
    • (2001) J. Virol. , vol.75 , Issue.11 , pp. 5425-5428
    • Dumonceaux, J.1    Goujon, C.2    Joliot, V.3    Briand, P.4    Hazan, U.5
  • 19
    • 34548680527 scopus 로고    scopus 로고
    • Loss of the N-linked glycosylation site at position 386 in the HIV envelope V4 region enhances macrophage tropism and is associated with dementia
    • Dunfee R.L., Thomas E.R., Wang J., Kunstman K., Wolinsky S.M., Gabuzda D. Loss of the N-linked glycosylation site at position 386 in the HIV envelope V4 region enhances macrophage tropism and is associated with dementia. Virology 2007, 367(1):222-234.
    • (2007) Virology , vol.367 , Issue.1 , pp. 222-234
    • Dunfee, R.L.1    Thomas, E.R.2    Wang, J.3    Kunstman, K.4    Wolinsky, S.M.5    Gabuzda, D.6
  • 20
    • 0035168058 scopus 로고    scopus 로고
    • Immunogenicity and protective efficacy of oligomeric human immunodeficiency virus type 1 gp140
    • Earl P.L., Sugiura W., Montefiori D.C., Broder C.C., Lee S.A., Wild C., Lifson J., Moss B. Immunogenicity and protective efficacy of oligomeric human immunodeficiency virus type 1 gp140. J. Virol. 2001, 75(2):645-653.
    • (2001) J. Virol. , vol.75 , Issue.2 , pp. 645-653
    • Earl, P.L.1    Sugiura, W.2    Montefiori, D.C.3    Broder, C.C.4    Lee, S.A.5    Wild, C.6    Lifson, J.7    Moss, B.8
  • 21
    • 13944254982 scopus 로고    scopus 로고
    • Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection
    • Flynn N.M., Forthal D.N., Harro C.D., Judson F.N., Mayer K.H., Para M.F. Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection. J. Infect. Dis. 2005, 191(5):654-665.
    • (2005) J. Infect. Dis. , vol.191 , Issue.5 , 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
  • 25
    • 0028839622 scopus 로고
    • Candidate AIDS vaccines
    • Graham B.S., Wright P.F. Candidate AIDS vaccines. N. Engl. J. Med. 1995, 333(20):1331-1339.
    • (1995) N. Engl. J. Med. , vol.333 , Issue.20 , pp. 1331-1339
    • Graham, B.S.1    Wright, P.F.2
  • 26
    • 34648816125 scopus 로고    scopus 로고
    • N-linked glycan modifications in gp120 of human immunodeficiency virus type 1 subtype C render partial sensitivity to 2G12 antibody neutralization
    • Gray E.S., Moore P.L., Pantophlet R.A., Morris L. N-linked glycan modifications in gp120 of human immunodeficiency virus type 1 subtype C render partial sensitivity to 2G12 antibody neutralization. J. Virol. 2007, 81(19):10769-10776.
    • (2007) J. Virol. , vol.81 , Issue.19 , pp. 10769-10776
    • Gray, E.S.1    Moore, P.L.2    Pantophlet, R.A.3    Morris, L.4
  • 27
    • 0028449193 scopus 로고
    • Measuring vaccine-induced HIV neutralization: report of a workshop
    • Hanson C.V. Measuring vaccine-induced HIV neutralization: report of a workshop. AIDS Res. Hum. Retroviruses 1994, 10(6):645-648.
    • (1994) AIDS Res. Hum. Retroviruses , vol.10 , Issue.6 , pp. 645-648
    • Hanson, C.V.1
  • 29
    • 0034466833 scopus 로고    scopus 로고
    • Evolution of the human immunodeficiency virus type 1 envelope during infection reveals molecular corollaries of specificity for coreceptor utilization and AIDS pathogenesis
    • Hu Q.X., Barry A.P., Wang Z.X., Connolly S.M., Peiper S.C., Greenberg M.L. Evolution of the human immunodeficiency virus type 1 envelope during infection reveals molecular corollaries of specificity for coreceptor utilization and AIDS pathogenesis. J. Virol. 2000, 74(24):11858-11872.
    • (2000) J. Virol. , vol.74 , Issue.24 , pp. 11858-11872
    • Hu, Q.X.1    Barry, A.P.2    Wang, Z.X.3    Connolly, S.M.4    Peiper, S.C.5    Greenberg, M.L.6
  • 30
    • 20544458737 scopus 로고    scopus 로고
    • Restricted variable residues in the C-terminal segment of HIV-1 V3 loop regulate the molecular anatomy of CCR5 utilization
    • Hu Q., Napier K.B., Trent J.O., Wang Z., Taylor S., Griffin G.E., Peiper S.C., Shattock R.J. Restricted variable residues in the C-terminal segment of HIV-1 V3 loop regulate the molecular anatomy of CCR5 utilization. J. Mol. Biol. 2005, 350(4):699-712.
    • (2005) J. Mol. Biol. , vol.350 , Issue.4 , pp. 699-712
    • Hu, Q.1    Napier, K.B.2    Trent, J.O.3    Wang, Z.4    Taylor, S.5    Griffin, G.E.6    Peiper, S.C.7    Shattock, R.J.8
  • 31
    • 35348992649 scopus 로고    scopus 로고
    • High-mannose-specific deglycosylation of HIV-1 gp120 induced by resistance to cyanovirin-N and the impact on antibody neutralization
    • Hu Q., Mahmood N., Shattock R.J. High-mannose-specific deglycosylation of HIV-1 gp120 induced by resistance to cyanovirin-N and the impact on antibody neutralization. Virology 2007, 368(1):145-154.
    • (2007) Virology , vol.368 , Issue.1 , pp. 145-154
    • Hu, Q.1    Mahmood, N.2    Shattock, R.J.3
  • 32
    • 78650058333 scopus 로고    scopus 로고
    • CCR5 utilization of transmitted and early founder HIV-1 envelopes and the sensitivity to small-molecule CCR5 inhibitors
    • Hu Q., Huang X., Shattock R.J. CCR5 utilization of transmitted and early founder HIV-1 envelopes and the sensitivity to small-molecule CCR5 inhibitors. J. Gen. Virol. 2010, 91:2965-2973.
    • (2010) J. Gen. Virol. , vol.91 , pp. 2965-2973
    • Hu, Q.1    Huang, X.2    Shattock, R.J.3
  • 33
    • 80052936296 scopus 로고    scopus 로고
    • Removal of two high-mannose N-linked glycans on gp120 renders human immunodeficiency virus 1 largely resistant to the carbohydrate-binding agent griffithsin
    • Huang X., Jin W., Griffin G.E., Shattock R.J., Hu Q. Removal of two high-mannose N-linked glycans on gp120 renders human immunodeficiency virus 1 largely resistant to the carbohydrate-binding agent griffithsin. J. Gen. Virol. 2011, 92(Pt 10):2367-2373.
    • (2011) J. Gen. Virol. , vol.92 , Issue.PART. 10 , pp. 2367-2373
    • Huang, X.1    Jin, W.2    Griffin, G.E.3    Shattock, R.J.4    Hu, Q.5
  • 34
    • 1242338175 scopus 로고    scopus 로고
    • Expression and characterisation of recombinant oligomeric envelope glycoproteins derived from primary isolates of HIV-1
    • Jeffs S.A., Goriup S., Kebble B., Crane D., Bolgiano B., Sattentau Q., Jones S., Holmes H. Expression and characterisation of recombinant oligomeric envelope glycoproteins derived from primary isolates of HIV-1. Vaccine 2004, 22(8):1032-1046.
    • (2004) Vaccine , vol.22 , Issue.8 , 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
  • 36
    • 13144302861 scopus 로고    scopus 로고
    • Comparison of HIV Type 1 ADA gp120 monomers versus gp140 trimers as immunogens for the induction of neutralizing antibodies
    • Kim M., Qiao Z.S., Montefiori D.C., Haynes B.F., Reinherz E.L., Liao H.X. Comparison of HIV Type 1 ADA gp120 monomers versus gp140 trimers as immunogens for the induction of neutralizing antibodies. AIDS Res. Hum. Retroviruses 2005, 21(1):58-67.
    • (2005) AIDS Res. Hum. Retroviruses , vol.21 , Issue.1 , pp. 58-67
    • Kim, M.1    Qiao, Z.S.2    Montefiori, D.C.3    Haynes, B.F.4    Reinherz, E.L.5    Liao, H.X.6
  • 37
    • 0041920924 scopus 로고    scopus 로고
    • Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition
    • Koch M., Pancera M., Kwong P.D., Kolchinsky P., Grundner C., Wang L., Hendrickson W.A., Sodroski J., Wyatt R. Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition. Virology 2003, 313(2):387-400.
    • (2003) Virology , vol.313 , Issue.2 , pp. 387-400
    • Koch, M.1    Pancera, M.2    Kwong, P.D.3    Kolchinsky, P.4    Grundner, C.5    Wang, L.6    Hendrickson, W.A.7    Sodroski, J.8    Wyatt, R.9
  • 38
    • 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. 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. 2001, 75(7):3435-3443.
    • (2001) J. Virol. , vol.75 , Issue.7 , pp. 3435-3443
    • Kolchinsky, P.1    Kiprilov, E.2    Bartley, P.3    Rubinstein, R.4    Sodroski, J.5
  • 39
    • 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. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998, 393(6686):648-659.
    • (1998) Nature , vol.393 , Issue.6686 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 40
    • 0026582808 scopus 로고
    • Nonrandom distribution of gp120 N-linked glycosylation sites important for infectivity of human immunodeficiency virus type 1
    • Lee W.R., Syu W.J., Du B., Matsuda M., Tan S., Wolf A., Essex M., Lee T.H. Nonrandom distribution of gp120 N-linked glycosylation sites important for infectivity of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. U. S. A. 1992, 89(6):2213-2217.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , Issue.6 , pp. 2213-2217
    • Lee, W.R.1    Syu, W.J.2    Du, B.3    Matsuda, M.4    Tan, S.5    Wolf, A.6    Essex, M.7    Lee, T.H.8
  • 41
    • 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. 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. 1990, 265(18):10373-10382.
    • (1990) J. Biol. Chem. , vol.265 , Issue.18 , 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
  • 42
    • 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 B.A., Anderson D., Montefiori D., Polacino P., Hu S.L. 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. 2008, 82(2):638-651.
    • (2008) J. Virol. , vol.82 , Issue.2 , 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
  • 43
    • 0033942750 scopus 로고    scopus 로고
    • V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCR5 receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies
    • Ly A., Stamatatos L. V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCR5 receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies. J. Virol. 2000, 74(15):6769-6776.
    • (2000) J. Virol. , vol.74 , Issue.15 , pp. 6769-6776
    • Ly, A.1    Stamatatos, L.2
  • 44
    • 0034469170 scopus 로고    scopus 로고
    • The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors
    • Malenbaum S.E., Yang D., Cavacini L., Posner M., Robinson J., Cheng-Mayer C. The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors. J. Virol. 2000, 74(23):11008-11016.
    • (2000) J. Virol. , vol.74 , Issue.23 , pp. 11008-11016
    • Malenbaum, S.E.1    Yang, D.2    Cavacini, L.3    Posner, M.4    Robinson, J.5    Cheng-Mayer, C.6
  • 46
    • 0028453157 scopus 로고
    • Dilemma of neutralization resistance of HIV-1 field isolates and vaccine development
    • Matthews T.J. Dilemma of neutralization resistance of HIV-1 field isolates and vaccine development. AIDS Res. Hum. Retroviruses 1994, 10(6):631-632.
    • (1994) AIDS Res. Hum. Retroviruses , vol.10 , Issue.6 , pp. 631-632
    • Matthews, T.J.1
  • 47
    • 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 R.A., 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(7):3279-3295.
    • (2004) J. Virol. , vol.78 , Issue.7 , pp. 3279-3295
    • McCaffrey, R.A.1    Saunders, C.2    Hensel, M.3    Stamatatos, L.4
  • 48
    • 60349089294 scopus 로고    scopus 로고
    • Measuring HIV neutralization in a luciferase reporter gene assay
    • Montefiori D.C. 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
  • 51
    • 0034974149 scopus 로고    scopus 로고
    • N-linked glycosylation sites adjacent to and within the V1/V2 and the V3 loops of dualtropic human immunodeficiency virus type 1 isolate DH12 gp120 affect coreceptor usage and cellular tropism
    • Ogert R.A., Lee M.K., Ross W., Buckler-White A., Martin M.A., Cho M.W. N-linked glycosylation sites adjacent to and within the V1/V2 and the V3 loops of dualtropic human immunodeficiency virus type 1 isolate DH12 gp120 affect coreceptor usage and cellular tropism. J. Virol. 2001, 75(13):5998-6006.
    • (2001) J. Virol. , vol.75 , Issue.13 , pp. 5998-6006
    • Ogert, R.A.1    Lee, M.K.2    Ross, W.3    Buckler-White, A.4    Martin, M.A.5    Cho, M.W.6
  • 52
    • 33646146379 scopus 로고    scopus 로고
    • GP120: target for neutralizing HIV-1 antibodies
    • Pantophlet R., Burton D.R. 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
  • 53
    • 33845433434 scopus 로고    scopus 로고
    • Randomized, double-blind, placebo-controlled efficacy trial of a bivalent recombinant glycoprotein 120 HIV-1 vaccine among injection drug users in Bangkok, Thailand
    • Pitisuttithum P., Gilbert P., Gurwith M., Heyward W., Martin M., van Griensven F., Hu D., Tappero J.W., Choopanya K. Randomized, double-blind, placebo-controlled efficacy trial of a bivalent recombinant glycoprotein 120 HIV-1 vaccine among injection drug users in Bangkok, Thailand. J. Infect. Dis. 2006, 194(12):1661-1671.
    • (2006) J. Infect. Dis. , vol.194 , Issue.12 , pp. 1661-1671
    • Pitisuttithum, P.1    Gilbert, P.2    Gurwith, M.3    Heyward, W.4    Martin, M.5    van Griensven, F.6    Hu, D.7    Tappero, J.W.8    Choopanya, K.9
  • 54
    • 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 M.I., Goudsmit J., Paxton W.A. 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(16):13433-13441.
    • (2001) J. Biol. Chem. , vol.276 , Issue.16 , pp. 13433-13441
    • Pollakis, G.1    Kang, S.2    Kliphuis, A.3    Chalaby, M.I.4    Goudsmit, J.5    Paxton, W.A.6
  • 55
    • 0035098352 scopus 로고    scopus 로고
    • Loss of N-linked glycans in the V3-loop region of gp120 is correlated to an enhanced infectivity of HIV-1
    • Polzer S., Dittmar M.T., Schmitz H., Meyer B., Muller H., Krausslich H.G., Schreiber M. Loss of N-linked glycans in the V3-loop region of gp120 is correlated to an enhanced infectivity of HIV-1. Glycobiology 2001, 11(1):11-19.
    • (2001) Glycobiology , vol.11 , Issue.1 , pp. 11-19
    • Polzer, S.1    Dittmar, M.T.2    Schmitz, H.3    Meyer, B.4    Muller, H.5    Krausslich, H.G.6    Schreiber, M.7
  • 56
    • 0036935266 scopus 로고    scopus 로고
    • The N-linked glycan g15 within the V3 loop of the HIV-1 external glycoprotein gp120 affects coreceptor usage, cellular tropism, and neutralization
    • Polzer S., Dittmar M.T., Schmitz H., Schreiber M. The N-linked glycan g15 within the V3 loop of the HIV-1 external glycoprotein gp120 affects coreceptor usage, cellular tropism, and neutralization. Virology 2002, 304(1):70-80.
    • (2002) Virology , vol.304 , Issue.1 , pp. 70-80
    • Polzer, S.1    Dittmar, M.T.2    Schmitz, H.3    Schreiber, M.4
  • 57
    • 0036229473 scopus 로고    scopus 로고
    • Role of N-linked glycans in a human immunodeficiency virus envelope glycoprotein: effects on protein function and the neutralizing antibody response
    • Quinones-Kochs M.I., Buonocore L., Rose J.K. Role of N-linked glycans in a human immunodeficiency virus envelope glycoprotein: effects on protein function and the neutralizing antibody response. J. Virol. 2002, 76(9):4199-4211.
    • (2002) J. Virol. , vol.76 , Issue.9 , pp. 4199-4211
    • Quinones-Kochs, M.I.1    Buonocore, L.2    Rose, J.K.3
  • 58
    • 33846894323 scopus 로고    scopus 로고
    • Prime-boost immunization with DNA, recombinant fowlpox virus and VLP(SHIV) elicit both neutralizing antibodies and IFNgamma-producing T cells against the HIV-envelope protein in mice that control env-bearing tumour cells
    • Radaelli A., Bonduelle O., Beggio P., Mahe B., Pozzi E., Elli V., Paganini M., Zanotto C., De Giuli Morghen C., Combadiere B. Prime-boost immunization with DNA, recombinant fowlpox virus and VLP(SHIV) elicit both neutralizing antibodies and IFNgamma-producing T cells against the HIV-envelope protein in mice that control env-bearing tumour cells. Vaccine 2007, 25(11):2128-2138.
    • (2007) Vaccine , vol.25 , Issue.11 , pp. 2128-2138
    • Radaelli, A.1    Bonduelle, O.2    Beggio, P.3    Mahe, B.4    Pozzi, E.5    Elli, V.6    Paganini, M.7    Zanotto, C.8    De Giuli Morghen, C.9    Combadiere, B.10
  • 59
    • 0031749469 scopus 로고    scopus 로고
    • A role for carbohydrates in immune evasion in AIDS
    • Reitter J.N., Means R.E., Desrosiers R.C. A role for carbohydrates in immune evasion in AIDS. Nat. Med. 1998, 4(6):679-684.
    • (1998) Nat. Med. , vol.4 , Issue.6 , pp. 679-684
    • Reitter, J.N.1    Means, R.E.2    Desrosiers, R.C.3
  • 60
    • 70349568514 scopus 로고    scopus 로고
    • Working towards an HIV/AIDS vaccine
    • Robinson H.L. Working towards an HIV/AIDS vaccine. Hum. Vaccin. 2009, 5(7):436-438.
    • (2009) Hum. Vaccin. , vol.5 , Issue.7 , pp. 436-438
    • Robinson, H.L.1
  • 61
    • 33748925430 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity
    • Sagar M., Wu X., Lee S., Overbaugh J. Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity. J. Virol. 2006, 80(19):9586-9598.
    • (2006) J. Virol. , vol.80 , Issue.19 , pp. 9586-9598
    • Sagar, M.1    Wu, X.2    Lee, S.3    Overbaugh, J.4
  • 62
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • Sanders R.W., Venturi M., Schiffner L., Kalyanaraman R., Katinger H., Lloyd K.O., Kwong P.D., Moore J.P. The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J. Virol. 2002, 76(14):7293-7305.
    • (2002) J. Virol. , vol.76 , Issue.14 , pp. 7293-7305
    • Sanders, R.W.1    Venturi, M.2    Schiffner, L.3    Kalyanaraman, R.4    Katinger, H.5    Lloyd, K.O.6    Kwong, P.D.7    Moore, J.P.8
  • 64
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1->2 mannose residues on the outer face of gp120
    • Scanlan C.N., Pantophlet R., Wormald M.R., Ollmann Saphire E., Stanfield R., Wilson I.A., Katinger H., Dwek R.A., Rudd P.M., Burton D.R. The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1->2 mannose residues on the outer face of gp120. J. Virol. 2002, 76(14):7306-7321.
    • (2002) J. Virol. , vol.76 , Issue.14 , pp. 7306-7321
    • Scanlan, C.N.1    Pantophlet, R.2    Wormald, M.R.3    Ollmann Saphire, E.4    Stanfield, R.5    Wilson, I.A.6    Katinger, H.7    Dwek, R.A.8    Rudd, P.M.9    Burton, D.R.10
  • 65
    • 0035659831 scopus 로고    scopus 로고
    • The HIV vaccine pipeline, from preclinical to phase III
    • Schultz A.M., Bradac J.A. The HIV vaccine pipeline, from preclinical to phase III. AIDS 2001, 15(Suppl 5):S147-S158.
    • (2001) AIDS , vol.15 , Issue.SUPPL. 5
    • Schultz, A.M.1    Bradac, J.A.2
  • 66
    • 43049162225 scopus 로고    scopus 로고
    • SnapShot: HIV-1 proteins
    • (742 e1)
    • Swanson C.M., Malim M.H. SnapShot: HIV-1 proteins. Cell 2008, 133(4):742. (742 e1).
    • (2008) Cell , vol.133 , Issue.4 , pp. 742
    • Swanson, C.M.1    Malim, M.H.2
  • 67
    • 77949773004 scopus 로고    scopus 로고
    • Antibody responses elicited through homologous or heterologous prime-boost DNA and protein vaccinations differ in functional activity and avidity
    • Vaine M., Wang S., Hackett A., Arthos J., Lu S. Antibody responses elicited through homologous or heterologous prime-boost DNA and protein vaccinations differ in functional activity and avidity. Vaccine 2010, 28(17):2999-3007.
    • (2010) Vaccine , vol.28 , Issue.17 , pp. 2999-3007
    • Vaine, M.1    Wang, S.2    Hackett, A.3    Arthos, J.4    Lu, S.5
  • 71
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens
    • Wyatt R., Sodroski J. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 1998, 280(5371):1884-1888.
    • (1998) Science , vol.280 , Issue.5371 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 72
    • 0034687168 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells
    • Zhu X., Borchers C., Bienstock R.J., Tomer K.B. Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells. Biochemistry 2000, 39(37):11194-11204.
    • (2000) Biochemistry , vol.39 , Issue.37 , pp. 11194-11204
    • Zhu, X.1    Borchers, C.2    Bienstock, R.J.3    Tomer, K.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.