메뉴 건너뛰기




Volumn 282, Issue 24, 2015, Pages 4679-4691

The HIV glycan shield as a target for broadly neutralizing antibodies

Author keywords

broadly neutralizing antibody; envelope trimer; glycosylation; HIV; vaccine

Indexed keywords

BROADLY NEUTRALIZING ANTIBODY; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; NEUTRALIZING ANTIBODY; SIALIC ACID; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; GLYCOPROTEIN; MANNAN; POLYSACCHARIDE;

EID: 84959117772     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13530     Document Type: Review
Times cited : (101)

References (86)
  • 1
    • 0029112274 scopus 로고
    • The alpha-glucosidase inhibitor N-butyldeoxynojirimycin inhibits human immunodeficiency virus entry at the level of post-CD4 binding
    • Fischer PB, Collin M, Karlsson GB, James W, Butters TD, Davis SJ, Gordon S, Dwek RA, &, Platt FM, (1995) The alpha-glucosidase inhibitor N-butyldeoxynojirimycin inhibits human immunodeficiency virus entry at the level of post-CD4 binding. J Virol 69, 5791-5797.
    • (1995) J Virol , vol.69 , pp. 5791-5797
    • Fischer, P.B.1    Collin, M.2    Karlsson, G.B.3    James, W.4    Butters, T.D.5    Davis, S.J.6    Gordon, S.7    Dwek, R.A.8    Platt, F.M.9
  • 2
    • 84892754407 scopus 로고    scopus 로고
    • Emerging principles for the therapeutic exploitation of glycosylation
    • Dalziel M, Crispin M, Scanlan CN, Zitzmann N, &, Dwek RA, (2014) Emerging principles for the therapeutic exploitation of glycosylation. Science 343, 1235681.
    • (2014) Science , vol.343 , pp. 1235681
    • Dalziel, M.1    Crispin, M.2    Scanlan, C.N.3    Zitzmann, N.4    Dwek, R.A.5
  • 3
    • 34247636624 scopus 로고    scopus 로고
    • Exploiting the defensive sugars of HIV-1 for drug and vaccine design
    • Scanlan CN, Offer J, Zitzmann N, &, Dwek RA, (2007) Exploiting the defensive sugars of HIV-1 for drug and vaccine design. Nature 446, 1038-1045.
    • (2007) Nature , vol.446 , pp. 1038-1045
    • Scanlan, C.N.1    Offer, J.2    Zitzmann, N.3    Dwek, R.A.4
  • 5
    • 84924787042 scopus 로고    scopus 로고
    • Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design
    • Crispin M, &, Doores KJ, (2015) Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design. Curr Opin Virol 11, 63-69.
    • (2015) Curr Opin Virol , vol.11 , pp. 63-69
    • Crispin, M.1    Doores, K.J.2
  • 6
    • 84929896699 scopus 로고    scopus 로고
    • Antibody responses to envelope glycoproteins in HIV-1 infection
    • Burton DR, &, Mascola JR, (2015) Antibody responses to envelope glycoproteins in HIV-1 infection. Nat Immunol 16, 571-576.
    • (2015) Nat Immunol , vol.16 , pp. 571-576
    • Burton, D.R.1    Mascola, J.R.2
  • 8
  • 10
    • 84921606536 scopus 로고    scopus 로고
    • Insights into the trimeric HIV-1 envelope glycoprotein structure
    • Ward AB, &, Wilson IA, (2015) Insights into the trimeric HIV-1 envelope glycoprotein structure. Trends Biochem Sci 40, 101-107.
    • (2015) Trends Biochem Sci , vol.40 , pp. 101-107
    • Ward, A.B.1    Wilson, I.A.2
  • 12
    • 84861374644 scopus 로고    scopus 로고
    • PGV04, an HIV-1 gp120 CD4 binding site antibody, is broad and potent in neutralization but does not induce conformational changes characteristic of CD4
    • Falkowska E, Ramos A, Feng Y, Zhou T, Moquin S, Walker LM, Wu X, Seaman MS, Wrin T, Kwong PD, et al,. (2012) PGV04, an HIV-1 gp120 CD4 binding site antibody, is broad and potent in neutralization but does not induce conformational changes characteristic of CD4. J Virol 86, 4394-4403.
    • (2012) J Virol , vol.86 , pp. 4394-4403
    • Falkowska, E.1    Ramos, A.2    Feng, Y.3    Zhou, T.4    Moquin, S.5    Walker, L.M.6    Wu, X.7    Seaman, M.S.8    Wrin, T.9    Kwong, P.D.10
  • 22
    • 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, (2010) 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 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
  • 23
    • 84921564277 scopus 로고    scopus 로고
    • Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy
    • Murin CD, Julien JP, Sok D, Stanfield RL, Khayat R, Cupo A, Moore JP, Burton DR, Wilson IA, &, Ward AB, (2014) Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy. J Virol 88, 10177-10188.
    • (2014) J Virol , vol.88 , pp. 10177-10188
    • Murin, C.D.1    Julien, J.P.2    Sok, D.3    Stanfield, R.L.4    Khayat, R.5    Cupo, A.6    Moore, J.P.7    Burton, D.R.8    Wilson, I.A.9    Ward, A.B.10
  • 25
    • 84878519611 scopus 로고    scopus 로고
    • Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans
    • Julien JP, Sok D, Khayat R, Lee JH, Doores KJ, Walker LM, Ramos A, Diwanji DC, Pejchal R, Cupo A, et al,. (2013) Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans. PLoS Pathog 9, e1003342.
    • (2013) PLoS Pathog , vol.9 , pp. e1003342
    • Julien, J.P.1    Sok, D.2    Khayat, R.3    Lee, J.H.4    Doores, K.J.5    Walker, L.M.6    Ramos, A.7    Diwanji, D.C.8    Pejchal, R.9    Cupo, A.10
  • 28
    • 80052938385 scopus 로고    scopus 로고
    • Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors
    • Bonsignori M, Hwang KK, Chen X, Tsao CY, Morris L, Gray E, Marshall DJ, Crump JA, Kapiga SH, Sam NE, et al,. (2011) Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors. J Virol 85, 9998-10009.
    • (2011) J Virol , vol.85 , pp. 9998-10009
    • Bonsignori, M.1    Hwang, K.K.2    Chen, X.3    Tsao, C.Y.4    Morris, L.5    Gray, E.6    Marshall, D.J.7    Crump, J.A.8    Kapiga, S.H.9    Sam, N.E.10
  • 34
    • 0023811767 scopus 로고
    • Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein 120
    • Geyer H, Holschbach C, Hunsmann G, &, Schneider J, (1988) Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein 120. J Biol Chem 263, 11760-11767.
    • (1988) J Biol Chem , vol.263 , pp. 11760-11767
    • Geyer, H.1    Holschbach, C.2    Hunsmann, G.3    Schneider, J.4
  • 35
    • 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 CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, &, Gregory TJ, (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
  • 36
    • 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, (1988) 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 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
  • 37
    • 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, (1988) Carbohydrate structures of the human-immunodeficiency-virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese-hamster ovary cells. Biochem J 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
  • 38
    • 0025374887 scopus 로고
    • Diversity of oligosaccharide structures on the envelope glycoprotein gp 120 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, (1990) Diversity of oligosaccharide structures on the envelope glycoprotein gp 120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N-acetylglucosamine residues. J Biol Chem 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
  • 43
    • 84938149437 scopus 로고    scopus 로고
    • Comparative analysis of the glycosylation profiles of membrane-anchored HIV-1 envelope glycoprotein trimers and soluble gp140
    • Go EP, Herschhorn A, Gu C, Castillo-Menendez L, Zhang S, Mao Y, Chen H, Ding H, Wakefield JK, Hua D, et al,. (2015) Comparative analysis of the glycosylation profiles of membrane-anchored HIV-1 envelope glycoprotein trimers and soluble gp140. J Virol 89, 8245-8257.
    • (2015) J Virol , vol.89 , pp. 8245-8257
    • Go, E.P.1    Herschhorn, A.2    Gu, C.3    Castillo-Menendez, L.4    Zhang, S.5    Mao, Y.6    Chen, H.7    Ding, H.8    Wakefield, J.K.9    Hua, D.10
  • 44
    • 84938924964 scopus 로고    scopus 로고
    • Cellular and protein-directed glycosylation of native cleaved HIV-1 envelope
    • Pritchard LK, Harvey DJ, Bonomelli C, Crispin M, &, Doores KJ, (2015) Cellular and protein-directed glycosylation of native cleaved HIV-1 envelope. J Virol 89, 8932-8944.
    • (2015) J Virol , vol.89 , pp. 8932-8944
    • Pritchard, L.K.1    Harvey, D.J.2    Bonomelli, C.3    Crispin, M.4    Doores, K.J.5
  • 47
    • 56449121966 scopus 로고    scopus 로고
    • Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: A template for antiviral and vaccine design
    • Bowden TA, Crispin M, Harvey DJ, Aricescu AR, Grimes JM, Jones EY, &, Stuart DI, (2008) Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design. J Virol 82, 11628-11636.
    • (2008) J Virol , vol.82 , pp. 11628-11636
    • Bowden, T.A.1    Crispin, M.2    Harvey, D.J.3    Aricescu, A.R.4    Grimes, J.M.5    Jones, E.Y.6    Stuart, D.I.7
  • 48
    • 77956832815 scopus 로고    scopus 로고
    • Characterization of the envelope glycoproteins associated with infectious hepatitis C virus
    • Vieyres G, Thomas X, Descamps V, Duverlie G, Patel AH, &, Dubuisson J, (2010) Characterization of the envelope glycoproteins associated with infectious hepatitis C virus. J Virol 84, 10159-10168.
    • (2010) J Virol , vol.84 , pp. 10159-10168
    • Vieyres, G.1    Thomas, X.2    Descamps, V.3    Duverlie, G.4    Patel, A.H.5    Dubuisson, J.6
  • 50
    • 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, (2000) Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells. Biochemistry 39, 11194-11204.
    • (2000) Biochemistry , vol.39 , pp. 11194-11204
    • Zhu, X.1    Borchers, C.2    Bienstock, R.J.3    Tomer, K.B.4
  • 51
    • 7244232761 scopus 로고    scopus 로고
    • Characterization of glycopeptides from HIV-I(SF2) gp120 by liquid chromatography mass spectrometry
    • Cutalo JM, Deterding LJ, &, Tomer KB, (2004) Characterization of glycopeptides from HIV-I(SF2) gp120 by liquid chromatography mass spectrometry. J Am Soc Mass Spectrom 15, 1545-1555.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 1545-1555
    • Cutalo, J.M.1    Deterding, L.J.2    Tomer, K.B.3
  • 52
    • 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, (2008) 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 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
  • 55
    • 84874622598 scopus 로고    scopus 로고
    • Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins
    • Go EP, Liao HX, Alam SM, Hua D, Haynes BF, &, Desaire H, (2013) Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins. J Proteome Res 12, 1223-1234.
    • (2013) J Proteome Res , vol.12 , pp. 1223-1234
    • Go, E.P.1    Liao, H.X.2    Alam, S.M.3    Hua, D.4    Haynes, B.F.5    Desaire, H.6
  • 56
    • 84930891393 scopus 로고    scopus 로고
    • Glycan microheterogeneity at the PGT135 antibody recognition site on HIV-1 gp120 reveals a molecular mechanism for neutralization resistance
    • Pritchard LK, Spencer DI, Royle L, Vasiljevic S, Krumm SA, Doores KJ, &, Crispin M, (2015) Glycan microheterogeneity at the PGT135 antibody recognition site on HIV-1 gp120 reveals a molecular mechanism for neutralization resistance. J Virol 89, 6952-6959.
    • (2015) J Virol , vol.89 , pp. 6952-6959
    • Pritchard, L.K.1    Spencer, D.I.2    Royle, L.3    Vasiljevic, S.4    Krumm, S.A.5    Doores, K.J.6    Crispin, M.7
  • 57
    • 84884678235 scopus 로고    scopus 로고
    • A next-generation cleaved, soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies
    • Sanders RW, Derking R, Cupo A, Julien JP, Yasmeen A, de Val N, Kim HJ, Blattner C, de la Pena AT, Korzun J, et al,. (2013) A next-generation cleaved, soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies. PLoS Pathog 9, e1003618.
    • (2013) PLoS Pathog , vol.9 , pp. e1003618
    • Sanders, R.W.1    Derking, R.2    Cupo, A.3    Julien, J.P.4    Yasmeen, A.5    De Val, N.6    Kim, H.J.7    Blattner, C.8    De La Pena, A.T.9    Korzun, J.10
  • 61
    • 84939128392 scopus 로고    scopus 로고
    • A new approach to produce HIV-1 envelope trimers: Both cleavage and proper glycosylation are essential to generate authentic trimers
    • AlSalmi W, Mahalingam M, Ananthaswamy N, Hamlin C, Flores D, Gao G, &, Rao VB, (2015) A new approach to produce HIV-1 envelope trimers: both cleavage and proper glycosylation are essential to generate authentic trimers. J Biol Chem 290, 19780-19795.
    • (2015) J Biol Chem , vol.290 , pp. 19780-19795
    • AlSalmi, W.1    Mahalingam, M.2    Ananthaswamy, N.3    Hamlin, C.4    Flores, D.5    Gao, G.6    Rao, V.B.7
  • 62
    • 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, (2013) A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization. Retrovirology 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
  • 63
    • 83355166921 scopus 로고    scopus 로고
    • The highly conserved glycan at asparagine 260 of HIV-1 gp120 is indispensable for viral entry
    • Francois KO, &, Balzarini J, (2011) The highly conserved glycan at asparagine 260 of HIV-1 gp120 is indispensable for viral entry. J Biol Chem 286, 42900-42910.
    • (2011) J Biol Chem , vol.286 , pp. 42900-42910
    • Francois, K.O.1    Balzarini, J.2
  • 64
    • 84903388369 scopus 로고    scopus 로고
    • Deletion of the highly conserved N-glycan at Asn260 of HIV-1 gp120 affects folding and lysosomal degradation of gp120, and results in loss of viral infectivity
    • Mathys L, Francois KO, Quandte M, Braakman I, &, Balzarini J, (2014) Deletion of the highly conserved N-glycan at Asn260 of HIV-1 gp120 affects folding and lysosomal degradation of gp120, and results in loss of viral infectivity. PLoS One 9, e101181.
    • (2014) PLoS One , vol.9 , pp. e101181
    • Mathys, L.1    Francois, K.O.2    Quandte, M.3    Braakman, I.4    Balzarini, J.5
  • 65
    • 33751224478 scopus 로고    scopus 로고
    • Genetic and neutralization properties of subtype C human immunodeficiency virus type 1 molecular env clones from acute and early heterosexually acquired infections in Southern Africa
    • Li M, Salazar-Gonzalez JF, Derdeyn CA, Morris L, Williamson C, Robinson JE, Decker JM, Li Y, Salazar MG, Polonis VR, et al,. (2006) Genetic and neutralization properties of subtype C human immunodeficiency virus type 1 molecular env clones from acute and early heterosexually acquired infections in Southern Africa. J Virol 80, 11776-11790.
    • (2006) J Virol , vol.80 , pp. 11776-11790
    • Li, M.1    Salazar-Gonzalez, J.F.2    Derdeyn, C.A.3    Morris, L.4    Williamson, C.5    Robinson, J.E.6    Decker, J.M.7    Li, Y.8    Salazar, M.G.9    Polonis, V.R.10
  • 66
    • 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, (2006) 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 80, 9586-9598.
    • (2006) J Virol , vol.80 , pp. 9586-9598
    • Sagar, M.1    Wu, X.2    Lee, S.3    Overbaugh, J.4
  • 67
    • 0001719863 scopus 로고
    • Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1
    • Pal R, Hoke GM, &, Sarngadharan MG, (1989) Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. Proc Natl Acad Sci USA 86, 3384-3388.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3384-3388
    • Pal, R.1    Hoke, G.M.2    Sarngadharan, M.G.3
  • 68
    • 0024334165 scopus 로고
    • Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: Effects of monensin on glycosylation and transport
    • Dewar RL, Vasudevachari MB, Natarajan V, &, Salzman NP, (1989) Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport. J Virol 63, 2452-2456.
    • (1989) J Virol , vol.63 , pp. 2452-2456
    • Dewar, R.L.1    Vasudevachari, M.B.2    Natarajan, V.3    Salzman, N.P.4
  • 71
    • 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, (2010) Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. J Virol 84, 10510-10521.
    • (2010) J Virol , vol.84 , pp. 10510-10521
    • Doores, K.J.1    Burton, D.R.2
  • 74
    • 33947602811 scopus 로고    scopus 로고
    • Siglecs and their roles in the immune system
    • Crocker PR, Paulson JC, &, Varki A, (2007) Siglecs and their roles in the immune system. Nat Rev Immunol 7, 255-266.
    • (2007) Nat Rev Immunol , vol.7 , pp. 255-266
    • Crocker, P.R.1    Paulson, J.C.2    Varki, A.3
  • 75
    • 84921786419 scopus 로고    scopus 로고
    • Siglec-mediated regulation of immune cell function in disease
    • Macauley MS, Crocker PR, &, Paulson JC, (2014) Siglec-mediated regulation of immune cell function in disease. Nat Rev Immunol 14, 653-666.
    • (2014) Nat Rev Immunol , vol.14 , pp. 653-666
    • MacAuley, M.S.1    Crocker, P.R.2    Paulson, J.C.3
  • 79
    • 0027957921 scopus 로고
    • Human immunodeficiency virus type 1 envelope glycoprotein is modified by O-linked oligosaccharides
    • Bernstein HB, Tucker SP, Hunter E, Schutzbach JS, &, Compans RW, (1994) Human immunodeficiency virus type 1 envelope glycoprotein is modified by O-linked oligosaccharides. J Virol 68, 463-468.
    • (1994) J Virol , vol.68 , pp. 463-468
    • Bernstein, H.B.1    Tucker, S.P.2    Hunter, E.3    Schutzbach, J.S.4    Compans, R.W.5
  • 80
    • 0026451818 scopus 로고
    • An O-linked carbohydrate neutralization epitope of HIV-1 gp 120 is expressed by HIV-1 env gene recombinant vaccinia virus
    • Hansen JE, Clausen H, Hu SL, Nielsen JO, &, Olofsson S, (1992) An O-linked carbohydrate neutralization epitope of HIV-1 gp 120 is expressed by HIV-1 env gene recombinant vaccinia virus. Arch Virol 126, 11-20.
    • (1992) Arch Virol , vol.126 , pp. 11-20
    • Hansen, J.E.1    Clausen, H.2    Hu, S.L.3    Nielsen, J.O.4    Olofsson, S.5
  • 82
    • 84904310904 scopus 로고    scopus 로고
    • Glycoform analysis of recombinant and human immunodeficiency virus envelope protein gp120 via higher energy collisional dissociation and spectral-aligning strategy
    • Yang W, Shah P, Toghi Eshghi S, Yang S, Sun S, Ao M, Rubin A, Jackson JB, &, Zhang H, (2014) Glycoform analysis of recombinant and human immunodeficiency virus envelope protein gp120 via higher energy collisional dissociation and spectral-aligning strategy. Anal Chem 86, 6959-6967.
    • (2014) Anal Chem , vol.86 , pp. 6959-6967
    • Yang, W.1    Shah, P.2    Toghi Eshghi, S.3    Yang, S.4    Sun, S.5    Ao, M.6    Rubin, A.7    Jackson, J.B.8    Zhang, H.9
  • 84
    • 84930365226 scopus 로고    scopus 로고
    • Vaccine-elicited tier 2 HIV-1 neutralizing antibodies bind to quaternary epitopes involving glycan-deficient patches proximal to the CD4 binding site
    • Crooks ET, Tong T, Chakrabarti B, Narayan K, Georgiev IS, Menis S, Huang X, Kulp D, Osawa K, Muranaka J, et al,. (2015) Vaccine-elicited tier 2 HIV-1 neutralizing antibodies bind to quaternary epitopes involving glycan-deficient patches proximal to the CD4 binding site. PLoS Pathog 11, e1004932.
    • (2015) PLoS Pathog , vol.11 , pp. e1004932
    • Crooks, E.T.1    Tong, T.2    Chakrabarti, B.3    Narayan, K.4    Georgiev, I.S.5    Menis, S.6    Huang, X.7    Kulp, D.8    Osawa, K.9    Muranaka, J.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.