메뉴 건너뛰기




Volumn 47, Issue , 2018, Pages 499-523

Structure and Immune Recognition of the HIV Glycan Shield

Author keywords

broadly neutralizing antibody; EM structure; glycan composition; glycosylation; viral glycoprotein; X ray structure

Indexed keywords

CD4 ANTIGEN; GLYCAN; GLYCOPEPTIDE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; NEUTRALIZING ANTIBODY; VIRUS ENVELOPE PROTEIN;

EID: 85047543847     PISSN: 1936122X     EISSN: 19361238     Source Type: Book Series    
DOI: 10.1146/annurev-biophys-060414-034156     Document Type: Review
Times cited : (101)

References (152)
  • 2
    • 9144261693 scopus 로고    scopus 로고
    • The glycosylation of human serum IgD and IgE and the accessibility of identified oligomannose structures for interaction with mannan-binding lectin
    • Arnold JN, Radcliffe CM, Wormald MR, Royle L, Harvey DJ, et al. 2004. The glycosylation of human serum IgD and IgE and the accessibility of identified oligomannose structures for interaction with mannan-binding lectin. J. Immunol. 173:6831-40
    • (2004) J. Immunol. , vol.173 , pp. 6831-6840
    • Arnold, J.N.1    Radcliffe, C.M.2    Wormald, M.R.3    Royle, L.4    Harvey, D.J.5
  • 3
    • 0033952103 scopus 로고    scopus 로고
    • Human neutralizingmonoclonal antibodies of the IgG1 subtype protect against mucosal simian-human immunodeficiency virus infection
    • Baba TW, Liska V, Hofmann-Lehmann R, Vlasak J, Xu W, et al. 2000. Human neutralizingmonoclonal antibodies of the IgG1 subtype protect against mucosal simian-human immunodeficiency virus infection. Nat. Med. 6:200-6
    • (2000) Nat. Med. , vol.6 , pp. 200-206
    • Baba, T.W.1    Liska, V.2    Hofmann-Lehmann, R.3    Vlasak, J.4    Xu, W.5
  • 4
    • 84855466746 scopus 로고    scopus 로고
    • Antibody-based protection against HIV infection by vectored immunoprophylaxis
    • Balazs AB, Chen J, Hong CM, Rao DS, Yang L, Baltimore D. 2011. Antibody-based protection against HIV infection by vectored immunoprophylaxis. Nature 481:81-84
    • (2011) Nature , vol.481 , pp. 81-84
    • Balazs, A.B.1    Chen, J.2    Hong, C.M.3    Rao, D.S.4    Yang, L.5    Baltimore, D.6
  • 5
    • 84890196626 scopus 로고    scopus 로고
    • Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy
    • Bartesaghi A, Merk A, Borgnia MJ, Milne JL, Subramaniam S. 2013. Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy. Nat. Struct. Mol. Biol. 20:1352-57
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1352-1357
    • Bartesaghi, A.1    Merk, A.2    Borgnia, M.J.3    Milne, J.L.4    Subramaniam, S.5
  • 6
    • 85016231197 scopus 로고    scopus 로고
    • Structural principles controlling HIV envelope glycosylation
    • Behrens AJ, CrispinM. 2017. Structural principles controlling HIV envelope glycosylation. Curr. Opin. Struct. Biol. 44:125-33
    • (2017) Curr. Opin. Struct. Biol. , vol.44 , pp. 125-133
    • Behrens, A.J.1    Crispin, M.2
  • 7
    • 85008682118 scopus 로고    scopus 로고
    • Molecular architecture of the cleavagedependent mannose patch on a soluble HIV-1 envelope glycoprotein trimer
    • Behrens AJ, Harvey DJ, Milne E, Cupo A, Kumar A, et al. 2017. Molecular architecture of the cleavagedependent mannose patch on a soluble HIV-1 envelope glycoprotein trimer. J. Virol. 91:e01894-16
    • (2017) J. Virol. , vol.91 , pp. e01894-e01916
    • Behrens, A.J.1    Harvey, D.J.2    Milne, E.3    Cupo, A.4    Kumar, A.5
  • 8
    • 84959932564 scopus 로고    scopus 로고
    • Composition and antigenic effects of individual glycan sites of a trimeric HIV-1 envelope glycoprotein
    • Behrens AJ, Vasiljevic S, Pritchard LK, Harvey DJ, Andev RS, et al. 2016. Composition and antigenic effects of individual glycan sites of a trimeric HIV-1 envelope glycoprotein. Cell Rep. 14:2695-706
    • (2016) Cell Rep. , vol.14 , pp. 2695-2706
    • Behrens, A.J.1    Vasiljevic, S.2    Pritchard, L.K.3    Harvey, D.J.4    Andev, R.S.5
  • 9
    • 0033985999 scopus 로고    scopus 로고
    • A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure
    • Binley JM, Sanders RW, Clas B, Schuelke N, Master A, et al. 2000. A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure. J. Virol. 74:627-43
    • (2000) J. Virol. , vol.74 , pp. 627-643
    • Binley, J.M.1    Sanders, R.W.2    Clas, B.3    Schuelke, N.4    Master, A.5
  • 10
    • 0036184790 scopus 로고    scopus 로고
    • Enhancing the proteolytic maturation of human immunodeficiency virus type 1 envelope glycoproteins
    • Binley JM, Sanders RW, Master A, Cayanan CS, Wiley CL, et al. 2002. Enhancing the proteolytic maturation of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 76:2606-16
    • (2002) J. Virol. , vol.76 , pp. 2606-2616
    • Binley, J.M.1    Sanders, R.W.2    Master, A.3    Cayanan, C.S.4    Wiley, C.L.5
  • 11
    • 84900467984 scopus 로고    scopus 로고
    • Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers
    • Blattner C, Lee JH, SliepenK, Derking R, FalkowskaE, et al. 2014. Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. Immunity 40:669-80
    • (2014) Immunity , vol.40 , pp. 669-680
    • Blattner, C.1    Lee, J.H.2    Sliepen, K.3    Derking, R.4    Falkowska, E.5
  • 12
    • 10344233222 scopus 로고    scopus 로고
    • Printed covalent glycan array for ligand profiling of diverse glycan binding proteins
    • Blixt O, Head S, Mondala T, Scanlan C, Huflejt ME, et al. 2004. Printed covalent glycan array for ligand profiling of diverse glycan binding proteins. PNAS 101:17033-38
    • (2004) PNAS , vol.101 , pp. 17033-17038
    • Blixt, O.1    Head, S.2    Mondala, T.3    Scanlan, C.4    Huflejt, M.E.5
  • 13
    • 80051677678 scopus 로고    scopus 로고
    • The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade
    • Bonomelli C, Doores KJ, Dunlop DC, Thaney V, Dwek RA, et al. 2011. The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade. PLOS ONE 6:e23521
    • (2011) PLOS ONE , vol.6 , pp. e23521
    • Bonomelli, C.1    Doores, K.J.2    Dunlop, D.C.3    Thaney, V.4    Dwek, R.A.5
  • 14
    • 84986296891 scopus 로고    scopus 로고
    • Tailored immunogens direct affinity maturation toward HIV neutralizing antibodies
    • e11
    • Briney B, Sok D, Jardine JG, Kulp DW, Skog P, et al. 2016. Tailored immunogens direct affinity maturation toward HIV neutralizing antibodies. Cell 166:1459-70.e11
    • (2016) Cell , vol.166 , pp. 1459-1470
    • Briney, B.1    Sok, D.2    Jardine, J.G.3    Kulp, D.W.4    Skog, P.5
  • 15
    • 3242672218 scopus 로고    scopus 로고
    • Covalent display of oligosaccharide arrays in microtiter plates
    • Bryan MC, Fazio F, Lee HK, Huang CY, Chang A, et al. 2004. Covalent display of oligosaccharide arrays in microtiter plates. J. Am. Chem. Soc. 126:8640-41
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8640-8641
    • Bryan, M.C.1    Fazio, F.2    Lee, H.K.3    Huang, C.Y.4    Chang, A.5
  • 17
    • 84969835812 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies to HIV and their role in vaccine design
    • Burton DR, Hangartner L. 2016. Broadly neutralizing antibodies to HIV and their role in vaccine design. Annu. Rev. Immunol. 34:635-59
    • (2016) Annu. Rev. Immunol. , vol.34 , pp. 635-659
    • Burton, D.R.1    Hangartner, L.2
  • 18
    • 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. 16:571-76
    • (2015) Nat. Immunol. , vol.16 , pp. 571-576
    • Burton, D.R.1    Mascola, J.R.2
  • 19
    • 12444291017 scopus 로고    scopus 로고
    • Antibody domain exchange is an immunological solution to carbohydrate cluster recognition
    • Calarese DA, Scanlan CN, Zwick MB, Deechongkit S, Mimura Y, et al. 2003. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300:2065-71
    • (2003) Science , vol.300 , pp. 2065-2071
    • Calarese, D.A.1    Scanlan, C.N.2    Zwick, M.B.3    Deechongkit, S.4    Mimura, Y.5
  • 20
    • 85019399814 scopus 로고    scopus 로고
    • Virus-like particles identify an HIV V1V2 apex-binding neutralizing antibody that lacks a protruding loop
    • Cale EM, Gorman J, Radakovich NA, Crooks ET, Osawa K, et al. 2017. Virus-like particles identify an HIV V1V2 apex-binding neutralizing antibody that lacks a protruding loop. Immunity 46:777-91
    • (2017) Immunity , vol.46 , pp. 777-791
    • Cale, E.M.1    Gorman, J.2    Radakovich, N.A.3    Crooks, E.T.4    Osawa, K.5
  • 21
    • 85016232433 scopus 로고    scopus 로고
    • Global site-specific N-glycosylation analysis of HIV envelope glycoprotein
    • Cao L, Diedrich JK, Kulp DW, Pauthner M, He L, et al. 2017. Global site-specific N-glycosylation analysis of HIV envelope glycoprotein. Nat. Commun. 8:14954
    • (2017) Nat. Commun. , vol.8 , pp. 14954
    • Cao, L.1    Diedrich, J.K.2    Kulp, D.W.3    Pauthner, M.4    He, L.5
  • 22
    • 77957113558 scopus 로고    scopus 로고
    • Glycan array on aluminum oxide-coated glass slides through phosphonate chemistry
    • Chang SH, Han JL, Tseng SY, Lee HY, Lin CW, et al. 2010. Glycan array on aluminum oxide-coated glass slides through phosphonate chemistry. J. Am. Chem. Soc. 132:13371-80
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13371-13380
    • Chang, S.H.1    Han, J.L.2    Tseng, S.Y.3    Lee, H.Y.4    Lin, C.W.5
  • 24
    • 85001115582 scopus 로고    scopus 로고
    • HIV-1 glycan density drives the persistence of the mannose patch within an infected individual
    • Coss KP, Vasiljevic S, Pritchard LK, Krumm SA, Glaze M, et al. 2016. HIV-1 glycan density drives the persistence of the mannose patch within an infected individual. J. Virol. 90:11132-44
    • (2016) J. Virol. , vol.90 , pp. 11132-11144
    • Coss, K.P.1    Vasiljevic, S.2    Pritchard, L.K.3    Krumm, S.A.4    Glaze, M.5
  • 25
    • 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
  • 26
    • 2442487932 scopus 로고    scopus 로고
    • Monoglucosylated glycans in the secreted human complement component C3: Implications for protein biosynthesis and structure
    • Crispin M, Ritchie GE, Critchley AJ, Morgan BP, Wilson IA, et al. 2004. Monoglucosylated glycans in the secreted human complement component C3: implications for protein biosynthesis and structure. FEBS Lett. 566:270-74
    • (2004) FEBS Lett. , vol.566 , pp. 270-274
    • Crispin, M.1    Ritchie, G.E.2    Critchley, A.J.3    Morgan, B.P.4    Wilson, I.A.5
  • 28
    • 85014472256 scopus 로고    scopus 로고
    • Effects of partially dismantling the CD4 binding site glycan fence of HIV-1 Envelope glycoprotein trimers on neutralizing antibody induction
    • Crooks ET, Osawa K, Tong T, Grimley SL, Dai YD, et al. 2017. Effects of partially dismantling the CD4 binding site glycan fence of HIV-1 Envelope glycoprotein trimers on neutralizing antibody induction. Virology 505:193-209
    • (2017) Virology , vol.505 , pp. 193-209
    • Crooks, E.T.1    Osawa, K.2    Tong, T.3    Grimley, S.L.4    Dai, Y.D.5
  • 29
    • 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, 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
  • 30
    • 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. 15:1545-55
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 1545-1555
    • Cutalo, J.M.1    Deterding, L.J.2    Tomer, K.B.3
  • 31
    • 84950267324 scopus 로고    scopus 로고
    • Immunogenicity of stabilizedHIV-1 envelope trimers with reduced exposure of non-neutralizing epitopes
    • de Taeye SW, Ozorowski G, Torrents de la Pena A, Guttman M, Julien J-P, et al. 2015. Immunogenicity of stabilizedHIV-1 envelope trimers with reduced exposure of non-neutralizing epitopes. Cell 163:1702-15
    • (2015) Cell , vol.163 , pp. 1702-1715
    • De Taeye, S.W.1    Ozorowski, G.2    De La Pena, A.3    Guttman, M.4    Julien, J.-P.5
  • 32
    • 0028362008 scopus 로고
    • The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM)
    • Decroly E, Vandenbranden M, Ruysschaert JM, Cogniaux J, JacobGS, et al. 1994. The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM). J. Biol. Chem. 269:12240-47
    • (1994) J. Biol. Chem. , vol.269 , pp. 12240-12247
    • Decroly, E.1    Vandenbranden, M.2    Ruysschaert, J.M.3    Cogniaux, J.4    Jacob, G.S.5
  • 33
    • 77953673590 scopus 로고    scopus 로고
    • Therapeutic antibodies, vaccines and antibodyomes
    • Dimitrov DS. 2010. Therapeutic antibodies, vaccines and antibodyomes. mAbs 2:347-56
    • (2010) MAbs , vol.2 , pp. 347-356
    • Dimitrov, D.S.1
  • 35
    • 84959117772 scopus 로고    scopus 로고
    • The HIV glycan shield as a target for broadly neutralizing antibodies
    • Doores KJ. 2015. The HIV glycan shield as a target for broadly neutralizing antibodies. FEBS J. 282:4679-91
    • (2015) FEBS J. , vol.282 , pp. 4679-4691
    • Doores, K.J.1
  • 36
    • 77956385205 scopus 로고    scopus 로고
    • Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens
    • Doores KJ, Bonomelli C, Harvey DJ, Vasiljevic S, Dwek RA, et al. 2010. Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens. PNAS 107:13800-5
    • (2010) PNAS , vol.107 , pp. 13800-13805
    • Doores, K.J.1    Bonomelli, C.2    Harvey, D.J.3    Vasiljevic, S.4    Dwek, R.A.5
  • 38
    • 0026557112 scopus 로고
    • Prevention of HIV-1 infection in chimpanzees by gp120 V3 domain-specific monoclonal antibody
    • Emini EA, Schleif WA, Nunberg JH, Conley AJ, Eda Y, et al. 1992. Prevention of HIV-1 infection in chimpanzees by gp120 V3 domain-specific monoclonal antibody. Nature 355:728-30
    • (1992) Nature , vol.355 , pp. 728-730
    • Emini, E.A.1    Schleif, W.A.2    Nunberg, J.H.3    Conley, A.J.4    Eda, Y.5
  • 39
  • 40
    • 84900517557 scopus 로고    scopus 로고
    • Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers
    • Falkowska E, Le KM, Ramos A, Doores KJ, Lee JH, et al. 2014. Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers. Immunity 40:657-68
    • (2014) Immunity , vol.40 , pp. 657-668
    • Falkowska, E.1    Le, K.M.2    Ramos, A.3    Doores, K.J.4    Lee, J.H.5
  • 41
    • 84946045414 scopus 로고    scopus 로고
    • A new glycan-dependent CD4-binding site neutralizing antibody exerts pressure on HIV-1 in vivo
    • Freund NT, Horwitz JA, Nogueira L, Sievers SA, Scharf L, et al. 2015. A new glycan-dependent CD4-binding site neutralizing antibody exerts pressure on HIV-1 in vivo. PLOS Pathog. 11:e1005238
    • (2015) PLOS Pathog. , vol.11 , pp. e1005238
    • Freund, N.T.1    Horwitz, J.A.2    Nogueira, L.3    Sievers, S.A.4    Scharf, L.5
  • 42
    • 0036788485 scopus 로고    scopus 로고
    • Oligosaccharide microarrays for highthroughput detection and specificity assignments of carbohydrate-protein interactions
    • Fukui S, Feizi T, Galustian C, Lawson AM, Chai W. 2002. Oligosaccharide microarrays for highthroughput detection and specificity assignments of carbohydrate-protein interactions. Nat. Biotechnol. 20:1011-17
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1011-1017
    • Fukui, S.1    Feizi, T.2    Galustian, C.3    Lawson, A.M.4    Chai, W.5
  • 43
    • 84963620358 scopus 로고    scopus 로고
    • Affinity maturation of a potent family of HIV antibodies is primarily focused on accommodating or avoiding glycans
    • Garces F, Lee JH, de Val N, de la Pena AT, Kong L, et al. 2015. Affinity maturation of a potent family of HIV antibodies is primarily focused on accommodating or avoiding glycans. Immunity 43:1053-63
    • (2015) Immunity , vol.43 , pp. 1053-1063
    • Garces, F.1    Lee, J.H.2    De Val, N.3    De La Pena, A.T.4    Kong, L.5
  • 44
    • 84907527916 scopus 로고    scopus 로고
    • Structural evolution of glycan recognition by a family of potent HIV antibodies
    • Garces F, Sok D, Kong L, McBride R, Kim HJ, et al. 2014. Structural evolution of glycan recognition by a family of potent HIV antibodies. Cell 159:69-79
    • (2014) Cell , vol.159 , pp. 69-79
    • Garces, F.1    Sok, D.2    Kong, L.3    McBride, R.4    Kim, H.J.5
  • 45
    • 84975462735 scopus 로고    scopus 로고
    • Glycan arrays: From basic biochemical research to bioanalytical and biomedical applications
    • Geissner A, Seeberger PH. 2016. Glycan arrays: from basic biochemical research to bioanalytical and biomedical applications. Annu. Rev. Anal. Chem. 9:223-47
    • (2016) Annu. Rev. Anal. Chem. , vol.9 , pp. 223-247
    • Geissner, A.1    Seeberger, P.H.2
  • 46
    • 85017545019 scopus 로고    scopus 로고
    • Glycosylation benchmark profile for HIV-1 envelope glycoprotein production based on eleven Env trimers
    • Go EP, Ding H, Zhang S, Ringe RP, Nicely N, et al. 2017. Glycosylation benchmark profile for HIV-1 envelope glycoprotein production based on eleven Env trimers. J. Virol. 91:e02428-16
    • (2017) J. Virol. , vol.91 , pp. e02428-e02516
    • Go, E.P.1    Ding, H.2    Zhang, S.3    Ringe, R.P.4    Nicely, N.5
  • 47
    • 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, et al. 2015. Comparative analysis of the glycosylation profiles of membrane-anchored HIV-1 envelope glycoprotein trimers and soluble gp140. J. Virol. 89:8245-57
    • (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
  • 48
    • 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 H-X, 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. 12:1223-34
    • (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
  • 49
    • 34548046221 scopus 로고    scopus 로고
    • Mammalian N-glycan branching protects against innate immune self-recognition and inflammation in autoimmune disease pathogenesis
    • Green RS, Stone EL, Tenno M, Lehtonen E, Farquhar MG, Marth JD. 2007. Mammalian N-glycan branching protects against innate immune self-recognition and inflammation in autoimmune disease pathogenesis. Immunity 27:308-20
    • (2007) Immunity , vol.27 , pp. 308-320
    • Green, R.S.1    Stone, E.L.2    Tenno, M.3    Lehtonen, E.4    Farquhar, M.G.5    Marth, J.D.6
  • 50
    • 84987652813 scopus 로고    scopus 로고
    • Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site
    • Gristick HB, von Boehmer L, West AP Jr., SchamberM, Gazumyan A, et al. 2016. Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site. Nat. Struct. Mol. Biol. 23:906-15
    • (2016) Nat. Struct. Mol. Biol. , vol.23 , pp. 906-915
    • Gristick, H.B.1    Von Boehmer, L.2    West, A.P.3    Schamber, M.4    Gazumyan, A.5
  • 51
    • 84961124024 scopus 로고    scopus 로고
    • Structure-guided redesign increases the propensity of HIV Env to generate highly stable soluble trimers
    • Guenaga J, Dubrovskaya V, de Val N, Sharma SK, Carrette B, et al. 2015. Structure-guided redesign increases the propensity of HIV Env to generate highly stable soluble trimers. J. Virol. 90:2806-17
    • (2015) J. Virol. , vol.90 , pp. 2806-2817
    • Guenaga, J.1    Dubrovskaya, V.2    De Val, N.3    Sharma, S.K.4    Carrette, B.5
  • 52
    • 85019482085 scopus 로고    scopus 로고
    • Glycine substitution at helix-to-coil transitions facilitates the structural determination of a stabilized subtype C HIV envelope glycoprotein
    • Guenaga J, Garces F, de Val N, Stanfield RL, Dubrovskaya V, et al. 2017. Glycine substitution at helix-to-coil transitions facilitates the structural determination of a stabilized subtype C HIV envelope glycoprotein. Immunity 46:792-803
    • (2017) Immunity , vol.46 , pp. 792-803
    • Guenaga, J.1    Garces, F.2    De Val, N.3    Stanfield, R.L.4    Dubrovskaya, V.5
  • 54
    • 67249131966 scopus 로고    scopus 로고
    • Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers
    • Hessell AJ, Rakasz EG, Poignard P, Hangartner L, Landucci G, et al. 2009. Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers. PLOS Pathog. 5:e1000433
    • (2009) PLOS Pathog. , vol.5 , pp. e1000433
    • Hessell, A.J.1    Rakasz, E.G.2    Poignard, P.3    Hangartner, L.4    Landucci, G.5
  • 55
    • 73949154006 scopus 로고    scopus 로고
    • Broadly neutralizing monoclonal antibodies 2F5 and 4E10 directed against the human immunodeficiency virus type 1 gp41 membrane-proximal external region protect against mucosal challenge by simian-human immunodeficiency virus SHIVBa-L
    • Hessell AJ, Rakasz EG, Tehrani DM, Huber M, Weisgrau KL, et al. 2010. Broadly neutralizing monoclonal antibodies 2F5 and 4E10 directed against the human immunodeficiency virus type 1 gp41 membrane-proximal external region protect against mucosal challenge by simian-human immunodeficiency virus SHIVBa-L. J. Virol. 84:1302-13
    • (2010) J. Virol. , vol.84 , pp. 1302-1313
    • Hessell, A.J.1    Rakasz, E.G.2    Tehrani, D.M.3    Huber, M.4    Weisgrau, K.L.5
  • 56
    • 84942134414 scopus 로고    scopus 로고
    • Murine antibody responses to cleaved soluble HIV-1 envelope trimers are highly restricted in specificity
    • Hu JK, Crampton JC, Cupo A, Ketas T, van Gils MJ, et al. 2015. Murine antibody responses to cleaved soluble HIV-1 envelope trimers are highly restricted in specificity. J. Virol. 89:10383-98
    • (2015) J. Virol. , vol.89 , pp. 10383-10398
    • Hu, J.K.1    Crampton, J.C.2    Cupo, A.3    Ketas, T.4    Van Gils, M.J.5
  • 57
    • 84921607768 scopus 로고    scopus 로고
    • Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface
    • Huang J, Kang BH, Pancera M, Lee JH, Tong T, et al. 2014. Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface. Nature 515:138-42
    • (2014) Nature , vol.515 , pp. 138-142
    • Huang, J.1    Kang, B.H.2    Pancera, M.3    Lee, J.H.4    Tong, T.5
  • 58
    • 84877609579 scopus 로고    scopus 로고
    • Rational HIV immunogen design to target specific germline B cell receptors
    • Jardine JG, Julien J-P, Menis S, Ota T, Kalyuzhniy O, et al. 2013. Rational HIV immunogen design to target specific germline B cell receptors. Science 340:711-16
    • (2013) Science , vol.340 , pp. 711-716
    • Jardine, J.G.1    Julien, J.-P.2    Menis, S.3    Ota, T.4    Kalyuzhniy, O.5
  • 59
    • 84962251178 scopus 로고    scopus 로고
    • HIV-1 broadly neutralizing antibody precursor B cells revealed by germline-targeting immunogen
    • Jardine JG, KulpDW, Havenar-DaughtonC, Sarkar A, Briney B, et al. 2016. HIV-1 broadly neutralizing antibody precursor B cells revealed by germline-targeting immunogen. Science 351:1458-63
    • (2016) Science , vol.351 , pp. 1458-1463
    • Jardine, J.G.1    Kulp, D.W.2    Havenar-Daughton, C.3    Sarkar, A.4    Briney, B.5
  • 60
    • 84934954773 scopus 로고    scopus 로고
    • Priming a broadly neutralizing antibody response to HIV-1 using a germline-targeting immunogen
    • Jardine JG, Ota T, Sok D, Pauthner M, Kulp DW, et al. 2015. Priming a broadly neutralizing antibody response to HIV-1 using a germline-targeting immunogen. Science 349:156-61
    • (2015) Science , vol.349 , pp. 156-161
    • Jardine, J.G.1    Ota, T.2    Sok, D.3    Pauthner, M.4    Kulp, D.W.5
  • 61
    • 84984802096 scopus 로고    scopus 로고
    • Minimally mutated HIV-1 broadly neutralizing antibodies to guide reductionist vaccine design
    • Jardine JG, Sok D, Julien J-P, Briney B, Sarkar A, et al. 2016. Minimally mutated HIV-1 broadly neutralizing antibodies to guide reductionist vaccine design. PLOS Pathog. 12:e1005815
    • (2016) PLOS Pathog. , vol.12 , pp. e1005815
    • Jardine, J.G.1    Sok, D.2    Julien, J.-P.3    Briney, B.4    Sarkar, A.5
  • 62
    • 84890858459 scopus 로고    scopus 로고
    • Crystal structure of a soluble cleaved HIV-1 envelope trimer
    • Julien J-P, Cupo A, Sok D, Stanfield RL, Lyumkis D, et al. 2013. Crystal structure of a soluble cleaved HIV-1 envelope trimer. Science 342:1477-83
    • (2013) Science , vol.342 , pp. 1477-1483
    • Julien, J.-P.1    Cupo, A.2    Sok, D.3    Stanfield, R.L.4    Lyumkis, D.5
  • 63
    • 84875034460 scopus 로고    scopus 로고
    • Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9
    • Julien J-P, Lee JH, Cupo A, Murin CD, Derking R, et al. 2013. Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9. PNAS 110:4351-56
    • (2013) PNAS , vol.110 , pp. 4351-4356
    • Julien, J.-P.1    Lee, J.H.2    Cupo, A.3    Murin, C.D.4    Derking, R.5
  • 64
    • 84942856317 scopus 로고    scopus 로고
    • Design and structure of two HIV-1 clade C SOSIP 664 trimers that increase the arsenal of native-like Env immunogens
    • Julien J-P, Lee JH, Ozorowski G, Hua Y, Torrents de la Pena A, et al. 2015. Design and structure of two HIV-1 clade C SOSIP.664 trimers that increase the arsenal of native-like Env immunogens. PNAS 112:11947-52
    • (2015) PNAS , vol.112 , pp. 11947-11952
    • Julien, J.-P.1    Lee, J.H.2    Ozorowski, G.3    Hua, Y.4    De La Pena, A.5
  • 65
    • 84867427047 scopus 로고    scopus 로고
    • Structural insights into key sites of vulnerability onHIV-1 Env and influenza HA
    • Julien J-P, Lee PS, Wilson IA. 2012. Structural insights into key sites of vulnerability onHIV-1 Env and influenza HA. Immunol. Rev. 250:180-98
    • (2012) Immunol. Rev. , vol.250 , pp. 180-198
    • Julien, J.-P.1    Lee, P.S.2    Wilson, I.A.3
  • 66
    • 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 J-P, Sok D, Khayat R, Lee JH, Doores KJ, 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
  • 67
    • 84883275866 scopus 로고    scopus 로고
    • Structural characterization of cleaved, soluble HIV-1 envelope glycoprotein trimers
    • Khayat R, Lee JH, Julien J-P, Cupo A, Klasse PJ, et al. 2013. Structural characterization of cleaved, soluble HIV-1 envelope glycoprotein trimers. J. Virol. 87:9865-72
    • (2013) J. Virol. , vol.87 , pp. 9865-9872
    • Khayat, R.1    Lee, J.H.2    Julien, J.-P.3    Cupo, A.4    Klasse, P.J.5
  • 69
    • 84989899203 scopus 로고    scopus 로고
    • Sequential and simultaneous immunization of rabbits with HIV-1 envelope glycoprotein SOSIP 664 trimers from Clades A, B and C
    • Klasse PJ, LaBranche CC, Ketas TJ, Ozorowski G, Cupo A, et al. 2016. Sequential and simultaneous immunization of rabbits with HIV-1 envelope glycoprotein SOSIP.664 trimers from Clades A, B and C. PLOS Pathog. 12:e1005864
    • (2016) PLOS Pathog. , vol.12 , pp. e1005864
    • Klasse, P.J.1    LaBranche, C.C.2    Ketas, T.J.3    Ozorowski, G.4    Cupo, A.5
  • 70
    • 84866443327 scopus 로고    scopus 로고
    • Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein
    • Klein F, Gaebler C, Mouquet H, Sather DN, Lehmann C, et al. 2012. Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein. J. Exp. Med. 209:1469-79
    • (2012) J. Exp. Med. , vol.209 , pp. 1469-1479
    • Klein, F.1    Gaebler, C.2    Mouquet, H.3    Sather, D.N.4    Lehmann, C.5
  • 71
    • 84976633087 scopus 로고    scopus 로고
    • Uncleaved prefusion-optimized gp140 trimers derived from analysis of HIV-1 envelope metastability
    • Kong L, He L, de Val N, Vora N, Morris CD, et al. 2016. Uncleaved prefusion-optimized gp140 trimers derived from analysis of HIV-1 envelope metastability. Nat. Commun. 7:12040
    • (2016) Nat. Commun. , vol.7 , pp. 12040
    • Kong, L.1    He, L.2    De Val, N.3    Vora, N.4    Morris, C.D.5
  • 72
    • 84880161438 scopus 로고    scopus 로고
    • Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120
    • Kong L, Lee JH, Doores KJ, Murin CD, Julien J-P, et al. 2013. Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120. Nat. Struct. Mol. Biol. 20:796-803
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 796-803
    • Kong, L.1    Lee, J.H.2    Doores, K.J.3    Murin, C.D.4    Julien, J.-P.5
  • 73
    • 84944190259 scopus 로고    scopus 로고
    • Complete epitopes for vaccine design derived from a crystal structure of the broadly neutralizing antibodies PGT128 and 8ANC195 in complex with an HIV-1 Env trimer
    • Kong L, Torrents de la Pena A, Deller MC, Garces F, Sliepen K, et al. 2015. Complete epitopes for vaccine design derived from a crystal structure of the broadly neutralizing antibodies PGT128 and 8ANC195 in complex with an HIV-1 Env trimer. Acta Crystallogr. D Biol. Crystallogr. 71:2099-108
    • (2015) Acta Crystallogr. D Biol. Crystallogr. , vol.71 , pp. 2099-2108
    • Kong, L.1    De La Pena, A.2    Deller, M.C.3    Garces, F.4    Sliepen, K.5
  • 74
    • 0033548254 scopus 로고    scopus 로고
    • Probability analysis of variational crystallization and its application to gp120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1)
    • Kwong PD, Wyatt R, Desjardins E, Robinson J, Culp JS, et al. 1999. Probability analysis of variational crystallization and its application to gp120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1). J. Biol. Chem. 274:4115-23
    • (1999) J. Biol. Chem. , vol.274 , pp. 4115-4123
    • Kwong, P.D.1    Wyatt, R.2    Desjardins, E.3    Robinson, J.4    Culp, J.S.5
  • 75
    • 0026322017 scopus 로고
    • Characterisation of minor tetrato hepta-saccharides O-linked to human meconium glycoproteins by t.l.c.-m.s.microsequencing of neoglycolipid derivatives in conjunction with conventional m.s.and 1H-n.m.r.spectroscopy
    • Lawson AM, Hounsell EF, Stoll MS, Feeney J, Chai WG, et al. 1991. Characterisation of minor tetrato hepta-saccharides O-linked to human meconium glycoproteins by t.l.c.-m.s. microsequencing of neoglycolipid derivatives in conjunction with conventional m.s. and 1H-n.m.r. spectroscopy. Carbohydr. Res. 221:191-208
    • (1991) Carbohydr. Res. , vol.221 , pp. 191-208
    • Lawson, A.M.1    Hounsell, E.F.2    Stoll, M.S.3    Feeney, J.4    Chai, W.G.5
  • 76
    • 85019040760 scopus 로고    scopus 로고
    • A broadly neutralizing antibody targets the dynamic HIV envelope trimer apex via a long, rigidified, and anionic β-hairpin structure
    • Lee JH, Andrabi R, Su C-Y, Yasmeen A, Julien J-P, et al. 2017. A broadly neutralizing antibody targets the dynamic HIV envelope trimer apex via a long, rigidified, and anionic β-hairpin structure. Immunity 46:690-702
    • (2017) Immunity , vol.46 , pp. 690-702
    • Lee, J.H.1    Andrabi, R.2    Su, C.-Y.3    Yasmeen, A.4    Julien, J.-P.5
  • 77
    • 84943588030 scopus 로고    scopus 로고
    • Model building and refinement of a natively glycosylated HIV-1 Env protein by high-resolution cryoelectron microscopy
    • Lee JH, de Val N, LyumkisD, Ward AB. 2015. Model building and refinement of a natively glycosylated HIV-1 Env protein by high-resolution cryoelectron microscopy. Structure 23:1943-51
    • (2015) Structure , vol.23 , pp. 1943-1951
    • Lee, J.H.1    De Val, N.2    Lyumkis, D.3    Ward, A.B.4
  • 78
    • 84961231130 scopus 로고    scopus 로고
    • Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
    • Lee JH, OzorowskiG, Ward AB. 2016. Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer. Science 351:1043-48
    • (2016) Science , vol.351 , pp. 1043-1048
    • Lee, J.H.1    Ozorowski, G.2    Ward, A.B.3
  • 79
    • 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. 265:10373-82
    • (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
  • 80
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li X, Mooney P, Zheng S, Booth CR, Braunfeld MB, et al. 2013. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10:584-90
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1    Mooney, P.2    Zheng, S.3    Booth, C.R.4    Braunfeld, M.B.5
  • 81
    • 34948854718 scopus 로고    scopus 로고
    • Broad HIV-1 neutralization mediated by CD4-binding site antibodies
    • Li Y, Migueles SA, Welcher B, Svehla K, Phogat A, et al. 2007. Broad HIV-1 neutralization mediated by CD4-binding site antibodies. Nat. Med. 13:1032-34
    • (2007) Nat. Med. , vol.13 , pp. 1032-1034
    • Li, Y.1    Migueles, S.A.2    Welcher, B.3    Svehla, K.4    Phogat, A.5
  • 82
    • 85018259958 scopus 로고    scopus 로고
    • Conformational states of a soluble, uncleaved HIV-1 envelope trimer
    • Liu Y, Pan J, Cai Y, Grigorieff N, Harrison SC, Chen B. 2017. Conformational states of a soluble, uncleaved HIV-1 envelope trimer. J. Virol. 91:e00175-17
    • (2017) J. Virol. , vol.91 , pp. e00175-e00217
    • Liu, Y.1    Pan, J.2    Cai, Y.3    Grigorieff, N.4    Harrison, S.C.5    Chen, B.6
  • 83
    • 85019596288 scopus 로고    scopus 로고
    • CryoEM structure of an influenza virus receptor-binding site antibody-antigen interface
    • Liu Y, Pan J, Jenni S, Raymond DD, Caradonna T, et al. 2017. CryoEM structure of an influenza virus receptor-binding site antibody-antigen interface. J. Mol. Biol. 429:1829-39
    • (2017) J. Mol. Biol. , vol.429 , pp. 1829-1839
    • Liu, Y.1    Pan, J.2    Jenni, S.3    Raymond, D.D.4    Caradonna, T.5
  • 85
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • LyumkisD, Julien J-P, de Val N, Cupo A, PotterCS, et al. 2013. Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science 342:1484-90
    • (2013) Science , vol.342 , pp. 1484-1490
    • Lyumkis, D.1    Julien, J.-P.2    De Val, N.3    Cupo, A.4    Potter, C.S.5
  • 86
    • 0032947286 scopus 로고    scopus 로고
    • Protection of macaques against pathogenic simian/human immunodeficiency virus 89 6PD by passive transfer of neutralizing antibodies
    • Mascola JR, Lewis MG, Stiegler G, Harris D, VanCott TC, et al. 1999. Protection of macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies. J. Virol. 73:4009-18
    • (1999) J. Virol. , vol.73 , pp. 4009-4018
    • Mascola, J.R.1    Lewis, M.G.2    Stiegler, G.3    Harris, D.4    VanCott, T.C.5
  • 87
    • 85010908338 scopus 로고    scopus 로고
    • Identification and specificity of broadly neutralizing antibodies against HIV
    • McCoy LE, Burton DR. 2017. Identification and specificity of broadly neutralizing antibodies against HIV. Immunol. Rev. 275:11-20
    • (2017) Immunol. Rev. , vol.275 , pp. 11-20
    • McCoy, L.E.1    Burton, D.R.2
  • 88
    • 84940763233 scopus 로고    scopus 로고
    • Incomplete neutralization and deviation from sigmoidal neutralization curves forHIV broadly neutralizingmonoclonal antibodies
    • McCoy LE, Falkowska E, Doores KJ, Le K, Sok D, et al. 2015. Incomplete neutralization and deviation from sigmoidal neutralization curves forHIV broadly neutralizingmonoclonal antibodies. PLOS Pathog. 11:e1005110
    • (2015) PLOS Pathog. , vol.11 , pp. e1005110
    • McCoy, L.E.1    Falkowska, E.2    Doores, K.J.3    Le, K.4    Sok, D.5
  • 89
    • 84989809446 scopus 로고    scopus 로고
    • Holes in the glycan shield of the native HIV envelope are a target of trimer-elicited neutralizing antibodies
    • McCoy LE, van Gils MJ, Ozorowski G, Messmer T, Briney B, et al. 2016. Holes in the glycan shield of the native HIV envelope are a target of trimer-elicited neutralizing antibodies. Cell Rep. 16:2327-38
    • (2016) Cell Rep. , vol.16 , pp. 2327-2338
    • McCoy, L.E.1    Van Gils, M.J.2    Ozorowski, G.3    Messmer, T.4    Briney, B.5
  • 90
    • 83455254775 scopus 로고    scopus 로고
    • Structure ofHIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • McLellan JS, Pancera M, Carrico C, Gorman J, Julien J-P, et al. 2011. Structure ofHIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 480:336-43
    • (2011) Nature , vol.480 , pp. 336-343
    • McLellan, J.S.1    Pancera, M.2    Carrico, C.3    Gorman, J.4    Julien, J.-P.5
  • 91
    • 85028886518 scopus 로고    scopus 로고
    • Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo
    • Medina-Ramírez M, Garces F, Escolano A, Skog P, de Taeye SW, et al. 2017. Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo. J. Exp. Med. 214:2573-90
    • (2017) J. Exp. Med. , vol.214 , pp. 2573-2590
    • Medina-Ramírez, M.1    Garces, F.2    Escolano, A.3    Skog, P.4    De Taeye, S.W.5
  • 92
    • 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
  • 93
    • 84869232528 scopus 로고    scopus 로고
    • Highly potent HIV-specific antibody neutralization in vitro translates into effective protection against mucosal SHIV challenge in vivo
    • Moldt B, Rakasz EG, Schultz N, Chan-Hui PY, Swiderek K, et al. 2012. Highly potent HIV-specific antibody neutralization in vitro translates into effective protection against mucosal SHIV challenge in vivo. PNAS 109:18921-25
    • (2012) PNAS , vol.109 , pp. 18921-18925
    • Moldt, B.1    Rakasz, E.G.2    Schultz, N.3    Chan-Hui, P.Y.4    Swiderek, K.5
  • 94
    • 0034634728 scopus 로고    scopus 로고
    • Maturation of HIV envelope glycoprotein precursors by cellular endoproteases
    • Moulard M, Decroly E. 2000. Maturation of HIV envelope glycoprotein precursors by cellular endoproteases. Biochim. Biophys. Acta 1469:121-32
    • (2000) Biochim. Biophys. Acta , vol.1469 , pp. 121-132
    • Moulard, M.1    Decroly, E.2
  • 95
    • 85025476641 scopus 로고    scopus 로고
    • Open and closed structures reveal allostery and pliability in the HIV-1 envelope spike
    • Ozorowski G, Pallesen J, de Val N, Lyumkis D, Cottrell CA, et al. 2017. Open and closed structures reveal allostery and pliability in the HIV-1 envelope spike. Nature 547:360-63
    • (2017) Nature , vol.547 , pp. 360-363
    • Ozorowski, G.1    Pallesen, J.2    De Val, N.3    Lyumkis, D.4    Cottrell, C.A.5
  • 96
    • 84867774199 scopus 로고    scopus 로고
    • Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140
    • Pabst M, Chang M, Stadlmann J, Altmann F. 2012. Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140. Biol. Chem. 393:719-30
    • (2012) Biol. Chem. , vol.393 , pp. 719-730
    • Pabst, M.1    Chang, M.2    Stadlmann, J.3    Altmann, F.4
  • 97
  • 98
    • 85028522287 scopus 로고    scopus 로고
    • Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
    • Pallesen J, WangN, Corbett KS, Wrapp D, Kirchdoerfer RN, et al. 2017. Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen. PNAS 114:E7348-57
    • (2017) PNAS , vol.114 , pp. E7348-E7357
    • Pallesen, J.1    Wang, N.2    Corbett, K.S.3    Wrapp, D.4    Kirchdoerfer, R.N.5
  • 100
    • 84909640954 scopus 로고    scopus 로고
    • Structure and immune recognition of trimeric pre-fusion HIV-1 Env
    • Pancera M, Zhou T, Druz A, Georgiev IS, Soto C, et al. 2014. Structure and immune recognition of trimeric pre-fusion HIV-1 Env. Nature 514:455-61
    • (2014) Nature , vol.514 , pp. 455-461
    • Pancera, M.1    Zhou, T.2    Druz, A.3    Georgiev, I.S.4    Soto, C.5
  • 101
    • 84986628335 scopus 로고    scopus 로고
    • Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding
    • Panico M, Bouche L, Binet D, O'Connor MJ, Rahman D, et al. 2016. Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding. Sci. Rep. 6:32956
    • (2016) Sci. Rep. , vol.6 , pp. 32956
    • Panico, M.1    Bouche, L.2    Binet, D.3    O'Connor, M.J.4    Rahman, D.5
  • 102
    • 0034864776 scopus 로고    scopus 로고
    • Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro
    • Parren PW, Marx PA, Hessell AJ, Luckay A, Harouse J, et al. 2001. Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro. J. Virol. 75:8340-47
    • (2001) J. Virol. , vol.75 , pp. 8340-8347
    • Parren, P.W.1    Marx, P.A.2    Hessell, A.J.3    Luckay, A.4    Harouse, J.5
  • 103
    • 82255179322 scopus 로고    scopus 로고
    • A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield
    • Pejchal R, Doores KJ, Walker LM, Khayat R, Huang P-S, et al. 2011. A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield. Science 334:1097-103
    • (2011) Science , vol.334 , pp. 1097-1103
    • Pejchal, R.1    Doores, K.J.2    Walker, L.M.3    Khayat, R.4    Huang, P.-S.5
  • 104
    • 85009935441 scopus 로고    scopus 로고
    • Recent H3N2 viruses have evolved specificity for extended, branched human-type receptors, conferring potential for increased avidity
    • Peng W, de Vries RP, Grant OC, Thompson AJ, McBride R, et al. 2017. Recent H3N2 viruses have evolved specificity for extended, branched human-type receptors, conferring potential for increased avidity. Cell Host Microbe 21:23-34
    • (2017) Cell Host Microbe , vol.21 , pp. 23-34
    • Peng, W.1    De Vries, R.P.2    Grant, O.C.3    Thompson, A.J.4    McBride, R.5
  • 107
    • 84933074280 scopus 로고    scopus 로고
    • Glycan clustering stabilizes themannose patch ofHIV-1 and preserves vulnerability to broadly neutralizing antibodies
    • Pritchard LK, Spencer DI, Royle L, Bonomelli C, Seabright GE, et al. 2015. Glycan clustering stabilizes themannose patch ofHIV-1 and preserves vulnerability to broadly neutralizing antibodies. Nat. Commun. 6:7479
    • (2015) Nat. Commun. , vol.6 , pp. 7479
    • Pritchard, L.K.1    Spencer, D.I.2    Royle, L.3    Bonomelli, C.4    Seabright, G.E.5
  • 108
    • 84930891393 scopus 로고    scopus 로고
    • Glycan microheterogeneity at the PGT135 antibody recognition site onHIV-1 gp120 reveals amolecular mechanism for neutralization resistance
    • Pritchard LK, Spencer DI, Royle L, Vasiljevic S, Krumm SA, et al. 2015. Glycan microheterogeneity at the PGT135 antibody recognition site onHIV-1 gp120 reveals amolecular mechanism for neutralization resistance. J. Virol. 89:6952-59
    • (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
  • 109
    • 84937641486 scopus 로고    scopus 로고
    • Structural constraints determine the glycosylation of HIV-1 envelope trimers
    • Pritchard LK, Vasiljevic S, Ozorowski G, Seabright GE, Cupo A, et al. 2015. Structural constraints determine the glycosylation of HIV-1 envelope trimers. Cell Rep. 11:1604-13
    • (2015) Cell Rep. , vol.11 , pp. 1604-1613
    • Pritchard, L.K.1    Vasiljevic, S.2    Ozorowski, G.3    Seabright, G.E.4    Cupo, A.5
  • 110
    • 84923172318 scopus 로고    scopus 로고
    • A native-like SOSIP 664 trimer based on an HIV-1 subtype B env gene
    • Pugach P, Ozorowski G, Cupo A, Ringe R, Yasmeen A, et al. 2015. A native-like SOSIP.664 trimer based on an HIV-1 subtype B env gene. J. Virol. 89:3380-95
    • (2015) J. Virol. , vol.89 , pp. 3380-3395
    • Pugach, P.1    Ozorowski, G.2    Cupo, A.3    Ringe, R.4    Yasmeen, A.5
  • 112
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Highlevel expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracyclineinducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, Khorana HG. 2002. Structure and function in rhodopsin: highlevel expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracyclineinducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. PNAS 99:13419-24
    • (2002) PNAS , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 113
    • 85023203355 scopus 로고    scopus 로고
    • Reducing V3 antigenicity and immunogenicity on soluble, native-like HIV-1 Env SOSIP trimers
    • Ringe RP, OzorowskiG, Rantalainen K, Struwe WB, Matthews K, et al. 2017. Reducing V3 antigenicity and immunogenicity on soluble, native-like HIV-1 Env SOSIP trimers. J. Virol. 91:e00677-17
    • (2017) J. Virol. , vol.91 , pp. e00677-e00717
    • Ringe, R.P.1    Ozorowski, G.2    Rantalainen, K.3    Struwe, W.B.4    Matthews, K.5
  • 114
    • 84887307095 scopus 로고    scopus 로고
    • Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation
    • Ringe RP, Sanders RW, Yasmeen A, Kim HJ, Lee JH, et al. 2013. Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation. PNAS 110:18256-61
    • (2013) PNAS , vol.110 , pp. 18256-18261
    • Ringe, R.P.1    Sanders, R.W.2    Yasmeen, A.3    Kim, H.J.4    Lee, J.H.5
  • 115
    • 84949656593 scopus 로고    scopus 로고
    • Influences on the design and purification of soluble, recombinant native-likeHIV-1 envelope glycoprotein trimers
    • Ringe RP, Yasmeen A, Ozorowski G, Go EP, Pritchard LK, et al. 2015. Influences on the design and purification of soluble, recombinant native-likeHIV-1 envelope glycoprotein trimers. J. Virol. 89:12189-210
    • (2015) J. Virol. , vol.89 , pp. 12189-12210
    • Ringe, R.P.1    Yasmeen, A.2    Ozorowski, G.3    Go, E.P.4    Pritchard, L.K.5
  • 116
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and the 3D structure of proteins
    • Rudd PM, Dwek RA. 1997. Glycosylation: heterogeneity and the 3D structure of proteins. Crit. Rev. Biochem. Mol. Biol. 32:1-100
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 117
    • 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 J-P, Yasmeen A, 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
  • 118
    • 85010843359 scopus 로고    scopus 로고
    • Native-like Env trimers as a platform forHIV-1 vaccine design
    • Sanders RW, Moore JP. 2017. Native-like Env trimers as a platform forHIV-1 vaccine design. Immunol. Rev. 275:161-82
    • (2017) Immunol. Rev. , vol.275 , pp. 161-182
    • Sanders, R.W.1    Moore, J.P.2
  • 119
    • 0036333661 scopus 로고    scopus 로고
    • Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1
    • Sanders RW, Vesanen M, Schuelke N, Master A, Schiffner L, et al. 2002. Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1. J. Virol. 76:8875-89
    • (2002) J. Virol. , vol.76 , pp. 8875-8889
    • Sanders, R.W.1    Vesanen, M.2    Schuelke, N.3    Master, A.4    Schiffner, L.5
  • 121
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of α1→2 mannose residues on the outer face of gp120
    • Scanlan CN, Pantophlet R, Wormald MR, Ollmann Saphire E, Stanfield R, et al. 2002. The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of α1→2 mannose residues on the outer face of gp120. J. Virol. 76:7306-21
    • (2002) J. Virol. , vol.76 , pp. 7306-7321
    • Scanlan, C.N.1    Pantophlet, R.2    Wormald, M.R.3    Ollmann, S.E.4    Stanfield, R.5
  • 122
    • 84899909771 scopus 로고    scopus 로고
    • Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike
    • Scharf L, Scheid JF, Lee JH, West AP, Chen C, et al. 2014. Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike. Cell Rep. 7:785-95
    • (2014) Cell Rep. , vol.7 , pp. 785-795
    • Scharf, L.1    Scheid, J.F.2    Lee, J.H.3    West, A.P.4    Chen, C.5
  • 123
    • 63849131879 scopus 로고    scopus 로고
    • Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals
    • Scheid JF, MouquetH, FeldhahnN, SeamanMS, Velinzon K, et al. 2009. Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals. Nature 458:636-40
    • (2009) Nature , vol.458 , pp. 636-640
    • Scheid, J.F.1    Mouquet, H.2    Feldhahn, N.3    Seaman, M.S.4    Velinzon, K.5
  • 125
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres SH. 2012. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180:519-30
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 126
    • 84973518493 scopus 로고    scopus 로고
    • Processing of structurally heterogeneous cryo-EM data inRELION
    • Scheres SH. 2016. Processing of structurally heterogeneous cryo-EM data inRELION. Methods Enzymol. 579:125-57
    • (2016) Methods Enzymol. , vol.579 , pp. 125-157
    • Scheres, S.H.1
  • 127
    • 84928583366 scopus 로고    scopus 로고
    • Cleavage-independentHIV-1 Env trimers engineered as soluble native spike mimetics for vaccine design
    • Sharma SK, de Val N, Bale S, Guenaga J, Tran K, et al. 2015. Cleavage-independentHIV-1 Env trimers engineered as soluble native spike mimetics for vaccine design. Cell Rep. 11:539-50
    • (2015) Cell Rep. , vol.11 , pp. 539-550
    • Sharma, S.K.1    De Val, N.2    Bale, S.3    Guenaga, J.4    Tran, K.5
  • 128
    • 0032907674 scopus 로고    scopus 로고
    • Neutralizing antibody directed against the HIV-1 envelope glycoprotein can completely block HIV-1/SIV chimeric virus infections of macaque monkeys
    • Shibata R, Igarashi T, Haigwood N, Buckler-White A, Ogert R, et al. 1999. Neutralizing antibody directed against the HIV-1 envelope glycoprotein can completely block HIV-1/SIV chimeric virus infections of macaque monkeys. Nat. Med. 5:204-10
    • (1999) Nat. Med. , vol.5 , pp. 204-210
    • Shibata, R.1    Igarashi, T.2    Haigwood, N.3    Buckler-White, A.4    Ogert, R.5
  • 129
    • 84901236516 scopus 로고    scopus 로고
    • Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV
    • SokD, Doores KJ, Briney B, LeKM, Saye-Francisco KL, et al. 2014. Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV. Sci. Transl. Med. 6:236ra63
    • (2014) Sci. Transl. Med. , vol.6 , pp. 236ra63
    • Sok, D.1    Doores, K.J.2    Briney, B.3    Le, K.M.4    Saye-Francisco, K.L.5
  • 130
    • 84990856306 scopus 로고    scopus 로고
    • A prominent site of antibody vulnerability on HIV envelope incorporates a motif associated with CCR5 binding and its camouflaging glycans
    • Sok D, Pauthner M, Briney B, Lee JH, Saye-Francisco KL, et al. 2016. A prominent site of antibody vulnerability on HIV envelope incorporates a motif associated with CCR5 binding and its camouflaging glycans. Immunity 45:31-45
    • (2016) Immunity , vol.45 , pp. 31-45
    • Sok, D.1    Pauthner, M.2    Briney, B.3    Lee, J.H.4    Saye-Francisco, K.L.5
  • 131
    • 84990876450 scopus 로고    scopus 로고
    • HIV vaccine design to target germline precursors of glycan-dependent broadly neutralizing antibodies
    • Steichen JM, KulpDW, Tokatlian T, Escolano A, Dosenovic P, et al. 2016. HIV vaccine design to target germline precursors of glycan-dependent broadly neutralizing antibodies. Immunity 45:483-96
    • (2016) Immunity , vol.45 , pp. 483-496
    • Steichen, J.M.1    Kulp, D.W.2    Tokatlian, T.3    Escolano, A.4    Dosenovic, P.5
  • 134
    • 84963936310 scopus 로고    scopus 로고
    • Trimeric HIV-1-Env structures define glycan shields from Clades A, B, and G
    • Stewart-JonesGB, Soto C, LemminT, Chuang GY, Druz A, et al. 2016. Trimeric HIV-1-Env structures define glycan shields from Clades A, B, and G. Cell 165:813-26
    • (2016) Cell , vol.165 , pp. 813-826
    • Stewart-Jones, G.B.1    Soto, C.2    Lemmin, T.3    Chuang, G.Y.4    Druz, A.5
  • 135
    • 84995528377 scopus 로고    scopus 로고
    • An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability
    • van Gils MJ, van den Kerkhof TL, Ozorowski G, Cottrell CA, Sok D, et al. 2016. An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability. Nat Microbiol 2:16199
    • (2016) Nat Microbiol , vol.2 , pp. 16199
    • Van Gils, M.J.1    Van Den Kerkhof, T.L.2    Ozorowski, G.3    Cottrell, C.A.4    Sok, D.5
  • 136
    • 84887235046 scopus 로고    scopus 로고
    • Maximizing the potential of electron cryomicroscopy data collected using direct detectors
    • Veesler D, Campbell MG, Cheng A, Fu CY, Murez Z, et al. 2013. Maximizing the potential of electron cryomicroscopy data collected using direct detectors. J. Struct. Biol. 184:193-202
    • (2013) J. Struct. Biol. , vol.184 , pp. 193-202
    • Veesler, D.1    Campbell, M.G.2    Cheng, A.3    Fu, C.Y.4    Murez, Z.5
  • 137
    • 84988039141 scopus 로고    scopus 로고
    • Single particle electron cryomicroscopy: Trends, issues and future perspective
    • Vinothkumar KR, Henderson R. 2016. Single particle electron cryomicroscopy: trends, issues and future perspective. Q. Rev. Biophys. 49:e13
    • (2016) Q. Rev. Biophys. , vol.49 , pp. e13
    • Vinothkumar, K.R.1    Henderson, R.2
  • 138
    • 77953543379 scopus 로고    scopus 로고
    • Rational antibody-based HIV-1 vaccine design: Current approaches and future directions
    • Walker LM, Burton DR. 2010. Rational antibody-based HIV-1 vaccine design: current approaches and future directions. Curr. Opin. Immunol. 22:358-66
    • (2010) Curr. Opin. Immunol. , vol.22 , pp. 358-366
    • Walker, L.M.1    Burton, D.R.2
  • 139
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker LM, Huber M, Doores KJ, Falkowska E, Pejchal R, et al. 2011. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 477:466-70
    • (2011) Nature , vol.477 , pp. 466-470
    • Walker, L.M.1    Huber, M.2    Doores, K.J.3    Falkowska, E.4    Pejchal, R.5
  • 140
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, Phogat SK, Chan-Hui PY, Wagner D, Phung P, et al. 2009. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326:285-89
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1    Phogat, S.K.2    Chan-Hui, P.Y.3    Wagner, D.4    Phung, P.5
  • 141
    • 84874181173 scopus 로고    scopus 로고
    • Integrative structural biology
    • Ward AB, Sali A, Wilson IA. 2013. Integrative structural biology. Science 339:913-15
    • (2013) Science , vol.339 , pp. 913-915
    • Ward, A.B.1    Sali, A.2    Wilson, I.A.3
  • 142
    • 85010843666 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoprotein structure: Nailing down a moving target
    • Ward AB, Wilson IA. 2017. The HIV-1 envelope glycoprotein structure: nailing down a moving target. Immunol. Rev. 275:21-32
    • (2017) Immunol. Rev. , vol.275 , pp. 21-32
    • Ward, A.B.1    Wilson, I.A.2
  • 143
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei X, Decker JM, Wang S, Hui H, Kappes JC, et al. 2003. Antibody neutralization and escape by HIV-1. Nature 422:307-12
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.1    Decker, J.M.2    Wang, S.3    Hui, H.4    Kappes, J.C.5
  • 144
    • 84995377829 scopus 로고    scopus 로고
    • Structure of anN276-dependent HIV-1 neutralizing antibody targeting a rare V5 glycan hole adjacent to the CD4 binding site
    • Wibmer CK, Gorman J, AnthonyCS, Mkhize NN, Druz A, et al. 2016. Structure of anN276-dependent HIV-1 neutralizing antibody targeting a rare V5 glycan hole adjacent to the CD4 binding site. J. Virol. 90:10220-35
    • (2016) J. Virol. , vol.90 , pp. 10220-10235
    • Wibmer, C.K.1    Gorman, J.2    Anthony, C.S.3    Mkhize, N.N.4    Druz, A.5
  • 145
    • 0029815226 scopus 로고    scopus 로고
    • Differential glycosylation, virion incorporation, and sensitivity to neutralizing antibodies of human immunodeficiency virus type 1 envelope produced from infected primary T-lymphocyte and macrophage cultures
    • Willey RL, Shibata R, Freed EO, Cho MW, Martin MA. 1996. Differential glycosylation, virion incorporation, and sensitivity to neutralizing antibodies of human immunodeficiency virus type 1 envelope produced from infected primary T-lymphocyte and macrophage cultures. J. Virol. 70:6431-36
    • (1996) J. Virol. , vol.70 , pp. 6431-6436
    • Willey, R.L.1    Shibata, R.2    Freed, E.O.3    Cho, M.W.4    Martin, M.A.5
  • 146
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3Å resolution
    • Wilson IA, Skehel JJ, Wiley DC. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3Å resolution. Nature 289:366-73
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 147
    • 0032543555 scopus 로고    scopus 로고
    • The antigenic structure of the HIV gp120 envelope glycoprotein
    • Wyatt R, Kwong PD, Desjardins E, Sweet RW, Robinson J, et al. 1998. The antigenic structure of the HIV gp120 envelope glycoprotein. Nature 393:705-11
    • (1998) Nature , vol.393 , pp. 705-711
    • Wyatt, R.1    Kwong, P.D.2    Desjardins, E.3    Sweet, R.W.4    Robinson, J.5
  • 148
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • Wyatt R, Sodroski J. 1998. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 280:1884-88
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 149
    • 84903173697 scopus 로고    scopus 로고
    • Differential binding of neutralizing and non-neutralizing antibodies to native-like soluble HIV-1 Env trimers, uncleaved Env proteins, and monomeric subunits
    • Yasmeen A, Ringe R, Derking R, Cupo A, Julien J-P, et al. 2014. Differential binding of neutralizing and non-neutralizing antibodies to native-like soluble HIV-1 Env trimers, uncleaved Env proteins, and monomeric subunits. Retrovirology 11:41
    • (2014) Retrovirology , vol.11 , pp. 41
    • Yasmeen, A.1    Ringe, R.2    Derking, R.3    Cupo, A.4    Julien, J.-P.5
  • 150
    • 85018708194 scopus 로고    scopus 로고
    • Quantification of the impact of the HIV-1-glycan shield on antibody elicitation
    • Zhou T, Doria-Rose NA, Cheng C, Stewart-Jones GBE, Chuang GY, et al. 2017. Quantification of the impact of the HIV-1-glycan shield on antibody elicitation. Cell Rep. 19:719-32
    • (2017) Cell Rep. , vol.19 , pp. 719-732
    • Zhou, T.1    Doria-Rose, N.A.2    Cheng, C.3    Stewart-Jones, G.B.E.4    Chuang, G.Y.5
  • 151
    • 84882589754 scopus 로고    scopus 로고
    • Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies
    • Zhou T, Zhu J, Wu X, Moquin S, Zhang B, et al. 2013. Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies. Immunity 39:245-58
    • (2013) Immunity , vol.39 , pp. 245-258
    • Zhou, T.1    Zhu, J.2    Wu, X.3    Moquin, S.4    Zhang, B.5
  • 152
    • 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 39:11194-204
    • (2000) Biochemistry , vol.39 , 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.