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Volumn 40, Issue 2, 2015, Pages 101-107

Insights into the trimeric HIV-1 envelope glycoprotein structure

Author keywords

Broadly neutralizing antibodies; Envelope glycoprotein trimer; HIV 1; Structure

Indexed keywords

EPITOPE; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; NEUTRALIZING ANTIBODY; VIRUS FUSION PROTEIN;

EID: 84921606536     PISSN: 09680004     EISSN: 13624326     Source Type: Journal    
DOI: 10.1016/j.tibs.2014.12.006     Document Type: Review
Times cited : (89)

References (60)
  • 1
    • 0032543555 scopus 로고    scopus 로고
    • The antigenic structure of the HIV gp120 envelope glycoprotein
    • Wyatt R., et al. The antigenic structure of the HIV gp120 envelope glycoprotein. Nature 1998, 393:705-711.
    • (1998) Nature , vol.393 , pp. 705-711
    • Wyatt, R.1
  • 2
    • 27744597054 scopus 로고    scopus 로고
    • Structure of a V3-containing HIV-1 gp120 core
    • Huang C.C., et al. Structure of a V3-containing HIV-1 gp120 core. Science 2005, 310:1025-1028.
    • (2005) Science , vol.310 , pp. 1025-1028
    • Huang, C.C.1
  • 3
    • 75749133275 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility
    • Pancera M., et al. Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:1166-1171.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1166-1171
    • Pancera, M.1
  • 4
    • 33847101745 scopus 로고    scopus 로고
    • Structural definition of a conserved neutralization epitope on HIV-1 gp120
    • Zhou T., et al. Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature 2007, 445:732-737.
    • (2007) Nature , vol.445 , pp. 732-737
    • Zhou, T.1
  • 5
    • 82755184131 scopus 로고    scopus 로고
    • Increasing the potency and breadth of an HIV antibody by using structure-based rational design
    • Diskin R., et al. Increasing the potency and breadth of an HIV antibody by using structure-based rational design. Science 2011, 334:1289-1293.
    • (2011) Science , vol.334 , pp. 1289-1293
    • Diskin, R.1
  • 6
    • 84907527916 scopus 로고    scopus 로고
    • Structural evolution of glycan recognition by a family of potent HIV antibodies
    • Garces F., et al. Structural evolution of glycan recognition by a family of potent HIV antibodies. Cell 2014, 159:69-79.
    • (2014) Cell , vol.159 , pp. 69-79
    • Garces, F.1
  • 7
    • 84877618448 scopus 로고    scopus 로고
    • Delineating antibody recognition in polyclonal sera from patterns of HIV-1 isolate neutralization
    • Georgiev I.S., et al. Delineating antibody recognition in polyclonal sera from patterns of HIV-1 isolate neutralization. Science 2013, 340:751-756.
    • (2013) Science , vol.340 , pp. 751-756
    • Georgiev, I.S.1
  • 8
    • 84875759341 scopus 로고    scopus 로고
    • Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization
    • Klein F., et al. Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization. Cell 2013, 153:126-138.
    • (2013) Cell , vol.153 , pp. 126-138
    • Klein, F.1
  • 9
    • 84880161438 scopus 로고    scopus 로고
    • Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120
    • Kong L., et al. Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120. Nat. Struct. Mol. Biol. 2013, 20:796-803.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 796-803
    • Kong, L.1
  • 10
    • 84876797103 scopus 로고    scopus 로고
    • Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus
    • Liao H.X., et al. Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. Nature 2013, 496:469-476.
    • (2013) Nature , vol.496 , pp. 469-476
    • Liao, H.X.1
  • 11
    • 82255179322 scopus 로고    scopus 로고
    • A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield
    • Pejchal R., et al. A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield. Science 2011, 334:1097-1103.
    • (2011) Science , vol.334 , pp. 1097-1103
    • Pejchal, R.1
  • 12
    • 84899909771 scopus 로고    scopus 로고
    • Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike
    • Scharf L., et al. Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike. Cell Rep. 2014, 7:785-795.
    • (2014) Cell Rep. , vol.7 , pp. 785-795
    • Scharf, L.1
  • 13
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • Wu X., et al. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 2011, 333:1593-1602.
    • (2011) Science , vol.333 , pp. 1593-1602
    • Wu, X.1
  • 14
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T., et al. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 2010, 329:811-817.
    • (2010) Science , vol.329 , pp. 811-817
    • Zhou, T.1
  • 15
    • 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., et al. Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies. Immunity 2013, 39:245-258.
    • (2013) Immunity , vol.39 , pp. 245-258
    • Zhou, T.1
  • 16
    • 84859561617 scopus 로고    scopus 로고
    • Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops
    • Kwon Y.D., et al. Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:5663-5668.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 5663-5668
    • Kwon, Y.D.1
  • 17
    • 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., et al. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998, 393:648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1
  • 18
    • 77953543379 scopus 로고    scopus 로고
    • Rational antibody-based HIV-1 vaccine design: current approaches and future directions
    • Walker L.M., Burton D.R. Rational antibody-based HIV-1 vaccine design: current approaches and future directions. Curr. Opin. Immunol. 2010, 22:358-366.
    • (2010) Curr. Opin. Immunol. , vol.22 , pp. 358-366
    • Walker, L.M.1    Burton, D.R.2
  • 19
    • 84890858459 scopus 로고    scopus 로고
    • Crystal structure of a soluble cleaved HIV-1 envelope trimer
    • Julien J.P., et al. Crystal structure of a soluble cleaved HIV-1 envelope trimer. Science 2013, 342:1477-1483.
    • (2013) Science , vol.342 , pp. 1477-1483
    • Julien, J.P.1
  • 20
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis D., et al. Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science 2013, 342:1484-1490.
    • (2013) Science , vol.342 , pp. 1484-1490
    • Lyumkis, D.1
  • 21
    • 84909640954 scopus 로고    scopus 로고
    • Structure and immune recognition of trimeric pre-fusion HIV-1 Env
    • Pancera M., et al. Structure and immune recognition of trimeric pre-fusion HIV-1 Env. Nature 2014, 514:455-461.
    • (2014) Nature , vol.514 , pp. 455-461
    • Pancera, M.1
  • 22
    • 33748038359 scopus 로고    scopus 로고
    • Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ
    • Zanetti G., et al. Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ. PLoS Pathog. 2006, 2:e83.
    • (2006) PLoS Pathog. , vol.2 , pp. e83
    • Zanetti, G.1
  • 23
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • Zhu P., et al. Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 2006, 441:847-852.
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1
  • 24
    • 57149107577 scopus 로고    scopus 로고
    • Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs
    • Zhu P., et al. Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs. PLoS Pathog. 2008, 4:e1000203.
    • (2008) PLoS Pathog. , vol.4 , pp. e1000203
    • Zhu, P.1
  • 25
    • 79960974710 scopus 로고    scopus 로고
    • Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures
    • Harris A., et al. Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:11440-11445.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 11440-11445
    • Harris, A.1
  • 26
    • 51349162563 scopus 로고    scopus 로고
    • Molecular architecture of native HIV-1 gp120 trimers
    • Liu J., et al. Molecular architecture of native HIV-1 gp120 trimers. Nature 2008, 455:109-113.
    • (2008) Nature , vol.455 , pp. 109-113
    • Liu, J.1
  • 27
    • 22544471847 scopus 로고    scopus 로고
    • Soluble mimetics of human immunodeficiency virus type 1 viral spikes produced by replacement of the native trimerization domain with a heterologous trimerization motif: characterization and ligand binding analysis
    • Pancera M., et al. Soluble mimetics of human immunodeficiency virus type 1 viral spikes produced by replacement of the native trimerization domain with a heterologous trimerization motif: characterization and ligand binding analysis. J. Virol. 2005, 79:9954-9969.
    • (2005) J. Virol. , vol.79 , pp. 9954-9969
    • Pancera, M.1
  • 28
    • 0036231093 scopus 로고    scopus 로고
    • Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin
    • Yang X., et al. Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin. J. Virol. 2002, 76:4634-4642.
    • (2002) J. Virol. , vol.76 , pp. 4634-4642
    • Yang, X.1
  • 29
    • 84887307095 scopus 로고    scopus 로고
    • Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation
    • Ringe R.P., et al. Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:18256-18261.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 18256-18261
    • Ringe, R.P.1
  • 30
    • 84894355475 scopus 로고    scopus 로고
    • Vaccine-elicited primate antibodies use a distinct approach to the HIV-1 primary receptor binding site informing vaccine redesign
    • Tran K., et al. Vaccine-elicited primate antibodies use a distinct approach to the HIV-1 primary receptor binding site informing vaccine redesign. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:E738-E747.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. E738-E747
    • Tran, K.1
  • 31
    • 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 J.M., et al. 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. 2000, 74:627-643.
    • (2000) J. Virol. , vol.74 , pp. 627-643
    • Binley, J.M.1
  • 32
    • 0036333661 scopus 로고    scopus 로고
    • Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1
    • Sanders R.W., et al. Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1. J. Virol. 2002, 76:8875-8889.
    • (2002) J. Virol. , vol.76 , pp. 8875-8889
    • Sanders, R.W.1
  • 33
    • 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 R.W., et al. 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. 2013, 9:e1003618.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003618
    • Sanders, R.W.1
  • 34
    • 84883275866 scopus 로고    scopus 로고
    • Structural characterization of cleaved, soluble HIV-1 envelope glycoprotein trimers
    • Khayat R., et al. Structural characterization of cleaved, soluble HIV-1 envelope glycoprotein trimers. J. Virol. 2013, 87:9865-9872.
    • (2013) J. Virol. , vol.87 , pp. 9865-9872
    • Khayat, R.1
  • 35
    • 84883308389 scopus 로고    scopus 로고
    • Influences on trimerization and aggregation of soluble, cleaved HIV-1 SOSIP envelope glycoprotein
    • Klasse P.J., et al. Influences on trimerization and aggregation of soluble, cleaved HIV-1 SOSIP envelope glycoprotein. J. Virol. 2013, 87:9873-9885.
    • (2013) J. Virol. , vol.87 , pp. 9873-9885
    • Klasse, P.J.1
  • 36
    • 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., et al. Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. Immunity 2014, 40:669-680.
    • (2014) Immunity , vol.40 , pp. 669-680
    • Blattner, C.1
  • 37
    • 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., et al. Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers. Immunity 2014, 40:657-668.
    • (2014) Immunity , vol.40 , pp. 657-668
    • Falkowska, E.1
  • 38
    • 84890196626 scopus 로고    scopus 로고
    • Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy
    • Bartesaghi A., et al. Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy. Nat. Struct. Mol. Biol. 2013, 20:1352-1357.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1352-1357
    • Bartesaghi, A.1
  • 39
    • 0030962291 scopus 로고    scopus 로고
    • Atomic structure of the ectodomain from HIV-1 gp41
    • Weissenhorn W., et al. Atomic structure of the ectodomain from HIV-1 gp41. Nature 1997, 387:426-430.
    • (1997) Nature , vol.387 , pp. 426-430
    • Weissenhorn, W.1
  • 40
    • 84877609579 scopus 로고    scopus 로고
    • Rational HIV immunogen design to target specific germline B cell receptors
    • Jardine J., et al. Rational HIV immunogen design to target specific germline B cell receptors. Science 2013, 340:711-716.
    • (2013) Science , vol.340 , pp. 711-716
    • Jardine, J.1
  • 41
    • 84878626061 scopus 로고    scopus 로고
    • Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies
    • McGuire A.T., et al. Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies. J. Exp. Med. 2013, 210:655-663.
    • (2013) J. Exp. Med. , vol.210 , pp. 655-663
    • McGuire, A.T.1
  • 42
    • 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., et al. N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies. J. Virol. 2004, 78:3279-3295.
    • (2004) J. Virol. , vol.78 , pp. 3279-3295
    • McCaffrey, R.A.1
  • 43
    • 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 C.D., et al. Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy. J. Virol. 2014, 88:10177-10188.
    • (2014) J. Virol. , vol.88 , pp. 10177-10188
    • Murin, C.D.1
  • 44
    • 84901236516 scopus 로고    scopus 로고
    • Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV
    • Sok D., et al. Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV. Sci. Transl. Med. 2014, 6:236ra263.
    • (2014) Sci. Transl. Med. , vol.6 , pp. 236ra263
    • Sok, D.1
  • 45
    • 80051677678 scopus 로고    scopus 로고
    • The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade
    • Bonomelli C., et al. The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade. PLoS One 2011, 6:e23521.
    • (2011) PLoS One , vol.6 , pp. e23521
    • Bonomelli, C.1
  • 46
    • 84875034460 scopus 로고    scopus 로고
    • Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9
    • Julien J.P., et al. Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:4351-4356.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 4351-4356
    • Julien, J.P.1
  • 47
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • McLellan J.S., et al. Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 2011, 480:336-343.
    • (2011) Nature , vol.480 , pp. 336-343
    • McLellan, J.S.1
  • 48
    • 84880149399 scopus 로고    scopus 로고
    • Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16
    • Pancera M., et al. Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16. Nat. Struct. Mol. Biol. 2013, 20:804-813.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 804-813
    • Pancera, M.1
  • 49
    • 84899991983 scopus 로고    scopus 로고
    • Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies
    • Doria-Rose N.A., et al. Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies. Nature 2014, 509:55-62.
    • (2014) Nature , vol.509 , pp. 55-62
    • Doria-Rose, N.A.1
  • 50
    • 84887270287 scopus 로고    scopus 로고
    • Viral escape from HIV-1 neutralizing antibodies drives increased plasma neutralization breadth through sequential recognition of multiple epitopes and immunotypes
    • Wibmer C.K., et al. Viral escape from HIV-1 neutralizing antibodies drives increased plasma neutralization breadth through sequential recognition of multiple epitopes and immunotypes. PLoS Pathog. 2013, 9:e1003738.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003738
    • Wibmer, C.K.1
  • 51
    • 84868226722 scopus 로고    scopus 로고
    • MALDI-MS/MS with traveling wave ion mobility for the structural analysis of N-linked glycans
    • Harvey D.J., et al. MALDI-MS/MS with traveling wave ion mobility for the structural analysis of N-linked glycans. J. Am. Soc. Mass Spectrom. 2012, 23:1955-1966.
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 1955-1966
    • Harvey, D.J.1
  • 52
    • 84881610706 scopus 로고    scopus 로고
    • Travelling wave ion mobility and negative ion fragmentation for the structural determination of N-linked glycans
    • Harvey D.J., et al. Travelling wave ion mobility and negative ion fragmentation for the structural determination of N-linked glycans. Electrophoresis 2013, 34:2368-2378.
    • (2013) Electrophoresis , vol.34 , pp. 2368-2378
    • Harvey, D.J.1
  • 53
    • 79955753022 scopus 로고    scopus 로고
    • Ion mobility mass spectrometry for extracting spectra of N-glycans directly from incubation mixtures following glycan release: application to glycans from engineered glycoforms of intact, folded HIV gp120
    • Harvey D.J., et al. Ion mobility mass spectrometry for extracting spectra of N-glycans directly from incubation mixtures following glycan release: application to glycans from engineered glycoforms of intact, folded HIV gp120. J. Am. Soc. Mass Spectrom. 2011, 22:568-581.
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 568-581
    • Harvey, D.J.1
  • 54
    • 69249202492 scopus 로고    scopus 로고
    • Transitions to and from the CD4-bound conformation are modulated by a single-residue change in the human immunodeficiency virus type 1 gp120 inner domain
    • Kassa A., et al. Transitions to and from the CD4-bound conformation are modulated by a single-residue change in the human immunodeficiency virus type 1 gp120 inner domain. J. Virol. 2009, 83:8364-8378.
    • (2009) J. Virol. , vol.83 , pp. 8364-8378
    • Kassa, A.1
  • 55
    • 84864603281 scopus 로고    scopus 로고
    • Structural mechanism of trimeric HIV-1 envelope glycoprotein activation
    • Tran E.E., et al. Structural mechanism of trimeric HIV-1 envelope glycoprotein activation. PLoS Pathog. 2012, 8:e1002797.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002797
    • Tran, E.E.1
  • 56
    • 84869077778 scopus 로고    scopus 로고
    • HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully cleaved envelope glycoproteins
    • Li Y., et al. HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully cleaved envelope glycoproteins. J. Virol. 2012, 86:11231-11241.
    • (2012) J. Virol. , vol.86 , pp. 11231-11241
    • Li, Y.1
  • 57
    • 84921607768 scopus 로고    scopus 로고
    • Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface
    • Huang J., et al. Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface. Nature 2014, 515:138-142.
    • (2014) Nature , vol.515 , pp. 138-142
    • Huang, J.1
  • 58
    • 84886011849 scopus 로고    scopus 로고
    • Isolate-specific differences in the conformational dynamics and antigenicity of HIV-1 gp120
    • Davenport T.M., et al. Isolate-specific differences in the conformational dynamics and antigenicity of HIV-1 gp120. J. Virol. 2013, 87:10855-10873.
    • (2013) J. Virol. , vol.87 , pp. 10855-10873
    • Davenport, T.M.1
  • 59
    • 84904127504 scopus 로고    scopus 로고
    • CD4-induced activation in a soluble HIV-1 Env trimer
    • Guttman M., et al. CD4-induced activation in a soluble HIV-1 Env trimer. Structure 2014, 22:974-984.
    • (2014) Structure , vol.22 , pp. 974-984
    • Guttman, M.1
  • 60
    • 84909606387 scopus 로고    scopus 로고
    • Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
    • Munro J.B., et al. Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions. Science 2014, 34:759-763.
    • (2014) Science , vol.34 , pp. 759-763
    • Munro, J.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.