메뉴 건너뛰기




Volumn 11, Issue 3, 2015, Pages 1-22

Comprehensive Antigenic Map of a Cleaved Soluble HIV-1 Envelope Trimer

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; EPITOPE; GLYCAN; GLYCOPROTEIN GP 120; NEUTRALIZING ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS ANTIGEN; VIRUS ENVELOPE PROTEIN;

EID: 84926453015     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004767     Document Type: Article
Times cited : (91)

References (52)
  • 1
    • 84870701546 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies against HIV-1: templates for a vaccine
    • Van Gils MJ, Sanders RW, (2013) Broadly neutralizing antibodies against HIV-1: templates for a vaccine. Virology 435: 46–56. doi: 10.1016/j.virol.2012.10.004 23217615
    • (2013) Virology , vol.435 , pp. 46-56
    • Van Gils, M.J.1    Sanders, R.W.2
  • 2
    • 84887626950 scopus 로고    scopus 로고
    • Therapeutic efficacy of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys
    • Barouch DH, Whitney JB, Moldt B, Klein F, Oliveira TY, et al. (2013) Therapeutic efficacy of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys. Nature 503: 224–228. doi: 10.1038/nature12744 24172905
    • (2013) Nature , vol.503 , pp. 224-228
    • Barouch, D.H.1    Whitney, J.B.2    Moldt, B.3    Klein, F.4    Oliveira, T.Y.5
  • 3
    • 84927566324 scopus 로고    scopus 로고
    • Early development of broadly reactive HIV-1 neutralizing activity in elite neutralizers
    • Van den Kerkhof TLGM, Euler Z, van Gils MJ, Boeser-Nunnink BD, Schuitemaker H, et al. (2014) Early development of broadly reactive HIV-1 neutralizing activity in elite neutralizers. AIDS 28: 1237–1240. doi: 10.1097/QAD.0000000000000228 24556870
    • (2014) AIDS , vol.28 , pp. 1237-1240
    • Van den Kerkhof, T.L.G.M.1    Euler, Z.2    van Gils, M.J.3    Boeser-Nunnink, B.D.4    Schuitemaker, H.5
  • 4
    • 84899991983 scopus 로고    scopus 로고
    • Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies
    • Doria-Rose N a, Schramm C a, Gorman J, Moore PL, Bhiman JN, et al. (2014) Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies. Nature 509: 55–62. doi: 10.1038/nature13036 24590074
    • (2014) Nature , vol.509 , pp. 55-62
    • Doria-Rose, N.1    Schramm, C.2    Gorman, J.3    Moore, P.L.4    Bhiman, J.N.5
  • 5
    • 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, Sliepen K, Derking R, Falkowska E, et al. (2014) Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. Immunity 40: 669–680. doi: 10.1016/j.immuni.2014.04.008 24768348
    • (2014) Immunity , vol.40 , pp. 669-680
    • Blattner, C.1    Lee, J.H.2    Sliepen, K.3    Derking, R.4    Falkowska, E.5
  • 6
    • 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: 657–668. doi: 10.1016/j.immuni.2014.04.009 24768347
    • (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
  • 7
    • 84879538530 scopus 로고    scopus 로고
    • Computational analysis of anti-HIV-1 antibody neutralization panel data to identify potential functional epitope residues
    • West AP, Scharf L, Horwitz J, Klein F, Nussenzweig MC, et al. (2013) Computational analysis of anti-HIV-1 antibody neutralization panel data to identify potential functional epitope residues. Proc Natl Acad Sci U S A 110: 10598–10603. doi: 10.1073/pnas.1309215110 23754383
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 10598-10603
    • West, A.P.1    Scharf, L.2    Horwitz, J.3    Klein, F.4    Nussenzweig, M.C.5
  • 8
    • 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: 138–142. doi: 10.1038/nature13601 25186731
    • (2014) Nature , vol.515 , pp. 138-142
    • Huang, J.1    Kang, B.H.2    Pancera, M.3    Lee, J.H.4    Tong, T.5
  • 9
    • 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. Proc Natl Acad Sci U S A 110: 18256–18261. doi: 10.1073/pnas.1314351110 24145402
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 18256-18261
    • Ringe, R.P.1    Sanders, R.W.2    Yasmeen, A.3    Kim, H.J.4    Lee, J.H.5
  • 10
    • 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: 1469–1479. doi: 10.1084/jem.20120423 22826297
    • (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
  • 11
    • 84926478160 scopus 로고    scopus 로고
    • Pre-fusion gp41 conformational epitope antibodies neutralize HIV-1 by inducing viral spike decay
    • Lee JH et al. (2014) Pre-fusion gp41 conformational epitope antibodies neutralize HIV-1 by inducing viral spike decay. Submitted.
    • (2014)
    • Lee, J.H.1
  • 12
    • 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. doi: 10.1371/journal.ppat.1003618 24068931
    • (2013) PLoS Pathog , vol.9
    • Sanders, R.W.1    Derking, R.2    Cupo, A.3    Julien, J.-P.4    Yasmeen, A.5
  • 13
    • 0030043169 scopus 로고    scopus 로고
    • Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein
    • Moore JP, Sodroski J, (1996) Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J Virol 70: 1863–1872. 8627711
    • (1996) J Virol , vol.70 , pp. 1863-1872
    • Moore, J.P.1    Sodroski, J.2
  • 14
    • 84875034460 scopus 로고    scopus 로고
    • Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9
    • Julien J, Lee JH, Cupo A, Murin CD, Derking R, et al. (2013) Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9. Proc Natl Acad Sci U S A 110: 4351–4356. doi: 10.1073/pnas.1217537110 23426631
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 4351-4356
    • Julien, J.1    Lee, J.H.2    Cupo, A.3    Murin, C.D.4    Derking, R.5
  • 15
    • 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: 627–643. 10623724
    • (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
  • 16
    • 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: 8875–8889. 12163607
    • (2002) J Virol , vol.76 , pp. 8875-8889
    • Sanders, R.W.1    Vesanen, M.2    Schuelke, N.3    Master, A.4    Schiffner, L.5
  • 17
    • 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. doi: 10.1371/journal.ppat.1003342 23658524
    • (2013) PLoS Pathog , vol.9
    • Julien, J.-P.1    Sok, D.2    Khayat, R.3    Lee, J.H.4    Doores, K.J.5
  • 18
    • 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: 1477–1483. doi: 10.1126/science.1245625 24179159
    • (2013) Science , vol.342 , pp. 1477-1483
    • Julien, J.-P.1    Cupo, A.2    Sok, D.3    Stanfield, R.L.4    Lyumkis, D.5
  • 19
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis D, Julien J-P, de Val N, Cupo A, Potter CS, et al. (2013) Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science 342: 1484–1490. doi: 10.1126/science.1245627 24179160
    • (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
  • 20
    • 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. doi: 10.1038/nsmb.2594 23708606
    • (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
  • 21
    • 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: 455–461. doi: 10.1038/nature13808 25296255
    • (2014) Nature , vol.514 , pp. 455-461
    • Pancera, M.1    Zhou, T.2    Druz, A.3    Georgiev, I.S.4    Soto, C.5
  • 22
    • 84921834241 scopus 로고    scopus 로고
    • HIV: A stamp on the envelope
    • Sanders RW, Moore JP, (2014) HIV: A stamp on the envelope. Nature 514: 437–438. doi: 10.1038/nature13926 25296251
    • (2014) Nature , vol.514 , pp. 437-438
    • Sanders, R.W.1    Moore, J.P.2
  • 23
    • 84883308389 scopus 로고    scopus 로고
    • Influences on trimerization and aggregation of soluble, cleaved HIV-1 SOSIP envelope glycoprotein
    • Klasse PJ, Depetris RS, Pejchal R, Julien J-P, Khayat R, et al. (2013) Influences on trimerization and aggregation of soluble, cleaved HIV-1 SOSIP envelope glycoprotein. J Virol 87: 9873–9885. doi: 10.1128/JVI.01226-13 23824824
    • (2013) J Virol , vol.87 , pp. 9873-9885
    • Klasse, P.J.1    Depetris, R.S.2    Pejchal, R.3    Julien, J.-P.4    Khayat, R.5
  • 24
    • 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: 9865–9872. doi: 10.1128/JVI.01222-13 23824817
    • (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
  • 25
    • 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: 1097–1103. doi: 10.1126/science.1213256 21998254
    • (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
  • 26
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid JF, Mouquet H, Ueberheide B, Diskin R, Klein F, et al. (2011) Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 333: 1633–1637. doi: 10.1126/science.1207227 21764753
    • (2011) Science , vol.333 , pp. 1633-1637
    • Scheid, J.F.1    Mouquet, H.2    Ueberheide, B.3    Diskin, R.4    Klein, F.5
  • 27
    • 84909606387 scopus 로고    scopus 로고
    • Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
    • Munro JB, Gorman J, Ma X, Zhou Z, Arthos J, et al. (2014) Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions. Science 346: 759–763. doi: 10.1126/science.1254426 25298114
    • (2014) Science , vol.346 , pp. 759-763
    • Munro, J.B.1    Gorman, J.2    Ma, X.3    Zhou, Z.4    Arthos, J.5
  • 28
    • 84923164032 scopus 로고    scopus 로고
    • Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env
    • Guttman M, Cupo A, Julien J-P, Sanders RW, Wilson I a, et al. (2015) Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env. Nat Commun 6: 6144. doi: 10.1038/ncomms7144 25652336
    • (2015) Nat Commun , vol.6 , pp. 6144
    • Guttman, M.1    Cupo, A.2    Julien, J.-P.3    Sanders, R.W.4    Wilson, I.5
  • 29
    • 84877350114 scopus 로고    scopus 로고
    • Identification of an HIV-1 clade A envelope that exhibits broad antigenicity and neutralization sensitivity and elicits antibodies targeting three distinct epitopes
    • Hoffenberg S, Powell R, Carpov A, Wagner D, Wilson A, et al. (2013) Identification of an HIV-1 clade A envelope that exhibits broad antigenicity and neutralization sensitivity and elicits antibodies targeting three distinct epitopes. J Virol 87: 5372–5383. doi: 10.1128/JVI.02827-12 23468492
    • (2013) J Virol , vol.87 , pp. 5372-5383
    • Hoffenberg, S.1    Powell, R.2    Carpov, A.3    Wagner, D.4    Wilson, A.5
  • 30
    • 81255213876 scopus 로고    scopus 로고
    • Three-dimensional structures of soluble CD4-bound states of trimeric simian immunodeficiency virus envelope glycoproteins determined by using cryo-electron tomography
    • White T a, Bartesaghi A, Borgnia MJ, de la Cruz MJ V, Nandwani R, et al. (2011) Three-dimensional structures of soluble CD4-bound states of trimeric simian immunodeficiency virus envelope glycoproteins determined by using cryo-electron tomography. J Virol 85: 12114–12123. doi: 10.1128/JVI.05297-11 21937655
    • (2011) J Virol , vol.85 , pp. 12114-12123
    • White, T.1    Bartesaghi, A.2    Borgnia, M.J.3    de la Cruz, M.J.V.4    Nandwani, R.5
  • 31
    • 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: 466–470. doi: 10.1038/nature10373 21849977
    • (2011) Nature , vol.477 , pp. 466-470
    • Walker, L.M.1    Huber, M.2    Doores, K.J.3    Falkowska, E.4    Pejchal, R.5
  • 32
    • 80052287270 scopus 로고    scopus 로고
    • Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01
    • Li Y, O’Dell S, Walker LM, Wu X, Guenaga J, et al. (2011) Mechanism of neutralization by the broadly neutralizing HIV-1 monoclonal antibody VRC01. J Virol 85: 8954–8967. doi: 10.1128/JVI.00754-11 21715490
    • (2011) J Virol , vol.85 , pp. 8954-8967
    • Li, Y.1    O’Dell, S.2    Walker, L.M.3    Wu, X.4    Guenaga, J.5
  • 33
    • 84864603281 scopus 로고    scopus 로고
    • Structural mechanism of trimeric HIV-1 envelope glycoprotein activation
    • Tran EEH, Borgnia MJ, Kuybeda O, Schauder DM, Bartesaghi A, et al. (2012) Structural mechanism of trimeric HIV-1 envelope glycoprotein activation. PLoS Pathog 8: e1002797. doi: 10.1371/journal.ppat.1002797 22807678
    • (2012) PLoS Pathog , vol.8
    • Tran, E.E.H.1    Borgnia, M.J.2    Kuybeda, O.3    Schauder, D.M.4    Bartesaghi, A.5
  • 34
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali M, Moore JP, Furman C, Charles M, Ho DD, et al. (1993) Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J Virol 67: 3978–3988. 7685405
    • (1993) J Virol , vol.67 , pp. 3978-3988
    • Thali, M.1    Moore, J.P.2    Furman, C.3    Charles, M.4    Ho, D.D.5
  • 35
    • 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. doi: 10.1186/1742-4690-11-41 24884783
    • (2014) Retrovirology , vol.11 , pp. 41
    • Yasmeen, A.1    Ringe, R.2    Derking, R.3    Cupo, A.4    Julien, J.-P.5
  • 36
    • 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: 785–795. doi: 10.1016/j.celrep.2014.04.001 24767986
    • (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
  • 37
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T, Georgiev I, Wu X, Yang Z-Y, Dai K, et al. (2010) Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 329: 811–817. doi: 10.1126/science.1192819 20616231
    • (2010) Science , vol.329 , pp. 811-817
    • Zhou, T.1    Georgiev, I.2    Wu, X.3    Yang, Z.-Y.4    Dai, K.5
  • 38
    • 84880431984 scopus 로고    scopus 로고
    • The N276 glycosylation site is required for HIV-1 neutralization by the CD4 binding site specific HJ16 monoclonal antibody
    • Balla-Jhagjhoorsingh SS, Corti D, Heyndrickx L, Willems E, Vereecken K, et al. (2013) The N276 glycosylation site is required for HIV-1 neutralization by the CD4 binding site specific HJ16 monoclonal antibody. PLoS One 8: e68863. doi: 10.1371/journal.pone.0068863 23874792
    • (2013) PLoS One , vol.8
    • Balla-Jhagjhoorsingh, S.S.1    Corti, D.2    Heyndrickx, L.3    Willems, E.4    Vereecken, K.5
  • 39
    • 84878626061 scopus 로고    scopus 로고
    • Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies
    • McGuire AT, Hoot S, Dreyer AM, Lippy A, Stuart A, et al. (2013) Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies. J Exp Med 210: 655–663. doi: 10.1084/jem.20122824 23530120
    • (2013) J Exp Med , vol.210 , pp. 655-663
    • McGuire, A.T.1    Hoot, S.2    Dreyer, A.M.3    Lippy, A.4    Stuart, A.5
  • 40
    • 0027985431 scopus 로고
    • Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody
    • Burton DR, Pyati J, Koduri R, Sharp SJ, Thornton GB, et al. (1994) Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 266: 1024–1027. 7973652
    • (1994) Science , vol.266 , pp. 1024-1027
    • Burton, D.R.1    Pyati, J.2    Koduri, R.3    Sharp, S.J.4    Thornton, G.B.5
  • 41
    • 0028865465 scopus 로고
    • Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG
    • Trkola A, Pomales AB, Yuan H, Korber B, Maddon PJ, et al. (1995) Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG. J Virol 69: 6609–6617. 7474069
    • (1995) J Virol , vol.69 , pp. 6609-6617
    • Trkola, A.1    Pomales, A.B.2    Yuan, H.3    Korber, B.4    Maddon, P.J.5
  • 42
    • 0027378573 scopus 로고
    • A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1
    • Muster T, Steindl F, Purtscher M, Trkola a, Klima a, et al. (1993) A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J Virol 67: 6642–6647. 7692082
    • (1993) J Virol , vol.67 , pp. 6642-6647
    • Muster, T.1    Steindl, F.2    Purtscher, M.3    Trkola, A.4    Klima, A.5
  • 43
    • 0034759882 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41
    • Zwick MB, Labrijn AF, Wang M, Spenlehauer C, Saphire EO, et al. (2001) Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J Virol 75: 10892–10905. 11602729
    • (2001) J Virol , vol.75 , pp. 10892-10905
    • Zwick, M.B.1    Labrijn, A.F.2    Wang, M.3    Spenlehauer, C.4    Saphire, E.O.5
  • 44
    • 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 CK, Bhiman JN, Gray ES, Tumba N, Abdool Karim SS, et al. (2013) Viral escape from HIV-1 neutralizing antibodies drives increased plasma neutralization breadth through sequential recognition of multiple epitopes and immunotypes. PLoS Pathog 9: e1003738. doi: 10.1371/journal.ppat.1003738 24204277
    • (2013) PLoS Pathog , vol.9
    • Wibmer, C.K.1    Bhiman, J.N.2    Gray, E.S.3    Tumba, N.4    Abdool Karim, S.S.5
  • 45
    • 84905369598 scopus 로고    scopus 로고
    • Cooperation of B cell lineages in induction of HIV-1-broadly neutralizing antibodies
    • Gao F, Bonsignori M, Liao H-X, Kumar A, Xia S-M, et al. (2014) Cooperation of B cell lineages in induction of HIV-1-broadly neutralizing antibodies. Cell 158: 481–491. doi: 10.1016/j.cell.2014.06.022 25065977
    • (2014) Cell , vol.158 , pp. 481-491
    • Gao, F.1    Bonsignori, M.2    Liao, H.-X.3    Kumar, A.4    Xia, S.-M.5
  • 46
    • 84926454763 scopus 로고    scopus 로고
    • Gp120/CD4 Blocking Antibodies are Frequently Elicited in ART-naïve Chronically HIV-1 Infected Individuals
    • Carrillo J. et al (n.d.) Gp120/CD4 Blocking Antibodies are Frequently Elicited in ART-naïve Chronically HIV-1 Infected Individuals. Submitted.
    • Carrillo, J.1
  • 47
    • 63649113687 scopus 로고    scopus 로고
    • DoG Picker and TiltPicker: software tools to facilitate particle selection in single particle electron microscopy
    • Voss NR, Yoshioka CK, Radermacher M, Potter CS, Carragher B, (2009) DoG Picker and TiltPicker: software tools to facilitate particle selection in single particle electron microscopy. J Struct Biol 166: 205–213. 19374019
    • (2009) J Struct Biol , vol.166 , pp. 205-213
    • Voss, N.R.1    Yoshioka, C.K.2    Radermacher, M.3    Potter, C.S.4    Carragher, B.5
  • 48
    • 0142059303 scopus 로고    scopus 로고
    • Topology representing network enables highly accurate classification of protein images taken by cryo electron-microscope without masking
    • Ogura T, Iwasaki K, Sato C, (2003) Topology representing network enables highly accurate classification of protein images taken by cryo electron-microscope without masking. J Struct Biol 143: 185–200. 14572474
    • (2003) J Struct Biol , vol.143 , pp. 185-200
    • Ogura, T.1    Iwasaki, K.2    Sato, C.3
  • 49
    • 60649103238 scopus 로고    scopus 로고
    • Appion: an integrated, database-driven pipeline to facilitate EM image processing
    • Lander GC, Stagg SM, Voss NR, Cheng A, Fellmann D, et al. (2009) Appion: an integrated, database-driven pipeline to facilitate EM image processing. J Struct Biol 166: 95–102. 19263523
    • (2009) J Struct Biol , vol.166 , pp. 95-102
    • Lander, G.C.1    Stagg, S.M.2    Voss, N.R.3    Cheng, A.4    Fellmann, D.5
  • 50
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: an extensible image processing suite for electron microscopy
    • Tang G, Peng L, Baldwin PR, Mann DS, Jiang W, et al. (2007) EMAN2: an extensible image processing suite for electron microscopy. J Struct Biol 157: 38–46. 16859925
    • (2007) J Struct Biol , vol.157 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5
  • 51
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W, (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128: 82–97. 10600563
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 52


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.