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Volumn 11, Issue 5, 2015, Pages

Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site

(26)  Crooks, Ema T a   Tong, Tommy a   Chakrabarti, Bimal b,g   Narayan, Kristin c,k   Georgiev, Ivelin S d   Menis, Sergey b   Huang, Xiaoxing e   Kulp, Daniel b   Osawa, Keiko a   Muranaka, Janelle c   Stewart Jones, Guillaume d,f   Destefano, Joanne g   O’Dell, Sijy d   LaBranche, Celia h   Robinson, James E i   Montefiori, David C h   McKee, Krisha d   Du, Sean X c   Doria Rose, Nicole d   Kwong, Peter D d   more..


Author keywords

[No Author keywords available]

Indexed keywords

8ANC195; CD4 ANTIGEN; CD4 IMMUNOGLOBULIN G2; EPITOPE; GLYCAN DERIVATIVE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; PG9; UNCLASSIFIED DRUG; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; POLYSACCHARIDE;

EID: 84930365226     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004932     Document Type: Article
Times cited : (129)

References (90)
  • 1
    • 84880184277 scopus 로고    scopus 로고
    • Development of prophylactic vaccines against HIV-1
    • Schiffner T, Sattentau QJ, Dorrell L, (2013) Development of prophylactic vaccines against HIV-1. Retrovirology 10: 72. doi: 10.1186/1742-4690-10-72 23866844
    • (2013) Retrovirology , vol.10 , pp. 72
    • Schiffner, T.1    Sattentau, Q.J.2    Dorrell, L.3
  • 2
    • 77952311370 scopus 로고    scopus 로고
    • The role of antibodies in HIV vaccines
    • Mascola JR, Montefiori DC, (2010) The role of antibodies in HIV vaccines. Annu Rev Immunol 28: 413–444. doi: 10.1146/annurev-immunol-030409-101256 20192810
    • (2010) Annu Rev Immunol , vol.28 , pp. 413-444
    • Mascola, J.R.1    Montefiori, D.C.2
  • 3
    • 45049083040 scopus 로고    scopus 로고
    • Relationship of HIV-1 and SIV envelope glycoprotein trimer occupation and neutralization
    • Crooks ET, Jiang P, Franti M, Wong S, Zwick MB, et al. (2008) Relationship of HIV-1 and SIV envelope glycoprotein trimer occupation and neutralization. Virology 377: 364–378. doi: 10.1016/j.virol.2008.04.045 18539308
    • (2008) Virology , vol.377 , pp. 364-378
    • Crooks, E.T.1    Jiang, P.2    Franti, M.3    Wong, S.4    Zwick, M.B.5
  • 4
    • 84866495323 scopus 로고    scopus 로고
    • Human Antibodies that Neutralize HIV-1: Identification, Structures, and B Cell Ontogenies
    • Kwong PD, Mascola JR, (2012) Human Antibodies that Neutralize HIV-1: Identification, Structures, and B Cell Ontogenies. Immunity 37: 412–425. doi: 10.1016/j.immuni.2012.08.012 22999947
    • (2012) Immunity , vol.37 , pp. 412-425
    • Kwong, P.D.1    Mascola, J.R.2
  • 5
    • 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
  • 6
    • 84874561170 scopus 로고    scopus 로고
    • Neutralizing antibodies to HIV-1 induced by immunization
    • McCoy LE, Weiss RA, (2013) Neutralizing antibodies to HIV-1 induced by immunization. J Exp Med 210: 209–223. doi: 10.1084/jem.20121827 23401570
    • (2013) J Exp Med , vol.210 , pp. 209-223
    • McCoy, L.E.1    Weiss, R.A.2
  • 7
    • 0037389643 scopus 로고    scopus 로고
    • Rapid evolution of the neutralizing antibody response to HIV type 1 infection
    • Richman DD, Wrin T, Little SJ, Petropoulos CJ, (2003) Rapid evolution of the neutralizing antibody response to HIV type 1 infection. Proc Natl Acad Sci U S A 100: 4144–4149. 12644702
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4144-4149
    • Richman, D.D.1    Wrin, T.2    Little, S.J.3    Petropoulos, C.J.4
  • 8
    • 84878528694 scopus 로고    scopus 로고
    • Comparison of viral Env proteins from acute and chronic infections with subtype C human immunodeficiency virus type 1 identifies differences in glycosylation and CCR5 utilization and suggests a new strategy for immunogen design
    • Ping LH, Joseph SB, Anderson JA, Abrahams MR, Salazar-Gonzalez JF, et al. (2013) Comparison of viral Env proteins from acute and chronic infections with subtype C human immunodeficiency virus type 1 identifies differences in glycosylation and CCR5 utilization and suggests a new strategy for immunogen design. J Virol 87: 7218–7233. doi: 10.1128/JVI.03577-12 23616655
    • (2013) J Virol , vol.87 , pp. 7218-7233
    • Ping, L.H.1    Joseph, S.B.2    Anderson, J.A.3    Abrahams, M.R.4    Salazar-Gonzalez, J.F.5
  • 9
    • 84898538468 scopus 로고    scopus 로고
    • Development of broadly neutralizing antibodies from autologous neutralizing antibody responses in HIV infection
    • Derdeyn CA, Moore PL, Morris L, (2014) Development of broadly neutralizing antibodies from autologous neutralizing antibody responses in HIV infection. Curr Opin HIV AIDS 9: 210–216. doi: 10.1097/COH.0000000000000057 24662931
    • (2014) Curr Opin HIV AIDS , vol.9 , pp. 210-216
    • Derdeyn, C.A.1    Moore, P.L.2    Morris, L.3
  • 10
    • 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 , pp. 1003738
    • Wibmer, C.K.1    Bhiman, J.N.2    Gray, E.S.3    Tumba, N.4    Abdool, K.S.S.5
  • 11
    • 84869155712 scopus 로고    scopus 로고
    • Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape
    • Moore PL, Gray ES, Wibmer CK, Bhiman JN, Nonyane M, et al. (2012) Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape. Nat Med 18: 1688–1692. doi: 10.1038/nm.2985 23086475
    • (2012) Nat Med , vol.18 , pp. 1688-1692
    • Moore, P.L.1    Gray, E.S.2    Wibmer, C.K.3    Bhiman, J.N.4    Nonyane, M.5
  • 12
    • 67650741139 scopus 로고    scopus 로고
    • Structural and immunogenicity studies of a cleaved, stabilized envelope trimer derived from subtype A HIV-1
    • Kang YK, Andjelic S, Binley JM, Crooks ET, Franti M, et al. (2009) Structural and immunogenicity studies of a cleaved, stabilized envelope trimer derived from subtype A HIV-1. Vaccine 27: 5120–5132. doi: 10.1016/j.vaccine.2009.06.037 19567243
    • (2009) Vaccine , vol.27 , pp. 5120-5132
    • Kang, Y.K.1    Andjelic, S.2    Binley, J.M.3    Crooks, E.T.4    Franti, M.5
  • 13
    • 84888046822 scopus 로고    scopus 로고
    • Robust Neutralizing Antibodies Elicited by HIV-1 JRFL Envelope Glycoprotein Trimers in Nonhuman Primates
    • Chakrabarti BK, Feng Y, Sharma SK, McKee K, Karlsson Hedestam GB, et al. (2013) Robust Neutralizing Antibodies Elicited by HIV-1 JRFL Envelope Glycoprotein Trimers in Nonhuman Primates. J Virol 87: 13239–13251. doi: 10.1128/JVI.01247-13 24067980
    • (2013) J Virol , vol.87 , pp. 13239-13251
    • Chakrabarti, B.K.1    Feng, Y.2    Sharma, S.K.3    McKee, K.4    Karlsson, H.G.B.5
  • 14
    • 56349094315 scopus 로고    scopus 로고
    • Systemic neutralizing antibodies induced by long interval mucosally primed systemically boosted immunization correlate with protection from mucosal SHIV challenge
    • Bogers WM, Davis D, Baak I, Kan E, Hofman S, et al. (2008) Systemic neutralizing antibodies induced by long interval mucosally primed systemically boosted immunization correlate with protection from mucosal SHIV challenge. Virology 382: 217–225. doi: 10.1016/j.virol.2008.09.016 18947849
    • (2008) Virology , vol.382 , pp. 217-225
    • Bogers, W.M.1    Davis, D.2    Baak, I.3    Kan, E.4    Hofman, S.5
  • 15
    • 38149096202 scopus 로고    scopus 로고
    • Protection of macaques against vaginal SHIV challenge by systemic or mucosal and systemic vaccinations with HIV-envelope
    • Barnett SW, Srivastava IK, Kan E, Zhou F, Goodsell A, et al. (2008) Protection of macaques against vaginal SHIV challenge by systemic or mucosal and systemic vaccinations with HIV-envelope. Aids 22: 339–348. doi: 10.1097/QAD.0b013e3282f3ca57 18195560
    • (2008) Aids , vol.22 , pp. 339-348
    • Barnett, S.W.1    Srivastava, I.K.2    Kan, E.3    Zhou, F.4    Goodsell, A.5
  • 16
    • 77952688015 scopus 로고    scopus 로고
    • Antibody-mediated protection against mucosal simian-human immunodeficiency virus challenge of macaques immunized with alphavirus replicon particles and boosted with trimeric envelope glycoprotein in MF59 adjuvant
    • Barnett SW, Burke B, Sun Y, Kan E, Legg H, et al. (2010) Antibody-mediated protection against mucosal simian-human immunodeficiency virus challenge of macaques immunized with alphavirus replicon particles and boosted with trimeric envelope glycoprotein in MF59 adjuvant. Journal of virology 84: 5975–5985. doi: 10.1128/JVI.02533-09 20392857
    • (2010) Journal of virology , vol.84 , pp. 5975-5985
    • Barnett, S.W.1    Burke, B.2    Sun, Y.3    Kan, E.4    Legg, H.5
  • 17
    • 76449108010 scopus 로고    scopus 로고
    • Neutralizing antibody titers conferring protection to macaques from a simian/human immunodeficiency virus challenge using the TZM-bl assay
    • Willey R, Nason MC, Nishimura Y, Follmann DA, Martin MA, (2010) Neutralizing antibody titers conferring protection to macaques from a simian/human immunodeficiency virus challenge using the TZM-bl assay. AIDS Res Hum Retroviruses 26: 89–98. doi: 10.1089/aid.2009.0144 20059398
    • (2010) AIDS Res Hum Retroviruses , vol.26 , pp. 89-98
    • Willey, R.1    Nason, M.C.2    Nishimura, Y.3    Follmann, D.A.4    Martin, M.A.5
  • 18
    • 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: 204–210. 9930869
    • (1999) Nat Med , vol.5 , pp. 204-210
    • Shibata, R.1    Igarashi, T.2    Haigwood, N.3    Buckler-White, A.4    Ogert, R.5
  • 19
    • 20044393036 scopus 로고    scopus 로고
    • Protection of rhesus monkeys against infection with minimally pathogenic simian-human immunodeficiency virus: correlations with neutralizing antibodies and cytotoxic T cells
    • Quinnan GV, Jr.Yu XF, Lewis MG, Zhang PF, Sutter G, et al. (2005) Protection of rhesus monkeys against infection with minimally pathogenic simian-human immunodeficiency virus: correlations with neutralizing antibodies and cytotoxic T cells. J Virol 79: 3358–3369. 15731230
    • (2005) J Virol , vol.79 , pp. 3358-3369
    • Quinnan, G.V.1    Yu, X.F.2    Lewis, M.G.3    Zhang, P.F.4    Sutter, G.5
  • 20
    • 84872258840 scopus 로고    scopus 로고
    • Prime-boost immunization of rabbits with HIV-1 gp120 elicits potent neutralization activity against a primary viral isolate
    • Narayan KM, Agrawal N, Du SX, Muranaka JE, Bauer K, et al. (2013) Prime-boost immunization of rabbits with HIV-1 gp120 elicits potent neutralization activity against a primary viral isolate. PLoS One 8: e52732. doi: 10.1371/journal.pone.0052732 23326351
    • (2013) PLoS One , vol.8 , pp. 52732
    • Narayan, K.M.1    Agrawal, N.2    Du, S.X.3    Muranaka, J.E.4    Bauer, K.5
  • 21
    • 38049083122 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies protect against hepatitis C virus quasispecies challenge
    • Law M, Maruyama T, Lewis J, Giang E, Tarr AW, et al. (2008) Broadly neutralizing antibodies protect against hepatitis C virus quasispecies challenge. Nat Med 14: 25–27. 18064037
    • (2008) Nat Med , vol.14 , pp. 25-27
    • Law, M.1    Maruyama, T.2    Lewis, J.3    Giang, E.4    Tarr, A.W.5
  • 22
    • 47749129289 scopus 로고    scopus 로고
    • Improved induction of antibodies against key neutralizing epitopes by human immunodeficiency virus type 1 gp120 DNA prime-protein boost vaccination compared to gp120 protein-only vaccination
    • Vaine M, Wang S, Crooks ET, Jiang P, Montefiori DC, et al. (2008) Improved induction of antibodies against key neutralizing epitopes by human immunodeficiency virus type 1 gp120 DNA prime-protein boost vaccination compared to gp120 protein-only vaccination. Journal of virology 82: 7369–7378. doi: 10.1128/JVI.00562-08 18495775
    • (2008) Journal of virology , vol.82 , pp. 7369-7378
    • Vaine, M.1    Wang, S.2    Crooks, E.T.3    Jiang, P.4    Montefiori, D.C.5
  • 23
    • 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
  • 24
    • 84930369637 scopus 로고    scopus 로고
    • HIV neutralizing antibodies induced by native-like envelope trimers
    • Sanders RW (2015) HIV neutralizing antibodies induced by native-like envelope trimers. HIV Vaccines Keystone Symposium 2015.
    • (2015) HIV Vaccines Keystone Symposium , pp. 2015
    • Sanders, R.W.1
  • 25
    • 84861324362 scopus 로고    scopus 로고
    • HIV-1 virus-like particles bearing pure env trimers expose neutralizing epitopes but occlude nonneutralizing epitopes
    • Tong T, Crooks ET, Osawa K, Binley JM, (2012) HIV-1 virus-like particles bearing pure env trimers expose neutralizing epitopes but occlude nonneutralizing epitopes. Journal of virology 86: 3574–3587. doi: 10.1128/JVI.06938-11 22301141
    • (2012) Journal of virology , vol.86 , pp. 3574-3587
    • Tong, T.1    Crooks, E.T.2    Osawa, K.3    Binley, J.M.4
  • 26
    • 84870540478 scopus 로고    scopus 로고
    • Virus-like particles as a highly efficient vaccine platform: Diversity of targets and production systems and advances in clinical development
    • Kushnir N, Streatfield SJ, Yusibov V, (2012) Virus-like particles as a highly efficient vaccine platform: Diversity of targets and production systems and advances in clinical development. Vaccine 31: 58–83. doi: 10.1016/j.vaccine.2012.10.083 23142589
    • (2012) Vaccine , vol.31 , pp. 58-83
    • Kushnir, N.1    Streatfield, S.J.2    Yusibov, V.3
  • 28
    • 84897093858 scopus 로고    scopus 로고
    • Multi-Parameter Exploration of HIV-1 Virus-Like Particles as Neutralizing Antibody Immunogens in Guinea Pigs, Rabbits and Macaques
    • Tong T, Crooks ET, Osawa K, Robinson JE, Barnes M, et al. (2014) Multi-Parameter Exploration of HIV-1 Virus-Like Particles as Neutralizing Antibody Immunogens in Guinea Pigs, Rabbits and Macaques. Virology 456–457: 55–69.
    • (2014) Virology , vol.456-457 , pp. 55-69
    • Tong, T.1    Crooks, E.T.2    Osawa, K.3    Robinson, J.E.4    Barnes, M.5
  • 29
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis D, Julien JP, 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
  • 30
    • 84890858459 scopus 로고    scopus 로고
    • Crystal structure of a soluble cleaved HIV-1 envelope trimer
    • Julien JP, 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
  • 32
    • 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
  • 33
    • 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 ZY, 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
  • 34
    • 84917691102 scopus 로고    scopus 로고
    • HIV antibodies. Antigen modification regulates competition of broad and narrow neutralizing HIV antibodies
    • McGuire AT, Dreyer AM, Carbonetti S, Lippy A, Glenn J, et al. (2014) HIV antibodies. Antigen modification regulates competition of broad and narrow neutralizing HIV antibodies. Science 346: 1380–1383. doi: 10.1126/science.1259206 25504724
    • (2014) Science , vol.346 , pp. 1380-1383
    • McGuire, A.T.1    Dreyer, A.M.2    Carbonetti, S.3    Lippy, A.4    Glenn, J.5
  • 35
    • 79959716257 scopus 로고    scopus 로고
    • Molecular bases of genetic diversity and evolution of the immunoglobulin heavy chain variable region (IGHV) gene locus in leporids
    • Pinheiro A, Lanning D, Alves PC, Mage RG, Knight KL, et al. (2011) Molecular bases of genetic diversity and evolution of the immunoglobulin heavy chain variable region (IGHV) gene locus in leporids. Immunogenetics 63: 397–408. doi: 10.1007/s00251-011-0533-9 21594770
    • (2011) Immunogenetics , vol.63 , pp. 397-408
    • Pinheiro, A.1    Lanning, D.2    Alves, P.C.3    Mage, R.G.4    Knight, K.L.5
  • 36
    • 84883261870 scopus 로고    scopus 로고
    • Rabbit anti-HIV-1 monoclonal antibodies raised by immunization can mimic the antigen-binding modes of antibodies derived from HIV-1-infected humans
    • Pan R, Sampson JM, Chen Y, Vaine M, Wang S, et al. (2013) Rabbit anti-HIV-1 monoclonal antibodies raised by immunization can mimic the antigen-binding modes of antibodies derived from HIV-1-infected humans. J Virol 87: 10221–10231. doi: 10.1128/JVI.00843-13 23864637
    • (2013) J Virol , vol.87 , pp. 10221-10231
    • Pan, R.1    Sampson, J.M.2    Chen, Y.3    Vaine, M.4    Wang, S.5
  • 37
    • 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: 285–289. doi: 10.1126/science.1178746 19729618
    • (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
  • 38
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X, Yang ZY, Li Y, Hogerkorp CM, Schief WR, et al. (2010) Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 329: 856–861. doi: 10.1126/science.1187659 20616233
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1    Yang, Z.Y.2    Li, Y.3    Hogerkorp, C.M.4    Schief, W.R.5
  • 39
    • 77649318846 scopus 로고    scopus 로고
    • Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals
    • Corti D, Langedijk JP, Hinz A, Seaman MS, Vanzetta F, et al. (2010) Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals. PLoS One 5: e8805. doi: 10.1371/journal.pone.0008805 20098712
    • (2010) PLoS One , vol.5 , pp. 8805
    • Corti, D.1    Langedijk, J.P.2    Hinz, A.3    Seaman, M.S.4    Vanzetta, F.5
  • 40
    • 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
  • 41
    • 80052938385 scopus 로고    scopus 로고
    • Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors
    • Bonsignori M, Hwang KK, Chen X, Tsao CY, Morris L, et al. (2011) Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors. J Virol 85: 9998–10009. doi: 10.1128/JVI.05045-11 21795340
    • (2011) J Virol , vol.85 , pp. 9998-10009
    • Bonsignori, M.1    Hwang, K.K.2    Chen, X.3    Tsao, C.Y.4    Morris, L.5
  • 42
    • 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
  • 43
    • 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
  • 44
    • 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
  • 45
    • 84866493348 scopus 로고    scopus 로고
    • Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
    • Huang J, Ofek G, Laub L, Louder MK, Doria-Rose NA, et al. (2012) Broad and potent neutralization of HIV-1 by a gp41-specific human antibody. Nature 491: 406–412. doi: 10.1038/nature11544 23151583
    • (2012) Nature , vol.491 , pp. 406-412
    • Huang, J.1    Ofek, G.2    Laub, L.3    Louder, M.K.4    Doria-Rose, N.A.5
  • 46
    • 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
  • 47
    • 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, Jr.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
  • 48
    • 84917705974 scopus 로고    scopus 로고
    • Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex
    • Sok D, van Gils MJ, Pauthner M, Julien JP, Saye-Francisco KL, et al. (2014) Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex. Proc Natl Acad Sci U S A 111: 17624–17629. doi: 10.1073/pnas.1415789111 25422458
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 17624-17629
    • Sok, D.1    van Gils, M.J.2    Pauthner, M.3    Julien, J.P.4    Saye-Francisco, K.L.5
  • 49
    • 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
  • 50
    • 34548577658 scopus 로고    scopus 로고
    • A comparative immunogenicity study of HIV-1 virus-like particles bearing various forms of envelope proteins, particles bearing no envelope and soluble monomeric gp120
    • Crooks ET, Moore PL, Franti M, Cayanan CS, Zhu P, et al. (2007) A comparative immunogenicity study of HIV-1 virus-like particles bearing various forms of envelope proteins, particles bearing no envelope and soluble monomeric gp120. Virology 366: 245–262. 17580087
    • (2007) Virology , vol.366 , pp. 245-262
    • Crooks, E.T.1    Moore, P.L.2    Franti, M.3    Cayanan, C.S.4    Zhu, P.5
  • 51
    • 33144486096 scopus 로고    scopus 로고
    • Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1
    • Moore PL, Crooks ET, Porter L, Zhu P, Cayanan CS, et al. (2006) Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1. J Virol 80: 2515–2528. 16474158
    • (2006) J Virol , vol.80 , pp. 2515-2528
    • Moore, P.L.1    Crooks, E.T.2    Porter, L.3    Zhu, P.4    Cayanan, C.S.5
  • 52
    • 79958086672 scopus 로고    scopus 로고
    • Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected
    • Crooks ET, Tong T, Osawa K, Binley JM, (2011) Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected. Journal of virology 85: 5825–5839. doi: 10.1128/JVI.00154-11 21471242
    • (2011) Journal of virology , vol.85 , pp. 5825-5839
    • Crooks, E.T.1    Tong, T.2    Osawa, K.3    Binley, J.M.4
  • 53
    • 33646720281 scopus 로고    scopus 로고
    • Characterizing anti-HIV monoclonal antibodies and immune sera by defining the mechanism of neutralization
    • Crooks ET, Moore PL, Richman D, Robinson J, Crooks JA, et al. (2005) Characterizing anti-HIV monoclonal antibodies and immune sera by defining the mechanism of neutralization. Hum Antibodies 14: 101–113. 16720980
    • (2005) Hum Antibodies , vol.14 , pp. 101-113
    • Crooks, E.T.1    Moore, P.L.2    Richman, D.3    Robinson, J.4    Crooks, J.A.5
  • 54
    • 56449131391 scopus 로고    scopus 로고
    • Profiling the specificity of neutralizing antibodies in a large panel of plasmas from patients chronically infected with human immunodeficiency virus type 1 subtypes B and C
    • Binley JM, Lybarger EA, Crooks ET, Seaman MS, Gray E, et al. (2008) Profiling the specificity of neutralizing antibodies in a large panel of plasmas from patients chronically infected with human immunodeficiency virus type 1 subtypes B and C. Journal of virology 82: 11651–11668. doi: 10.1128/JVI.01762-08 18815292
    • (2008) Journal of virology , vol.82 , pp. 11651-11668
    • Binley, J.M.1    Lybarger, E.A.2    Crooks, E.T.3    Seaman, M.S.4    Gray, E.5
  • 55
    • 0038076112 scopus 로고    scopus 로고
    • Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions
    • Binley JM, Cayanan CS, Wiley C, Schulke N, Olson WC, et al. (2003) Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions. J Virol 77: 5678–5684. 12719560
    • (2003) J Virol , vol.77 , pp. 5678-5684
    • Binley, J.M.1    Cayanan, C.S.2    Wiley, C.3    Schulke, N.4    Olson, W.C.5
  • 56
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • Doores KJ, Burton DR, (2010) Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. J Virol 84: 10510–10521. doi: 10.1128/JVI.00552-10 20686044
    • (2010) J Virol , vol.84 , pp. 10510-10521
    • Doores, K.J.1    Burton, D.R.2
  • 57
    • 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
  • 58
    • 33947590277 scopus 로고    scopus 로고
    • A comparative immunogenicity study in rabbits of disulfide-stabilized, proteolytically cleaved, soluble trimeric human immunodeficiency virus type 1 gp140, trimeric cleavage-defective gp140 and monomeric gp120
    • Beddows S, Franti M, Dey AK, Kirschner M, Iyer SP, et al. (2007) A comparative immunogenicity study in rabbits of disulfide-stabilized, proteolytically cleaved, soluble trimeric human immunodeficiency virus type 1 gp140, trimeric cleavage-defective gp140 and monomeric gp120. Virology 360: 329–340. 17126869
    • (2007) Virology , vol.360 , pp. 329-340
    • Beddows, S.1    Franti, M.2    Dey, A.K.3    Kirschner, M.4    Iyer, S.P.5
  • 59
    • 34247166722 scopus 로고    scopus 로고
    • Antigenic and immunogenic study of membrane-proximal external region-grafted gp120 antigens by a DNA prime-protein boost immunization strategy
    • Law M, Cardoso RM, Wilson IA, Burton DR, (2007) Antigenic and immunogenic study of membrane-proximal external region-grafted gp120 antigens by a DNA prime-protein boost immunization strategy. J Virol 81: 4272–4285. 17267498
    • (2007) J Virol , vol.81 , pp. 4272-4285
    • Law, M.1    Cardoso, R.M.2    Wilson, I.A.3    Burton, D.R.4
  • 60
    • 84881238207 scopus 로고    scopus 로고
    • Topological analysis of HIV-1 glycoproteins expressed in situ on virus surfaces reveals tighter packing but greater conformational flexibility than for soluble gp120
    • Tong T, Osawa K, Robinson JE, Crooks ET, Binley JM, (2013) Topological analysis of HIV-1 glycoproteins expressed in situ on virus surfaces reveals tighter packing but greater conformational flexibility than for soluble gp120. J Virol 87: 9233–9249. doi: 10.1128/JVI.01145-13 23740975
    • (2013) J Virol , vol.87 , pp. 9233-9249
    • Tong, T.1    Osawa, K.2    Robinson, J.E.3    Crooks, E.T.4    Binley, J.M.5
  • 61
    • 43149113443 scopus 로고    scopus 로고
    • 4E10 and 2F5 monoclonal antibodies: binding specificities to phospholipids, tolerance, and clinical safety issues
    • Alving CR, (2008) 4E10 and 2F5 monoclonal antibodies: binding specificities to phospholipids, tolerance, and clinical safety issues. AIDS 22: 649–651. doi: 10.1097/QAD.0b013e3282f51922 18317008
    • (2008) AIDS , vol.22 , pp. 649-651
    • Alving, C.R.1
  • 62
    • 38849205377 scopus 로고    scopus 로고
    • Enhancing exposure of HIV-1 neutralization epitopes through mutations in gp41
    • Blish CA, Nguyen MA, Overbaugh J, (2008) Enhancing exposure of HIV-1 neutralization epitopes through mutations in gp41. PLoS Med 5: e9. doi: 10.1371/journal.pmed.0050009 18177204
    • (2008) PLoS Med , vol.5 , pp. 9
    • Blish, C.A.1    Nguyen, M.A.2    Overbaugh, J.3
  • 63
    • 77950537428 scopus 로고    scopus 로고
    • Prolonged exposure of the HIV-1 gp41 membrane proximal region with L669S substitution
    • Shen X, Dennison SM, Liu P, Gao F, Jaeger F, et al. (2010) Prolonged exposure of the HIV-1 gp41 membrane proximal region with L669S substitution. Proc Natl Acad Sci U S A 107: 5972–5977. doi: 10.1073/pnas.0912381107 20231447
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5972-5977
    • Shen, X.1    Dennison, S.M.2    Liu, P.3    Gao, F.4    Jaeger, F.5
  • 64
    • 77952001983 scopus 로고    scopus 로고
    • Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization
    • Binley JM, Ban YE, Crooks ET, Eggink D, Osawa K, et al. (2010) Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization. Journal of virology 84: 5637–5655. doi: 10.1128/JVI.00105-10 20335257
    • (2010) Journal of virology , vol.84 , pp. 5637-5655
    • Binley, J.M.1    Ban, Y.E.2    Crooks, E.T.3    Eggink, D.4    Osawa, K.5
  • 65
    • 84878566279 scopus 로고    scopus 로고
    • Inhibition of the HIV-1 spike by single-PG9/16-antibody binding suggests a coordinated-activation model for its three protomeric units
    • Loving R, Sjoberg M, Wu SR, Binley JM, Garoff H, (2013) Inhibition of the HIV-1 spike by single-PG9/16-antibody binding suggests a coordinated-activation model for its three protomeric units. J Virol 87: 7000–7007. doi: 10.1128/JVI.00530-13 23596290
    • (2013) J Virol , vol.87 , pp. 7000-7007
    • Loving, R.1    Sjoberg, M.2    Wu, S.R.3    Binley, J.M.4    Garoff, H.5
  • 66
    • 84926453015 scopus 로고    scopus 로고
    • Comprehensive Antigenic Map of a Cleaved Soluble HIV-1 Envelope Trimer
    • Derking R, Ozorowski G, Sliepen K, Yasmeen A, Cupo A, et al. (2015) Comprehensive Antigenic Map of a Cleaved Soluble HIV-1 Envelope Trimer. PLoS Pathog 11: e1004767. doi: 10.1371/journal.ppat.1004767 25807248
    • (2015) PLoS Pathog , vol.11 , pp. 1004767
    • Derking, R.1    Ozorowski, G.2    Sliepen, K.3    Yasmeen, A.4    Cupo, A.5
  • 67
    • 84883158359 scopus 로고    scopus 로고
    • A human antibody to the CD4 binding site of gp120 capable of highly potent but sporadic cross clade neutralization of primary HIV-1
    • Gach JS, Quendler H, Tong T, Narayan KM, Du SX, et al. (2013) A human antibody to the CD4 binding site of gp120 capable of highly potent but sporadic cross clade neutralization of primary HIV-1. PLoS One 8: e72054. doi: 10.1371/journal.pone.0072054 23991039
    • (2013) PLoS One , vol.8 , pp. 72054
    • Gach, J.S.1    Quendler, H.2    Tong, T.3    Narayan, K.M.4    Du, S.X.5
  • 68
    • 79954589594 scopus 로고    scopus 로고
    • Genetic and neutralization sensitivity of diverse HIV-1 env clones from chronically infected patients in China
    • Shang H, Han X, Shi X, Zuo T, Goldin M, et al. (2011) Genetic and neutralization sensitivity of diverse HIV-1 env clones from chronically infected patients in China. J Biol Chem 286: 14531–14541. doi: 10.1074/jbc.M111.224527 21325278
    • (2011) J Biol Chem , vol.286 , pp. 14531-14541
    • Shang, H.1    Han, X.2    Shi, X.3    Zuo, T.4    Goldin, M.5
  • 69
    • 84877618448 scopus 로고    scopus 로고
    • Delineating antibody recognition in polyclonal sera from patterns of HIV-1 isolate neutralization
    • Georgiev IS, Doria-Rose NA, Zhou T, Kwon YD, Staupe RP, et al. (2013) Delineating antibody recognition in polyclonal sera from patterns of HIV-1 isolate neutralization. Science 340: 751–756. doi: 10.1126/science.1233989 23661761
    • (2013) Science , vol.340 , pp. 751-756
    • Georgiev, I.S.1    Doria-Rose, N.A.2    Zhou, T.3    Kwon, Y.D.4    Staupe, R.P.5
  • 70
    • 37849026069 scopus 로고    scopus 로고
    • Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses
    • Li Y, Cleveland B, Klots I, Travis B, Richardson BA, et al. (2008) Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses. J Virol 82: 638–651. 17959660
    • (2008) J Virol , vol.82 , pp. 638-651
    • Li, Y.1    Cleveland, B.2    Klots, I.3    Travis, B.4    Richardson, B.A.5
  • 71
    • 84879538530 scopus 로고    scopus 로고
    • Computational analysis of anti-HIV-1 antibody neutralization panel data to identify potential functional epitope residues
    • West AP, Jr.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
  • 72
    • 84883381602 scopus 로고    scopus 로고
    • Residue-level prediction of HIV-1 antibody epitopes based on neutralization of diverse viral strains
    • Chuang GY, Acharya P, Schmidt SD, Yang Y, Louder MK, et al. (2013) Residue-level prediction of HIV-1 antibody epitopes based on neutralization of diverse viral strains. J Virol 87: 10047–10058. doi: 10.1128/JVI.00984-13 23843642
    • (2013) J Virol , vol.87 , pp. 10047-10058
    • Chuang, G.Y.1    Acharya, P.2    Schmidt, S.D.3    Yang, Y.4    Louder, M.K.5
  • 73
    • 79961221361 scopus 로고    scopus 로고
    • A prime-boost strategy using virus-like particles pseudotyped for HCV proteins triggers broadly neutralizing antibodies in macaques
    • Garrone P, Fluckiger AC, Mangeot PE, Gauthier E, Dupeyrot-Lacas P, et al. (2011) A prime-boost strategy using virus-like particles pseudotyped for HCV proteins triggers broadly neutralizing antibodies in macaques. Sci Transl Med 3: 94ra71.
    • (2011) Sci Transl Med , vol.3 , pp. 71
    • Garrone, P.1    Fluckiger, A.C.2    Mangeot, P.E.3    Gauthier, E.4    Dupeyrot-Lacas, P.5
  • 74
    • 84930373269 scopus 로고    scopus 로고
    • Why HIV Virions Have Low Numbers of Envelope Spikes: Implications for Vaccine Development
    • Schiller J, Chackerian B, (2014) Why HIV Virions Have Low Numbers of Envelope Spikes: Implications for Vaccine Development. PLoS Pathog 10: e1004254. doi: 10.1371/journal.ppat.1004254 25101974
    • (2014) PLoS Pathog , vol.10 , pp. 1004254
    • Schiller, J.1    Chackerian, B.2
  • 75
    • 84891630009 scopus 로고    scopus 로고
    • Improvement of antibody responses by HIV envelope DNA and protein co-immunization
    • Pissani F, Malherbe DC, Schuman JT, Robins H, Park BS, et al. (2014) Improvement of antibody responses by HIV envelope DNA and protein co-immunization. Vaccine 32: 507–513. doi: 10.1016/j.vaccine.2013.11.022 24280279
    • (2014) Vaccine , vol.32 , pp. 507-513
    • Pissani, F.1    Malherbe, D.C.2    Schuman, J.T.3    Robins, H.4    Park, B.S.5
  • 76
    • 84875061923 scopus 로고    scopus 로고
    • Recombinant HIV envelope proteins fail to engage germline versions of anti-CD4bs bNAbs
    • Hoot S, McGuire AT, Cohen KW, Strong RK, Hangartner L, et al. (2013) Recombinant HIV envelope proteins fail to engage germline versions of anti-CD4bs bNAbs. PLoS Pathog 9: e1003106. doi: 10.1371/journal.ppat.1003106 23300456
    • (2013) PLoS Pathog , vol.9 , pp. 1003106
    • Hoot, S.1    McGuire, A.T.2    Cohen, K.W.3    Strong, R.K.4    Hangartner, L.5
  • 77
    • 0041920924 scopus 로고    scopus 로고
    • Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition
    • Koch M, Pancera M, Kwong PD, Kolchinsky P, Grundner C, et al. (2003) Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition. Virology 313: 387–400. 12954207
    • (2003) Virology , vol.313 , pp. 387-400
    • Koch, M.1    Pancera, M.2    Kwong, P.D.3    Kolchinsky, P.4    Grundner, C.5
  • 78
    • 12144289425 scopus 로고    scopus 로고
    • Envelope-constrained neutralization-sensitive HIV-1 after heterosexual transmission
    • Derdeyn CA, Decker JM, Bibollet-Ruche F, Mokili JL, Muldoon M, et al. (2004) Envelope-constrained neutralization-sensitive HIV-1 after heterosexual transmission. Science 303: 2019–2022. 15044802
    • (2004) Science , vol.303 , pp. 2019-2022
    • Derdeyn, C.A.1    Decker, J.M.2    Bibollet-Ruche, F.3    Mokili, J.L.4    Muldoon, M.5
  • 79
    • 18144397438 scopus 로고    scopus 로고
    • Selection for human immunodeficiency virus type 1 envelope glycosylation variants with shorter V1-V2 loop sequences occurs during transmission of certain genetic subtypes and may impact viral RNA levels
    • Chohan B, Lang D, Sagar M, Korber B, Lavreys L, et al. (2005) Selection for human immunodeficiency virus type 1 envelope glycosylation variants with shorter V1-V2 loop sequences occurs during transmission of certain genetic subtypes and may impact viral RNA levels. J Virol 79: 6528–6531. 15858037
    • (2005) J Virol , vol.79 , pp. 6528-6531
    • Chohan, B.1    Lang, D.2    Sagar, M.3    Korber, B.4    Lavreys, L.5
  • 80
    • 30344485709 scopus 로고    scopus 로고
    • Neutralization escape variants of human immunodeficiency virus type 1 are transmitted from mother to infant
    • Wu X, Parast AB, Richardson BA, Nduati R, John-Stewart G, et al. (2006) Neutralization escape variants of human immunodeficiency virus type 1 are transmitted from mother to infant. J Virol 80: 835–844. 16378985
    • (2006) J Virol , vol.80 , pp. 835-844
    • Wu, X.1    Parast, A.B.2    Richardson, B.A.3    Nduati, R.4    John-Stewart, G.5
  • 81
    • 84905369598 scopus 로고    scopus 로고
    • Cooperation of B Cell Lineages in Induction of HIV-1-Broadly Neutralizing Antibodies
    • Gao F, Bonsignori M, Liao HX, Kumar A, Xia SM, 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
  • 82
    • 84884654961 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein signatures that correlate with the development of cross-reactive neutralizing activity
    • van den Kerkhof TL, Feenstra KA, Euler Z, van Gils MJ, Rijsdijk LW, et al. (2013) HIV-1 envelope glycoprotein signatures that correlate with the development of cross-reactive neutralizing activity. Retrovirology 10: 102. doi: 10.1186/1742-4690-10-102 24059682
    • (2013) Retrovirology , vol.10 , pp. 102
    • van den Kerkhof, T.L.1    Feenstra, K.A.2    Euler, Z.3    van Gils, M.J.4    Rijsdijk, L.W.5
  • 83
    • 84876797103 scopus 로고    scopus 로고
    • Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus
    • Liao HX, Lynch R, Zhou T, Gao F, Alam SM, et al. (2013) Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. Nature 496: 469–476. doi: 10.1038/nature12053 23552890
    • (2013) Nature , vol.496 , pp. 469-476
    • Liao, H.X.1    Lynch, R.2    Zhou, T.3    Gao, F.4    Alam, S.M.5
  • 84
    • 84899991983 scopus 로고    scopus 로고
    • Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies
    • Doria-Rose NA, Schramm CA, 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.A.1    Schramm, C.A.2    Gorman, J.3    Moore, P.L.4    Bhiman, J.N.5
  • 85
    • 84877626973 scopus 로고    scopus 로고
    • Viral escape from neutralizing antibodies in early subtype A HIV-1 infection drives an increase in autologous neutralization breadth
    • Murphy MK, Yue L, Pan R, Boliar S, Sethi A, et al. (2013) Viral escape from neutralizing antibodies in early subtype A HIV-1 infection drives an increase in autologous neutralization breadth. PLoS Pathog 9: e1003173. doi: 10.1371/journal.ppat.1003173 23468623
    • (2013) PLoS Pathog , vol.9 , pp. 1003173
    • Murphy, M.K.1    Yue, L.2    Pan, R.3    Boliar, S.4    Sethi, A.5
  • 86
    • 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, Poulsen C, Guenaga J, de Val N, Wilson R, et al. (2014) 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 111: E738–747. doi: 10.1073/pnas.1319512111 24550318
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 738-747
    • Tran, K.1    Poulsen, C.2    Guenaga, J.3    de Val, N.4    Wilson, R.5
  • 87
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of a1—>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 a1—>2 mannose residues on the outer face of gp120. J Virol 76: 7306–7321. 12072529
    • (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
  • 89
    • 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. doi: 10.1371/journal.pone.0023521 21858152
    • (2011) PloS one , vol.6 , pp. 23521
    • Bonomelli, C.1    Doores, K.J.2    Dunlop, D.C.3    Thaney, V.4    Dwek, R.A.5
  • 90
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2—a multiple sequence alignment editor and analysis workbench
    • Waterhouse AM, Procter JB, Martin DM, Clamp M, Barton GJ, (2009) Jalview Version 2—a multiple sequence alignment editor and analysis workbench. Bioinformatics 25: 1189–1191. doi: 10.1093/bioinformatics/btp033 19151095
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.