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Volumn 89, Issue 15, 2015, Pages 7478-7493

Comparable antigenicity and immunogenicity of oligomeric forms of a novel, acute HIV-1 subtype C gp145 envelope for use in preclinical and clinical vaccine research

(32)  Wieczorek, Lindsay a,b   Krebs, Shelly J a,b   Kalyanaraman, Vaniambadi c   Whitney, Stephen c   Tovanabutra, Sodsai a,b   Moscoso, Carlos G d,m   Sanders Buell, Eric a,b   Williams, Constance e   Slike, Bonnie a,b   Molnar, Sebastian a,b   Dussupt, Vincent a,b   Munir Alam, S f   Chenine, Agnes Laurence a,b   Tong, Tina b,l   Hill, Edgar L b   Liao, Hua Xin f   Hoelscher, Michael h,i   Maboko, Leonard j   Zolla Pazner, Susan e   Haynes, Barton F f   more..


Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN GP 145 VACCINE; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; VIRUS ENVELOPE PROTEIN;

EID: 84937689183     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00412-15     Document Type: Article
Times cited : (33)

References (97)
  • 1
    • 0035162494 scopus 로고    scopus 로고
    • Evolutionary and immunological implications of contemporary HIV-1 variation
    • Korber B, Gaschen B, Yusim K, Thakallapally R, Kesmir C, Detours V. 2001. Evolutionary and immunological implications of contemporary HIV-1 variation. Br Med Bull 58:19-42. http://dx.doi.org/10.1093/bmb/58.1.19.
    • (2001) Br Med Bull , vol.58 , pp. 19-42
    • Korber, B.1    Gaschen, B.2    Yusim, K.3    Thakallapally, R.4    Kesmir, C.5    Detours, V.6
  • 2
    • 0034978733 scopus 로고    scopus 로고
    • Genetic subtypes, humoral immunity, and human immunodeficiency virus type 1 vaccine development
    • Moore JP, Parren PW, Burton DR. 2001. Genetic subtypes, humoral immunity, and human immunodeficiency virus type 1 vaccine development. J Virol 75:5721-5729. http://dx.doi.org/10.1128/JVI.75.13.5721-5729.2001.
    • (2001) J Virol , vol.75 , pp. 5721-5729
    • Moore, J.P.1    Parren, P.W.2    Burton, D.R.3
  • 4
    • 78650876330 scopus 로고    scopus 로고
    • Correlations between HIV-1 clades and HIV-1 antibody neutralization sensitivity: significant for vaccine development?
    • van Gils MJ, Schuitemaker H. 2010. Correlations between HIV-1 clades and HIV-1 antibody neutralization sensitivity: significant for vaccine development?. Curr HIV Res 8:579-586. http://dx.doi.org/10.2174/157016210794088254.
    • (2010) Curr HIV Res , vol.8 , pp. 579-586
    • van Gils, M.J.1    Schuitemaker, H.2
  • 5
    • 33750253231 scopus 로고    scopus 로고
    • Global and regional distribution of HIV-1 genetic subtypes and recombinants in 2004
    • Hemelaar J, Gouws E, Ghys PD, Osmanov S. 2006. Global and regional distribution of HIV-1 genetic subtypes and recombinants in 2004. AIDS 20:W13-23. http://dx.doi.org/10.1097/01.aids.0000247564.73009.bc.
    • (2006) AIDS , vol.20 , pp. W13-W23
    • Hemelaar, J.1    Gouws, E.2    Ghys, P.D.3    Osmanov, S.4
  • 6
    • 34648824673 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 subtype distribution in the worldwide epidemic: pathogenetic and therapeutic implications
    • Buonaguro L, Tornesello ML, Buonaguro FM. 2007. Human immunodeficiency virus type 1 subtype distribution in the worldwide epidemic: pathogenetic and therapeutic implications. J Virol 81:10209-10219. http://dx.doi.org/10.1128/JVI.00872-07.
    • (2007) J Virol , vol.81 , pp. 10209-10219
    • Buonaguro, L.1    Tornesello, M.L.2    Buonaguro, F.M.3
  • 7
    • 43249120051 scopus 로고    scopus 로고
    • Cross-clade neutralization patterns among HIV-1 strains from the six major clades of the pandemic evaluated and compared in two different models
    • Brown BK, Wieczorek L, Sanders-Buell E, Rosa Borges A, Robb ML, Birx DL, Michael NL, McCutchan FE, Polonis VR. 2008. Cross-clade neutralization patterns among HIV-1 strains from the six major clades of the pandemic evaluated and compared in two different models. Virology 375:529-538. http://dx.doi.org/10.1016/j.virol.2008.02.022.
    • (2008) Virology , vol.375 , pp. 529-538
    • Brown, B.K.1    Wieczorek, L.2    Sanders-Buell, E.3    Rosa Borges, A.4    Robb, M.L.5    Birx, D.L.6    Michael, N.L.7    McCutchan, F.E.8    Polonis, V.R.9
  • 12
    • 79952414942 scopus 로고    scopus 로고
    • Global trends in molecular epidemiology of HIV-1 during 2000-2007
    • Hemelaar J, Gouws E, Ghys PD, Osmanov S. 2011. Global trends in molecular epidemiology of HIV-1 during 2000-2007. AIDS 25:679-689. http://dx.doi.org/10.1097/QAD.0b013e328342ff93.
    • (2011) AIDS , vol.25 , pp. 679-689
    • Hemelaar, J.1    Gouws, E.2    Ghys, P.D.3    Osmanov, S.4
  • 14
    • 79551518897 scopus 로고    scopus 로고
    • Characteristics of the earliest cross-neutralizing antibody response to HIV-1
    • Mikell I, Sather DN, Kalams SA, Altfeld M, Alter G, Stamatatos L. 2011. Characteristics of the earliest cross-neutralizing antibody response to HIV-1. PLoS Pathog 7:e1001251. http://dx.doi.org/10.1371/journal.ppat.1001251.
    • (2011) PLoS Pathog , vol.7
    • Mikell, I.1    Sather, D.N.2    Kalams, S.A.3    Altfeld, M.4    Alter, G.5    Stamatatos, L.6
  • 16
    • 58149487645 scopus 로고    scopus 로고
    • Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection
    • Sather DN, Armann J, Ching LK, Mavrantoni A, Sellhorn G, Caldwell Z, Yu X, Wood B, Self S, Kalams S, Stamatatos L. 2009. Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J Virol 83:757-769. http://dx.doi.org/10.1128/JVI.02036-08.
    • (2009) J Virol , vol.83 , pp. 757-769
    • Sather, D.N.1    Armann, J.2    Ching, L.K.3    Mavrantoni, A.4    Sellhorn, G.5    Caldwell, Z.6    Yu, X.7    Wood, B.8    Self, S.9    Kalams, S.10    Stamatatos, L.11
  • 17
    • 84892365659 scopus 로고    scopus 로고
    • Prevalence of broadly neutralizing antibody responses during chronic HIV-1 infection
    • Hraber P, Seaman MS, Bailer RT, Mascola JR, Montefiori DC, Korber BT. 2014. Prevalence of broadly neutralizing antibody responses during chronic HIV-1 infection. AIDS 28:163-169. http://dx.doi.org/10.1097/QAD.0000000000000106.
    • (2014) AIDS , vol.28 , pp. 163-169
    • Hraber, P.1    Seaman, M.S.2    Bailer, R.T.3    Mascola, J.R.4    Montefiori, D.C.5    Korber, B.T.6
  • 19
    • 77958115264 scopus 로고    scopus 로고
    • A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals
    • Walker LM, Simek MD, Priddy F, Gach JS, Wagner D, Zwick MB, Phogat SK, Poignard P, Burton DR. 2010. A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals. PLoS Pathog 6:e1001028. http://dx.doi.org/10.1371/journal.ppat.1001028.
    • (2010) PLoS Pathog , vol.6
    • Walker, L.M.1    Simek, M.D.2    Priddy, F.3    Gach, J.S.4    Wagner, D.5    Zwick, M.B.6    Phogat, S.K.7    Poignard, P.8    Burton, D.R.9
  • 36
    • 41649090223 scopus 로고    scopus 로고
    • A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies
    • Frey G, Peng H, Rits-Volloch S, Morelli M, Cheng Y, Chen B. 2008. A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies. Proc Natl Acad Sci USA 105:3739-3744. http://dx.doi.org/10.1073/pnas.0800255105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3739-3744
    • Frey, G.1    Peng, H.2    Rits-Volloch, S.3    Morelli, M.4    Cheng, Y.5    Chen, B.6
  • 37
    • 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. http://dx.doi.org/10.1006/jsbi.1999.4174.
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 38
    • 33947635198 scopus 로고    scopus 로고
    • The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes
    • Alam SM, McAdams M, Boren D, Rak M, Scearce RM, Gao F, Camacho ZT, Gewirth D, Kelsoe G, Chen P, Haynes BF. 2007. The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes. J Immunol 178:4424-4435. http://dx.doi.org/10.4049/jimmunol.178.7.4424.
    • (2007) J Immunol , vol.178 , pp. 4424-4435
    • Alam, S.M.1    McAdams, M.2    Boren, D.3    Rak, M.4    Scearce, R.M.5    Gao, F.6    Camacho, Z.T.7    Gewirth, D.8    Kelsoe, G.9    Chen, P.10    Haynes, B.F.11
  • 41
    • 43049120226 scopus 로고    scopus 로고
    • Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet
    • Abdiche Y, Malashock D, Pinkerton A, Pons J. 2008. Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet. Anal Biochem 377:209-217. http://dx.doi.org/10.1016/j.ab.2008.03.035.
    • (2008) Anal Biochem , vol.377 , pp. 209-217
    • Abdiche, Y.1    Malashock, D.2    Pinkerton, A.3    Pons, J.4
  • 43
    • 2342644898 scopus 로고    scopus 로고
    • The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection
    • Pinter A, Honnen WJ, He Y, Gorny MK, Zolla-Pazner S, Kayman SC. 2004. The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection. J Virol 78:5205-5215. http://dx.doi.org/10.1128/JVI.78.10.5205-5215.2004.
    • (2004) J Virol , vol.78 , pp. 5205-5215
    • Pinter, A.1    Honnen, W.J.2    He, Y.3    Gorny, M.K.4    Zolla-Pazner, S.5    Kayman, S.C.6
  • 45
    • 0034652565 scopus 로고    scopus 로고
    • Effects of oligomerization on the epitopes of the human immunodeficiency virus type 1 envelope glycoproteins
    • Gorny MK, VanCott TC, Williams C, Revesz K, Zolla-Pazner S. 2000. Effects of oligomerization on the epitopes of the human immunodeficiency virus type 1 envelope glycoproteins. Virology 267:220-228. http://dx.doi.org/10.1006/viro.1999.0095.
    • (2000) Virology , vol.267 , pp. 220-228
    • Gorny, M.K.1    VanCott, T.C.2    Williams, C.3    Revesz, K.4    Zolla-Pazner, S.5
  • 46
    • 0033942757 scopus 로고    scopus 로고
    • Conserved and exposed epitopes on intact, native, primary human immunodeficiency virus type 1 virions of group M
    • Nyambi PN, Mbah HA, Burda S, Williams C, Gorny MK, Nadas A, Zolla-Pazner S. 2000. Conserved and exposed epitopes on intact, native, primary human immunodeficiency virus type 1 virions of group M. J Virol 74:7096-7107. http://dx.doi.org/10.1128/JVI.74.15.7096-7107.2000.
    • (2000) J Virol , vol.74 , pp. 7096-7107
    • Nyambi, P.N.1    Mbah, H.A.2    Burda, S.3    Williams, C.4    Gorny, M.K.5    Nadas, A.6    Zolla-Pazner, S.7
  • 47
    • 79952232940 scopus 로고    scopus 로고
    • The genotype of early-transmitting HIV gp120s promotes alpha(4)beta(7)-reactivity, revealing alpha(4)beta(7)/CD4 T cells as key targets in mucosal transmission
    • Nawaz F, Cicala C, Van Ryk D, Block KE, Jelicic K, McNally JP, Ogundare O, Pascuccio M, Patel N, Wei D, Fauci AS, Arthos J. 2011. The genotype of early-transmitting HIV gp120s promotes alpha(4)beta(7)-reactivity, revealing alpha(4)beta(7)/CD4 T cells as key targets in mucosal transmission. PLoS Pathog 7:e1001301. http://dx.doi.org/10.1371/journal.ppat.1001301.
    • (2011) PLoS Pathog , vol.7
    • Nawaz, F.1    Cicala, C.2    Van Ryk, D.3    Block, K.E.4    Jelicic, K.5    McNally, J.P.6    Ogundare, O.7    Pascuccio, M.8    Patel, N.9    Wei, D.10    Fauci, A.S.11    Arthos, J.12
  • 48
    • 1342333037 scopus 로고    scopus 로고
    • Oil-in-water liposomal emulsions for vaccine delivery
    • Matyas GR, Muderhwa JM, Alving CR. 2003. Oil-in-water liposomal emulsions for vaccine delivery. Methods Enzymol 373:34-50. http://dx.doi.org/10.1016/S0076-6879(03)73003-1.
    • (2003) Methods Enzymol , vol.373 , pp. 34-50
    • Matyas, G.R.1    Muderhwa, J.M.2    Alving, C.R.3
  • 49
    • 77649337650 scopus 로고    scopus 로고
    • Neutralizing antibodies induced by liposomal HIV-1 glycoprotein 41 peptide simultaneously bind to both the 2F5 or 4E10 epitope and lipid epitopes
    • Matyas GR, Wieczorek L, Beck Z, Ochsenbauer-Jambor C, Kappes JC, Michael NL, Polonis VR, Alving CR. 2009. Neutralizing antibodies induced by liposomal HIV-1 glycoprotein 41 peptide simultaneously bind to both the 2F5 or 4E10 epitope and lipid epitopes. AIDS 23:2069-2077. http://dx.doi.org/10.1097/QAD.0b013e32832faea5.
    • (2009) AIDS , vol.23 , pp. 2069-2077
    • Matyas, G.R.1    Wieczorek, L.2    Beck, Z.3    Ochsenbauer-Jambor, C.4    Kappes, J.C.5    Michael, N.L.6    Polonis, V.R.7    Alving, C.R.8
  • 50
    • 23344454176 scopus 로고    scopus 로고
    • Human dendritic cells and macrophages exhibit different intracellular processing pathways for soluble and liposome-encapsulated antigens
    • Peachman KK, Rao M, Alving CR, Palmer DR, Sun W, Rothwell SW. 2005. Human dendritic cells and macrophages exhibit different intracellular processing pathways for soluble and liposome-encapsulated antigens. Immunobiology 210:321-333. http://dx.doi.org/10.1016/j.imbio.2005.06.002.
    • (2005) Immunobiology , vol.210 , pp. 321-333
    • Peachman, K.K.1    Rao, M.2    Alving, C.R.3    Palmer, D.R.4    Sun, W.5    Rothwell, S.W.6
  • 51
    • 84862954894 scopus 로고    scopus 로고
    • Anthrax vaccine antigen-adjuvant formulations completely protect New Zealand White rabbits against chal-lenge with Bacillus anthracis Ames strain spores
    • Peachman KK, Li Q, Matyas GR, Shivachandra SB, Lovchik J, Lyons RC, Alving CR, Rao VB, Rao M. 2012. Anthrax vaccine antigen-adjuvant formulations completely protect New Zealand White rabbits against chal-lenge with Bacillus anthracis Ames strain spores. Clin Vaccine Immunol 19:11-16. http://dx.doi.org/10.1128/CVI.05376-11.
    • (2012) Clin Vaccine Immunol , vol.19 , pp. 11-16
    • Peachman, K.K.1    Li, Q.2    Matyas, G.R.3    Shivachandra, S.B.4    Lovchik, J.5    Lyons, R.C.6    Alving, C.R.7    Rao, V.B.8    Rao, M.9
  • 52
    • 45849125030 scopus 로고    scopus 로고
    • Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays
    • Chapter 12, Unit 12.11
    • Montefiori DC. 2005. Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays. Curr Protoc Immunol Chapter 12:Unit 12.11. http://dx.doi.org/10.1002/0471142735.im1211s64.
    • (2005) Curr Protoc Immunol
    • Montefiori, D.C.1
  • 55
    • 33845636531 scopus 로고    scopus 로고
    • Effects of N-and C-terminal addition of oligolysines or native loop residues on the biophysical properties of transmembrane domain peptides from a G-protein coupled receptor
    • Cano-Sanchez P, Severino B, Sureshbabu VV, Russo J, Inui T, Ding FX, Arshava B, Becker J, Naider F. 2006. Effects of N-and C-terminal addition of oligolysines or native loop residues on the biophysical properties of transmembrane domain peptides from a G-protein coupled receptor. J Pept Sci 12:808-822. http://dx.doi.org/10.1002/psc.816.
    • (2006) J Pept Sci , vol.12 , pp. 808-822
    • Cano-Sanchez, P.1    Severino, B.2    Sureshbabu, V.V.3    Russo, J.4    Inui, T.5    Ding, F.X.6    Arshava, B.7    Becker, J.8    Naider, F.9
  • 56
    • 0031926765 scopus 로고    scopus 로고
    • Guidelines for membrane protein engineering derived from de novo designed model peptides
    • Liu LP, Deber CM. 1998. Guidelines for membrane protein engineering derived from de novo designed model peptides. Biopolymers 47:41-62. http://dx.doi.org/10.1002/(SICI)1097-0282(1998)47:1<41::AID-BIP6>3.0.CO;2-X.
    • (1998) Biopolymers , vol.47 , pp. 41-62
    • Liu, L.P.1    Deber, C.M.2
  • 60
    • 33746415825 scopus 로고    scopus 로고
    • Insensitivity of paediatric HIV-1 subtype C viruses to broadly neutralising monoclonal antibodies raised against subtype B
    • Gray ES, Meyers T, Gray G, Montefiori DC, Morris L. 2006. Insensitivity of paediatric HIV-1 subtype C viruses to broadly neutralising monoclonal antibodies raised against subtype B. PLoS Med 3:e255. http://dx.doi.org/10.1371/journal.pmed.0030255.
    • (2006) PLoS Med , vol.3
    • Gray, E.S.1    Meyers, T.2    Gray, G.3    Montefiori, D.C.4    Morris, L.5
  • 61
    • 84880816240 scopus 로고    scopus 로고
    • Epitope mapping of conformational V2-specific anti-HIV human monoclonal antibodies reveals an immunodominant site in V2
    • Mayr LM, Cohen S, Spurrier B, Kong XP, Zolla-Pazner S. 2013. Epitope mapping of conformational V2-specific anti-HIV human monoclonal antibodies reveals an immunodominant site in V2. PLoS One 8:e70859. http://dx.doi.org/10.1371/journal.pone.0070859.
    • (2013) PLoS One , vol.8
    • Mayr, L.M.1    Cohen, S.2    Spurrier, B.3    Kong, X.P.4    Zolla-Pazner, S.5
  • 62
    • 84896959968 scopus 로고    scopus 로고
    • Functional implications of the binding mode of a human conformationdependent V2 monoclonal antibody against HIV
    • Spurrier B, Sampson J, Gorny MK, Zolla-Pazner S, Kong XP. 2014. Functional implications of the binding mode of a human conformationdependent V2 monoclonal antibody against HIV. J Virol 88:4100-4112. http://dx.doi.org/10.1128/JVI.03153-13.
    • (2014) J Virol , vol.88 , pp. 4100-4112
    • Spurrier, B.1    Sampson, J.2    Gorny, M.K.3    Zolla-Pazner, S.4    Kong, X.P.5
  • 63
    • 0037470407 scopus 로고    scopus 로고
    • Public health. AIDS vaccine trial produces disappointment and confusion
    • Cohen J. 2003. Public health. AIDS vaccine trial produces disappointment and confusion. Science 299:1290-1291. http://dx.doi.org/10.1126/science.299.5611.1290.
    • (2003) Science , vol.299 , pp. 1290-1291
    • Cohen, J.1
  • 64
    • 13944254982 scopus 로고    scopus 로고
    • Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection
    • Flynn NM, Forthal DN, Harro CD, Judson FN, Mayer KH, Para MF. 2005. Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection. J Infect Dis 191:654-665. http://dx.doi.org/10.1086/428404.
    • (2005) J Infect Dis , vol.191 , pp. 654-665
    • Flynn, N.M.1    Forthal, D.N.2    Harro, C.D.3    Judson, F.N.4    Mayer, K.H.5    Para, M.F.6
  • 66
    • 33845433434 scopus 로고    scopus 로고
    • Randomized, double-blind, placebo-controlled efficacy trial of a bivalent recombinant glycoprotein 120 HIV-1 vaccine among injection drug users in Bangkok, Thailand
    • Pitisuttithum P, Gilbert P, Gurwith M, Heyward W, Martin M, van Griensven F, Hu D, Tappero JW, Choopanya K. 2006. Randomized, double-blind, placebo-controlled efficacy trial of a bivalent recombinant glycoprotein 120 HIV-1 vaccine among injection drug users in Bangkok, Thailand. J Infect Dis 194:1661-1671. http://dx.doi.org/10.1086/508748.
    • (2006) J Infect Dis , vol.194 , pp. 1661-1671
    • Pitisuttithum, P.1    Gilbert, P.2    Gurwith, M.3    Heyward, W.4    Martin, M.5    van Griensven, F.6    Hu, D.7    Tappero, J.W.8    Choopanya, K.9
  • 70
    • 84883187027 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies and the search for an HIV-1 vaccine: the end of the beginning
    • Kwong PD, Mascola JR, Nabel GJ. 2013. Broadly neutralizing antibodies and the search for an HIV-1 vaccine: the end of the beginning. Nat Rev Immunol 13:693-701. http://dx.doi.org/10.1038/nri3516.
    • (2013) Nat Rev Immunol , vol.13 , pp. 693-701
    • Kwong, P.D.1    Mascola, J.R.2    Nabel, G.J.3
  • 73
    • 0026098303 scopus 로고
    • Differential loss of envelope glycoprotein gp120 from virions of human immunodeficiency virus type 1 isolates: effects on infectivity and neutralization
    • McKeating JA, McKnight A, Moore JP. 1991. Differential loss of envelope glycoprotein gp120 from virions of human immunodeficiency virus type 1 isolates: effects on infectivity and neutralization. J Virol 65:852-860.
    • (1991) J Virol , vol.65 , pp. 852-860
    • McKeating, J.A.1    McKnight, A.2    Moore, J.P.3
  • 74
    • 0030023304 scopus 로고    scopus 로고
    • Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation
    • Poignard P, Fouts T, Naniche D, Moore JP, Sattentau QJ. 1996. Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation. J Exp Med 183:473-484. http://dx.doi.org/10.1084/jem.183.2.473.
    • (1996) J Exp Med , vol.183 , pp. 473-484
    • Poignard, P.1    Fouts, T.2    Naniche, D.3    Moore, J.P.4    Sattentau, Q.J.5
  • 75
    • 33947590277 scopus 로고    scopus 로고
    • A comparative immunogenicity study in rabbits of disulfidestabilized, 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, Fisch DC, Ketas T, Yuste E, Desrosiers RC, Klasse PJ, Maddon PJ, Olson WC, Moore JP. 2007. A comparative immunogenicity study in rabbits of disulfidestabilized, proteolytically cleaved, soluble trimeric human immunodeficiency virus type 1 gp140, trimeric cleavage-defective gp140 and monomeric gp120. Virology 360:329-340. http://dx.doi.org/10.1016/j.virol.2006.10.032.
    • (2007) Virology , vol.360 , pp. 329-340
    • Beddows, S.1    Franti, M.2    Dey, A.K.3    Kirschner, M.4    Iyer, S.P.5    Fisch, D.C.6    Ketas, T.7    Yuste, E.8    Desrosiers, R.C.9    Klasse, P.J.10    Maddon, P.J.11    Olson, W.C.12    Moore, J.P.13
  • 77
    • 0034087050 scopus 로고    scopus 로고
    • Characterization of stable, soluble trimers containing complete ectodomains of human immunodeficiency virus type 1 envelope glycoproteins
    • Yang X, Farzan M, Wyatt R, Sodroski J. 2000. Characterization of stable, soluble trimers containing complete ectodomains of human immunodeficiency virus type 1 envelope glycoproteins. J Virol 74:5716-5725. http://dx.doi.org/10.1128/JVI.74.12.5716-5725.2000.
    • (2000) J Virol , vol.74 , pp. 5716-5725
    • Yang, X.1    Farzan, M.2    Wyatt, R.3    Sodroski, J.4
  • 78
    • 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, Lee J, Mahony EM, Kwong PD, Wyatt R, Sodroski J. 2002. Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin. J Virol 76:4634-4642. http://dx.doi.org/10.1128/JVI.76.9.4634-4642.2002.
    • (2002) J Virol , vol.76 , pp. 4634-4642
    • Yang, X.1    Lee, J.2    Mahony, E.M.3    Kwong, P.D.4    Wyatt, R.5    Sodroski, J.6
  • 81
    • 84892457583 scopus 로고    scopus 로고
    • Antigenic properties of the HIV envelope on virions in solution
    • Ray K, Mengistu M, Yu L, Lewis GK, Lakowicz JR, DeVico AL. 2014. Antigenic properties of the HIV envelope on virions in solution. J Virol 88:1795-1808. http://dx.doi.org/10.1128/JVI.03048-13.
    • (2014) J Virol , vol.88 , pp. 1795-1808
    • Ray, K.1    Mengistu, M.2    Yu, L.3    Lewis, G.K.4    Lakowicz, J.R.5    DeVico, A.L.6
  • 82
    • 84901308280 scopus 로고    scopus 로고
    • Immunization of rabbits with highly purified, soluble, trimeric human immunodeficiency virus type 1 envelope glycoprotein induces a vigorous B cell response and broadly cross-reactive neutralization
    • Quinnan GV, Jr, Onabajo O, Zhang P, Yan L, Mattapallil JJ, Zhang Z, Dong M, Lu M, Montefiori D, LaBranche C, Broder CC. 2014. Immunization of rabbits with highly purified, soluble, trimeric human immunodeficiency virus type 1 envelope glycoprotein induces a vigorous B cell response and broadly cross-reactive neutralization. PLoS One 9:e98060. http://dx.doi.org/10.1371/journal.pone.0098060.
    • (2014) PLoS One , vol.9
    • Quinnan, G.V.1    Onabajo, O.2    Zhang, P.3    Yan, L.4    Mattapallil, J.J.5    Zhang, Z.6    Dong, M.7    Lu, M.8    Montefiori, D.9    LaBranche, C.10    Broder, C.C.11
  • 85
    • 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 JP, Burton DR, Ward AB, Wilson IA, Sanders RW, Moore JP, Klasse PJ. 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. http://dx.doi.org/10.1186/1742-4690-11-41.
    • (2014) Retrovirology , vol.11 , pp. 41
    • Yasmeen, A.1    Ringe, R.2    Derking, R.3    Cupo, A.4    Julien, J.P.5    Burton, D.R.6    Ward, A.B.7    Wilson, I.A.8    Sanders, R.W.9    Moore, J.P.10    Klasse, P.J.11
  • 86
    • 84906329923 scopus 로고    scopus 로고
    • Envelope glycoprotein binding to the alpha4beta7 integrin complex is not a general property of most HIV-1 variants
    • Perez LG, Chen H, Liao H-X, Montefiori DC. 2014. Envelope glycoprotein binding to the alpha4beta7 integrin complex is not a general property of most HIV-1 variants. J Virol 88:10767-10777. http://dx.doi.org/10.1128/JVI.03296-13.
    • (2014) J Virol , vol.88 , pp. 10767-10777
    • Perez, L.G.1    Chen, H.2    Liao, H.-X.3    Montefiori, D.C.4
  • 90
    • 33744916994 scopus 로고    scopus 로고
    • Nonneutralizing antibodies are able to inhibit human immunodeficiency virus type 1 replication in macrophages and immature dendritic cells
    • Holl V, Peressin M, Decoville T, Schmidt S, Zolla-Pazner S, Aubertin AM, Moog C. 2006. Nonneutralizing antibodies are able to inhibit human immunodeficiency virus type 1 replication in macrophages and immature dendritic cells. J Virol 80:6177-6181. http://dx.doi.org/10.1128/JVI.02625-05.
    • (2006) J Virol , vol.80 , pp. 6177-6181
    • Holl, V.1    Peressin, M.2    Decoville, T.3    Schmidt, S.4    Zolla-Pazner, S.5    Aubertin, A.M.6    Moog, C.7


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