메뉴 건너뛰기




Volumn 88, Issue 8, 2014, Pages 4100-4112

Functional implications of the binding mode of a human conformation-dependent V2 monoclonal antibody against HIV

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA4BETA7 INTEGRIN; EPITOPE; INTEGRIN; ISOLEUCINE; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG; V2 MONOCLONAL ANTIBODY;

EID: 84896959968     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03153-13     Document Type: Article
Times cited : (37)

References (55)
  • 4
    • 0032169683 scopus 로고    scopus 로고
    • Effect of major deletions in the V1 and V2 loops of a macrophage-tropic HIV type 1 isolate on viral envelope structure, cell entry, and replication
    • Stamatatos L, Wiskerchen M, Cheng-Mayer C. 1998. Effect of major deletions in the V1 and V2 loops of a macrophage-tropic HIV type 1 isolate on viral envelope structure, cell entry, and replication. AIDS 14: 1129-1139.
    • (1998) AIDS , vol.14 , pp. 1129-1139
    • Stamatatos, L.1    Wiskerchen, M.2    Cheng-Mayer, C.3
  • 5
    • 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
  • 6
    • 0031023939 scopus 로고    scopus 로고
    • Prevalence of a V2 epitope in clade B primary isolates and its recognition by sera from HIV-1-infected individuals
    • Israel ZR, Gorny MK, Palmer C, McKeating JA, Zolla-Pazner S. 1997. Prevalence of a V2 epitope in clade B primary isolates and its recognition by sera from HIV-1-infected individuals. AIDS 11:128-130.
    • (1997) AIDS , vol.11 , pp. 128-130
    • Israel, Z.R.1    Gorny, M.K.2    Palmer, C.3    McKeating, J.A.4    Zolla-Pazner, S.5
  • 8
    • 77954100808 scopus 로고    scopus 로고
    • Structure-function relationships of HIV-1 envelope sequence-variable regions refocus vaccine design
    • Zolla-Pazner S, Cardozo T. 2010. Structure-function relationships of HIV-1 envelope sequence-variable regions refocus vaccine design. Nat. Rev. Immunol. 10:527-535. http://dx.doi.org/10.1038/nri2801.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 527-535
    • Zolla-Pazner, S.1    Cardozo, T.2
  • 10
    • 38949186531 scopus 로고    scopus 로고
    • Roles of HIV-1 Env variable regions in viral neutralization and vaccine development
    • Pinter A. 2007. Roles of HIV-1 Env variable regions in viral neutralization and vaccine development. Curr. HIV Res. 5:542-553. http://dx.doi.org/10.2174/157016207782418470.
    • (2007) Curr. HIV Res. , vol.5 , pp. 542-553
    • Pinter, A.1
  • 12
    • 25844482131 scopus 로고    scopus 로고
    • Perils at mucosal front lines for HIV and SIV and their hosts
    • Haase AT. 2005. Perils at mucosal front lines for HIV and SIV and their hosts. Nat. Rev. Immunol. 5:783-792. http://dx.doi.org/10.1038/nri1706.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 783-792
    • Haase, A.T.1
  • 15
    • 84862173040 scopus 로고    scopus 로고
    • Monoclonal antibodies to the V2 domain of MN-rgp120: fine mapping of epitopes and inhibition of alpha4beta7 binding
    • Nakamura GR, Fonseca DP, O'Rourke SM, Vollrath AL, Berman PW. 2012. Monoclonal antibodies to the V2 domain of MN-rgp120: fine mapping of epitopes and inhibition of alpha4beta7 binding. PLoS One 7:e39045. http://dx.doi.org/10.1371/journal.pone.0039045.
    • (2012) PLoS One , vol.7
    • Nakamura, G.R.1    Fonseca, D.P.2    O'Rourke, S.M.3    Vollrath, A.L.4    Berman, P.W.5
  • 16
    • 84865981605 scopus 로고    scopus 로고
    • A DNA-based candidate HIV vaccine delivered via in vivo electroporation induces CD4 responses toward the alpha4beta7-binding V2 loop of HIV gp120 in healthy volunteers
    • Kopycinski J, Cheeseman H, Ashraf A, Gill D, Hayes P, Hannaman D, Gilmour J, Cox JH, Vasan S. 2012. A DNA-based candidate HIV vaccine delivered via in vivo electroporation induces CD4 responses toward the alpha4beta7-binding V2 loop of HIV gp120 in healthy volunteers. Clin. Vaccine Immunol. 19:1557-1559. http://dx.doi.org/10.1128/CVI.00327-12.
    • (2012) Clin. Vaccine Immunol. , vol.19 , pp. 1557-1559
    • Kopycinski, J.1    Cheeseman, H.2    Ashraf, A.3    Gill, D.4    Hayes, P.5    Hannaman, D.6    Gilmour, J.7    Cox, J.H.8    Vasan, S.9
  • 17
    • 79251555316 scopus 로고    scopus 로고
    • Blocking of alpha4beta7 gut-homing integrin during acute infection leads to decreased plasma and gastrointestinal tissue viral loads in simian immunodeficiency virus-infected rhesus macaques
    • Ansari AA, Reimann KA, Mayne AE, Takahashi Y, Stephenson ST, Wang R, Wang X, Li J, Price AA, Little DM, Zaidi M, Lyles R, Villinger F. 2011. Blocking of alpha4beta7 gut-homing integrin during acute infection leads to decreased plasma and gastrointestinal tissue viral loads in simian immunodeficiency virus-infected rhesus macaques. J. Immunol. 186:1044-1059. http://dx.doi.org/10.4049/jimmunol.1003052.
    • (2011) J. Immunol. , vol.186 , pp. 1044-1059
    • Ansari, A.A.1    Reimann, K.A.2    Mayne, A.E.3    Takahashi, Y.4    Stephenson, S.T.5    Wang, R.6    Wang, X.7    Li, J.8    Price, A.A.9    Little, D.M.10    Zaidi, M.11    Lyles, R.12    Villinger, F.13
  • 18
    • 51349162563 scopus 로고    scopus 로고
    • Molecular architecture of native HIV-1 gp120 trimers
    • Liu J, Bartesaghi A, Borgnia MJ, Sapiro G, Subramaniam S. 2008. Molecular architecture of native HIV-1 gp120 trimers. Nature 455:109-113. http://dx.doi.org/10.1038/nature07159.
    • (2008) Nature , vol.455 , pp. 109-113
    • Liu, J.1    Bartesaghi, A.2    Borgnia, M.J.3    Sapiro, G.4    Subramaniam, S.5
  • 26
    • 16244419386 scopus 로고    scopus 로고
    • Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles
    • Gorny MK, Stamatatos L, Volsky B, Revesz K, Williams C, Wang XH, Cohen S, Staudinger R, Zolla-Pazner S. 2005. Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles. J. Virol. 79:5232-5237. http://dx.doi.org/10.1128/JVI.79.8.5232-5237.2005.
    • (2005) J. Virol. , vol.79 , pp. 5232-5237
    • Gorny, M.K.1    Stamatatos, L.2    Volsky, B.3    Revesz, K.4    Williams, C.5    Wang, X.H.6    Cohen, S.7    Staudinger, R.8    Zolla-Pazner, S.9
  • 33
    • 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
  • 35
    • 0026356679 scopus 로고
    • Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the human immunodeficiency virus type 1 envelope glycoprotein
    • Gorny MK, Xu JY, Gianakakos V, Karwowska S, Williams C, Sheppard HW, Hanson CV, Zolla-Pazner S. 1991. Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the human immunodeficiency virus type 1 envelope glycoprotein. Proc. Natl. Acad. Sci. U. S. A. 88:3238-3242. http://dx.doi.org/10.1073/pnas.88.8.3238.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 3238-3242
    • Gorny, M.K.1    Xu, J.Y.2    Gianakakos, V.3    Karwowska, S.4    Williams, C.5    Sheppard, H.W.6    Hanson, C.V.7    Zolla-Pazner, S.8
  • 36
    • 0021041087 scopus 로고
    • Construction and testing of mouse-human heteromyelomas for human monoclonal antibody production
    • Teng NN, Lam KS, Calvo Riera F, Kaplan HS. 1983. Construction and testing of mouse-human heteromyelomas for human monoclonal antibody production. Proc. Natl. Acad. Sci. U. S. A. 80:7308-7312. http://dx.doi.org/10.1073/pnas.80.23.7308.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 7308-7312
    • Teng, N.N.1    Lam, K.S.2    Calvo Riera, F.3    Kaplan, H.S.4
  • 38
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus PA, Diederichs K. 2012. Linking crystallographic model and data quality. Science 336:1030-1033. http://dx.doi.org/10.1126/science.121 8231.
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 42
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60:2126-2132. http://dx.doi.org/10.1107/S0907444904019158.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 43
    • 0036149480 scopus 로고    scopus 로고
    • Soft protein-protein docking in internal coordinates
    • Fernandez-Recio J, Totrov M, Abagyan R. 2002. Soft protein-protein docking in internal coordinates. Protein Sci. 11:280-291. http://dx.doi.org/10.1110/ps.19202.
    • (2002) Protein Sci. , vol.11 , pp. 280-291
    • Fernandez-Recio, J.1    Totrov, M.2    Abagyan, R.3
  • 44
    • 21044444449 scopus 로고    scopus 로고
    • Pocketome via comprehensive identification and classification of ligand binding envelopes
    • An J, Totrov M, Abagyan R. 2005. Pocketome via comprehensive identification and classification of ligand binding envelopes. Mol. Cell. Proteomics 4:752-761. http://dx.doi.org/10.1074/mcp. M400159-MCP200.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 752-761
    • An, J.1    Totrov, M.2    Abagyan, R.3
  • 46
    • 79551470095 scopus 로고    scopus 로고
    • Role of conformational sampling in computing mutation-induced changes in protein structure and stability
    • Kellogg EH, Leaver-Fay A, Baker D. 2011. Role of conformational sampling in computing mutation-induced changes in protein structure and stability. Proteins 79:830-838. http://dx.doi.org/10.1002/prot.22921.
    • (2011) Proteins , vol.79 , pp. 830-838
    • Kellogg, E.H.1    Leaver-Fay, A.2    Baker, D.3
  • 47
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible Nacetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, Khorana HG. 2002. Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible Nacetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl. Acad. Sci. U. S. A. 99:13419-13424. http://dx.doi.org/10.1073/pnas.212519299.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 48
    • 0025823716 scopus 로고
    • Identical V region amino acid sequences and segments of sequences in antibodies of different specificities. Relative contributions of VH and VL genes, minigenes, and complementaritydetermining regions to binding of antibody-combining sites
    • Kabat EA, Wu TT. 1991. Identical V region amino acid sequences and segments of sequences in antibodies of different specificities. Relative contributions of VH and VL genes, minigenes, and complementaritydetermining regions to binding of antibody-combining sites. J. Immunol. 147:1709-1719.
    • (1991) J. Immunol. , vol.147 , pp. 1709-1719
    • Kabat, E.A.1    Wu, T.T.2
  • 49
    • 77954982131 scopus 로고    scopus 로고
    • Crystal structure of PG16 and chimeric dissection with somatically related PG9: structurefunction analysis of two quaternary-specific antibodies that effectively neutralize HIV-1
    • Pancera M, McLellan JS, Wu X, Zhu J, Changela A, Schmidt SD, Yang Y, Zhou T, Phogat S, Mascola JR, Kwong PD. 2010. Crystal structure of PG16 and chimeric dissection with somatically related PG9: structurefunction analysis of two quaternary-specific antibodies that effectively neutralize HIV-1. J. Virol. 84:8098-8110. http://dx.doi.org/10.1128/JVI.00966-10.
    • (2010) J. Virol. , vol.84 , pp. 8098-8110
    • Pancera, M.1    McLellan, J.S.2    Wu, X.3    Zhu, J.4    Changela, A.5    Schmidt, S.D.6    Yang, Y.7    Zhou, T.8    Phogat, S.9    Mascola, J.R.10    Kwong, P.D.11
  • 51
    • 79955855015 scopus 로고    scopus 로고
    • Structural analysis of human and macaque mAbs 2909 and 2.5B: implications for the configuration of the quaternary neutralizing epitope of HIV-1 gp120
    • Spurrier B, Sampson JM, Totrov M, Li H, O'Neal T, Williams C, Robinson J, Gorny MK, Zolla-Pazner S, Kong XP. 2011. Structural analysis of human and macaque mAbs 2909 and 2.5B: implications for the configuration of the quaternary neutralizing epitope of HIV-1 gp120. Structure 19:691-699. http://dx.doi.org/10.1016/j.str.2011.02.012.
    • (2011) Structure , vol.19 , pp. 691-699
    • Spurrier, B.1    Sampson, J.M.2    Totrov, M.3    Li, H.4    O'Neal, T.5    Williams, C.6    Robinson, J.7    Gorny, M.K.8    Zolla-Pazner, S.9    Kong, X.P.10
  • 52
    • 36049029967 scopus 로고    scopus 로고
    • High-resolution structure prediction and the crystallographic phase problem
    • Qian B, Raman S, Das R, Bradley P, McCoy AJ, Read RJ, Baker D. 2007. High-resolution structure prediction and the crystallographic phase problem. Nature 450:259-264. http://dx.doi.org/10.1038/nature06249.
    • (2007) Nature , vol.450 , pp. 259-264
    • Qian, B.1    Raman, S.2    Das, R.3    Bradley, P.4    McCoy, A.J.5    Read, R.J.6    Baker, D.7
  • 53
    • 34548861782 scopus 로고    scopus 로고
    • Protein-protein docking with backbone flexibility
    • Wang C, Bradley P, Baker D. 2007. Protein-protein docking with backbone flexibility. J. Mol. Biol. 373:503-519. http://dx.doi.org/10.1016/j.jmb.2007.07.050.
    • (2007) J. Mol. Biol. , vol.373 , pp. 503-519
    • Wang, C.1    Bradley, P.2    Baker, D.3
  • 54
    • 84863012638 scopus 로고    scopus 로고
    • Structural specializations of alpha(4)beta(7), an integrin that mediates rolling adhesion
    • Yu Y, Zhu J, Mi LZ, Walz T, Sun H, Chen J, Springer TA. 2012. Structural specializations of alpha(4)beta(7), an integrin that mediates rolling adhesion. J. Cell Biol. 196:131-146. http://dx.doi.org/10.1083/jcb.201110023.
    • (2012) J. Cell Biol. , vol.196 , pp. 131-146
    • Yu, Y.1    Zhu, J.2    Mi, L.Z.3    Walz, T.4    Sun, H.5    Chen, J.6    Springer, T.A.7
  • 55
    • 84883500332 scopus 로고    scopus 로고
    • Blocking of integrins inhibits HIV-1 infection of human cervical mucosa immune cells with free and complement-opsonized virions
    • Tjomsland V, Ellegard R, Kjolhede P, Wodlin NB, Hinkula J, Lifson JD, Larsson M. 2013. Blocking of integrins inhibits HIV-1 infection of human cervical mucosa immune cells with free and complement-opsonized virions. Eur. J. Immunol. 43:2361-2372. http://dx.doi.org/10.1002/eji.20124 3257.
    • (2013) Eur. J. Immunol. , vol.43 , pp. 2361-2372
    • Tjomsland, V.1    Ellegard, R.2    Kjolhede, P.3    Wodlin, N.B.4    Hinkula, J.5    Lifson, J.D.6    Larsson, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.