메뉴 건너뛰기




Volumn 8, Issue 4, 2013, Pages

Chimeric HIV-1 Envelope Glycoproteins with Potent Intrinsic Granulocyte-Macrophage Colony-Stimulating Factor (GM-CSF) Activity*

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 140; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR;

EID: 84875674153     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0060126     Document Type: Article
Times cited : (7)

References (63)
  • 1
    • 84859393693 scopus 로고    scopus 로고
    • Immune-correlates analysis of an HIV-1 vaccine efficacy trial
    • 101056/NEJMoa1113425 [doi]
    • Haynes BF, Gilbert PB, McElrath MJ, Zolla-Pazner S, Tomaras GD, et al. (2012) Immune-correlates analysis of an HIV-1 vaccine efficacy trial. N Engl J Med 366: 1275-1286 101056/NEJMoa1113425 [doi].
    • (2012) N Engl J Med , vol.366 , pp. 1275-1286
    • Haynes, B.F.1    Gilbert, P.B.2    McElrath, M.J.3    Zolla-Pazner, S.4    Tomaras, G.D.5
  • 2
    • 0035000679 scopus 로고    scopus 로고
    • The ability of an oligomeric human immunodeficiency virus type 1 (HIV-1) envelope antigen to elicit neutralizing antibodies against primary HIV-1 isolates is improved following partial deletion of the second hypervariable region
    • 101128/JVI.75.12.5526-5540.2001 [doi]
    • Barnett SW, Lu S, Srivastava I, Cherpelis S, Gettie A, et al. (2001) The ability of an oligomeric human immunodeficiency virus type 1 (HIV-1) envelope antigen to elicit neutralizing antibodies against primary HIV-1 isolates is improved following partial deletion of the second hypervariable region. J Virol 75: 5526-5540 101128/JVI.75.12.5526-5540.2001 [doi].
    • (2001) J Virol , vol.75 , pp. 5526-5540
    • Barnett, S.W.1    Lu, S.2    Srivastava, I.3    Cherpelis, S.4    Gettie, A.5
  • 3
    • 78449241664 scopus 로고    scopus 로고
    • Stabilized HIV-1 envelope glycoprotein trimers lacking the V1V2 domain, obtained by virus evolution
    • M110.156588 [pii];10.1074/jbc.M110.156588 [doi]
    • Bontjer I, Melchers M, Eggink D, David K, Moore JP, et al. (2010) Stabilized HIV-1 envelope glycoprotein trimers lacking the V1V2 domain, obtained by virus evolution. J Biol Chem 285: 36456-36470. M110.156588 [pii];10.1074/jbc.M110.156588 [doi].
    • (2010) J Biol Chem , vol.285 , pp. 36456-36470
    • Bontjer, I.1    Melchers, M.2    Eggink, D.3    David, K.4    Moore, J.P.5
  • 4
    • 1542317452 scopus 로고    scopus 로고
    • HIV vaccine design and the neutralizing antibody problem
    • 101038/ni0304-233 [doi];ni0304-233 [pii]
    • Burton DR, Desrosiers RC, Doms RW, Koff WC, et al. (2004) HIV vaccine design and the neutralizing antibody problem. Nat Immunol 5: 233-236 101038/ni0304-233 [doi];ni0304-233 [pii].
    • (2004) Nat Immunol , vol.5 , pp. 233-236
    • Burton, D.R.1    Desrosiers, R.C.2    Doms, R.W.3    Koff, W.C.4
  • 5
    • 0030812563 scopus 로고    scopus 로고
    • Replication and neutralization of human immunodeficiency virus type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein
    • Cao J, Sullivan N, Desjardin E, Parolin C, Robinson J, et al. (1997) Replication and neutralization of human immunodeficiency virus type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein. J Virol 71: 9808-9812.
    • (1997) J Virol , vol.71 , pp. 9808-9812
    • Cao, J.1    Sullivan, N.2    Desjardin, E.3    Parolin, C.4    Robinson, J.5
  • 6
    • 65749107719 scopus 로고    scopus 로고
    • HIV-1 and influenza antibodies: Seeing antigens in new ways
    • ni.1746 [pii];10.1038/ni.1746 [doi]
    • Kwong PD, Wilson IA (2009) HIV-1 and influenza antibodies: seeing antigens in new ways. Nat Immunol 10: 573-578. ni.1746 [pii];10.1038/ni.1746 [doi].
    • (2009) Nat Immunol , vol.10 , pp. 573-578
    • Kwong, P.D.1    Wilson, I.A.2
  • 7
    • 0037321708 scopus 로고    scopus 로고
    • Changes in the immunogenic properties of soluble gp140 human immunodeficiency virus envelope constructs upon partial deletion of the second hypervariable region
    • Srivastava IK, VanDorsten K, Vojtech L, Barnett SW, Stamatatos L, (2003) Changes in the immunogenic properties of soluble gp140 human immunodeficiency virus envelope constructs upon partial deletion of the second hypervariable region. J Virol 77: 2310-2320.
    • (2003) J Virol , vol.77 , pp. 2310-2320
    • Srivastava, I.K.1    Vandorsten, K.2    Vojtech, L.3    Barnett, S.W.4    Stamatatos, L.5
  • 8
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • nature10696 [pii];10.1038/nature10696 [doi]
    • McLellan JS, Pancera M, Carrico C, Gorman J, Julien JP, et al. (2011) Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 480: 336-343. nature10696 [pii];10.1038/nature10696 [doi].
    • (2011) Nature , vol.480 , pp. 336-343
    • McLellan, J.S.1    Pancera, M.2    Carrico, C.3    Gorman, J.4    Julien, J.P.5
  • 9
    • 82255179322 scopus 로고    scopus 로고
    • A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield
    • science.1213256 [pii];10.1126/science.1213256 [doi]
    • Pejchal R, Doores KJ, Walker LM, Khayat R, Huang PS, et al. (2011) A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield. Science 334: 1097-1103. science.1213256 [pii];10.1126/science.1213256 [doi].
    • (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
  • 10
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • Sanders RW, Venturi M, Schiffner L, Kalyanaraman R, Katinger H, et al. (2002) The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J Virol 76: 7293-7305.
    • (2002) J Virol , vol.76 , pp. 7293-7305
    • Sanders, R.W.1    Venturi, M.2    Schiffner, L.3    Kalyanaraman, R.4    Katinger, H.5
  • 11
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1->2 mannose residues on the outer face of gp120
    • Scanlan CN, Pantophlet R, Wormald MR, Ollmann SE, Stanfield R, et al. (2002) The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1->2 mannose residues on the outer face of gp120. J Virol 76: 7306-7321.
    • (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
  • 12
    • 84863393535 scopus 로고    scopus 로고
    • Occluding the mannose moieties on human immunodeficiency virus type 1 gp120 with griffithsin improves the antibody responses to both proteins in mice
    • 101089/aid.2011.0101 [doi]
    • Banerjee K, Michael E, Eggink D, van Montfort T, Lasnik AB, et al. (2012) Occluding the mannose moieties on human immunodeficiency virus type 1 gp120 with griffithsin improves the antibody responses to both proteins in mice. AIDS Res Hum Retroviruses 28: 206-214 101089/aid.2011.0101 [doi].
    • (2012) AIDS Res Hum Retroviruses , vol.28 , pp. 206-214
    • Banerjee, K.1    Michael, E.2    Eggink, D.3    van Montfort, T.4    Lasnik, A.B.5
  • 13
    • 84869795022 scopus 로고    scopus 로고
    • HIV-1 gp120 Impairs the Induction of B Cell Responses by TLR9-Activated Plasmacytoid Dendritic Cells
    • jimmunol.1201905 [pii];10.4049/jimmunol.1201905 [doi]
    • Chung NP, Matthews K, Klasse PJ, Sanders RW, Moore JP (2012) HIV-1 gp120 Impairs the Induction of B Cell Responses by TLR9-Activated Plasmacytoid Dendritic Cells. J Immunol. jimmunol.1201905 [pii];10.4049/jimmunol.1201905 [doi].
    • (2012) J Immunol
    • Chung, N.P.1    Matthews, K.2    Klasse, P.J.3    Sanders, R.W.4    Moore, J.P.5
  • 14
    • 82455192354 scopus 로고    scopus 로고
    • Improving immunogenicity of HIV-1 envelope gp120 by glycan removal and immune complex formation
    • S0264-410X(11)01464-2 [pii];10.1016/j.vaccine.2011.09.057 [doi]
    • Kumar R, Tuen M, Li H, Tse DB, Hioe CE (2011) Improving immunogenicity of HIV-1 envelope gp120 by glycan removal and immune complex formation. Vaccine 29: 9064-9074. S0264-410X(11)01464-2 [pii];10.1016/j.vaccine.2011.09.057 [doi].
    • (2011) Vaccine , vol.29 , pp. 9064-9074
    • Kumar, R.1    Tuen, M.2    Li, H.3    Tse, D.B.4    Hioe, C.E.5
  • 15
    • 33847617830 scopus 로고    scopus 로고
    • HIV-1 gp120 inhibits TLR9-mediated activation and IFN-{alpha} secretion in plasmacytoid dendritic cells
    • 0611353104 [pii];10.1073/pnas.0611353104 [doi]
    • Martinelli E, Cicala C, Van RD, Goode DJ, Macleod K, et al. (2007) HIV-1 gp120 inhibits TLR9-mediated activation and IFN-{alpha} secretion in plasmacytoid dendritic cells. Proc Natl Acad Sci U S A 104: 3396-3401 0611353104 [pii];10.1073/pnas.0611353104 [doi].
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 3396-3401
    • Martinelli, E.1    Cicala, C.2    Van, R.D.3    Goode, D.J.4    Macleod, K.5
  • 16
    • 33144486096 scopus 로고    scopus 로고
    • Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1
    • 805/2515 [pii];10.1128/JVI.80.5.2515-2528.2006 [doi]
    • 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 805/2515 [pii];10.1128/JVI.80.5.2515-2528.2006 [doi].
    • (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
  • 17
    • 37349066496 scopus 로고    scopus 로고
    • HIV-1 gp120 mannoses induce immunosuppressive responses from dendritic cells
    • 07PLPA-RA-0438 [pii];10.1371/journal.ppat.0030169 [doi]
    • Shan M, Klasse PJ, Banerjee K, Dey AK, Iyer SP, et al. (2007) HIV-1 gp120 mannoses induce immunosuppressive responses from dendritic cells. PLoS Pathog 3: e169 07PLPA-RA-0438 [pii];10.1371/journal.ppat.0030169 [doi].
    • (2007) PLoS Pathog , vol.3
    • Shan, M.1    Klasse, P.J.2    Banerjee, K.3    Dey, A.K.4    Iyer, S.P.5
  • 19
    • 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.
    • (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
  • 20
    • 60349105588 scopus 로고    scopus 로고
    • Biochemical and biophysical comparison of cleaved and uncleaved soluble, trimeric HIV-1 envelope glycoproteins
    • S0042-6822(08)00802-7 [pii];10.1016/j.virol.2008.12.009 [doi]
    • Dey AK, David KB, Lu M, Moore JP (2009) Biochemical and biophysical comparison of cleaved and uncleaved soluble, trimeric HIV-1 envelope glycoproteins. Virology 385: 275-281. S0042-6822(08)00802-7 [pii];10.1016/j.virol.2008.12.009 [doi].
    • (2009) Virology , vol.385 , pp. 275-281
    • Dey, A.K.1    David, K.B.2    Lu, M.3    Moore, J.P.4
  • 21
    • 12344264596 scopus 로고    scopus 로고
    • Selective Recognition of Oligomeric HIV-1 Primary Isolate Envelope Glycoproteins By Potently Neutralizing Ligands Requires Efficient Precursor Cleavage
    • S0042-6822(04)00727-5 [pii];10.1016/j.virol.2004.10.042 [doi]
    • Pancera M, Wyatt R (2005) Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage. Virology 332: 145-156. S0042-6822(04)00727-5 [pii];10.1016/j.virol.2004.10.042 [doi].
    • (2005) Virology , vol.332 , pp. 145-156
    • Pancera, M.1    Wyatt, R.2
  • 22
    • 0037348281 scopus 로고    scopus 로고
    • Effects of HIV type 1 envelope glycoprotein proteolytic processing on antigenicity
    • 101089/088922203763315722 [doi]
    • Si Z, Phan N, Kiprilov E, Sodroski J (2003) Effects of HIV type 1 envelope glycoprotein proteolytic processing on antigenicity. AIDS Res Hum Retroviruses 19: 217-226 101089/088922203763315722 [doi].
    • (2003) AIDS Res Hum Retroviruses , vol.19 , pp. 217-226
    • Si, Z.1    Phan, N.2    Kiprilov, E.3    Sodroski, J.4
  • 23
    • 79959360925 scopus 로고    scopus 로고
    • A chimeric HIV-1 envelope glycoprotein trimer with an embedded granulocyte-macrophage colony-stimulating factor (GM-CSF) domain induces enhanced antibody and T cell responses
    • M111.229625 [pii];10.1074/jbc.M111.229625 [doi]
    • van Montfort T, Melchers M, Isik G, Menis S, Huang PS, et al. (2011) A chimeric HIV-1 envelope glycoprotein trimer with an embedded granulocyte-macrophage colony-stimulating factor (GM-CSF) domain induces enhanced antibody and T cell responses. J Biol Chem 286: 22250-22261. M111.229625 [pii];10.1074/jbc.M111.229625 [doi].
    • (2011) J Biol Chem , vol.286 , pp. 22250-22261
    • van Montfort, T.1    Melchers, M.2    Isik, G.3    Menis, S.4    Huang, P.S.5
  • 24
    • 0027738701 scopus 로고
    • Upregulation of lineage specific receptors and ligands in multipotential progenitor cells is part of an endogenous program of differentiation
    • Just U, Friel J, Heberlein C, Tamura T, Baccarini M, et al. (1993) Upregulation of lineage specific receptors and ligands in multipotential progenitor cells is part of an endogenous program of differentiation. Growth Factors 9: 291-300.
    • (1993) Growth Factors , vol.9 , pp. 291-300
    • Just, U.1    Friel, J.2    Heberlein, C.3    Tamura, T.4    Baccarini, M.5
  • 25
    • 0031238838 scopus 로고    scopus 로고
    • Differential role of calcium in tumour necrosis factor-mediated apoptosis and secretion of granulocyte-macrophage colony-stimulating factor in a T cell hybridoma
    • S1043-4666(97)90218-0 [pii];10.1006/cyto.1997.0218 [doi]
    • Denecker G, Vandenabeele P, Grooten J, Penning LC, Declercq W, et al. (1997) Differential role of calcium in tumour necrosis factor-mediated apoptosis and secretion of granulocyte-macrophage colony-stimulating factor in a T cell hybridoma. Cytokine 9: 631-638. S1043-4666(97)90218-0 [pii];10.1006/cyto.1997.0218 [doi].
    • (1997) Cytokine , vol.9 , pp. 631-638
    • Denecker, G.1    Vandenabeele, P.2    Grooten, J.3    Penning, L.C.4    Declercq, W.5
  • 26
    • 0020039959 scopus 로고
    • A study of added GM-CSF independent granulocyte and macrophage precursors in mouse spleen infected with myeloproliferative sarcoma virus (MPSV)
    • Klein B, Le Bousse-Kerdiles C, Smadja-Joffe F, Pragnell I, Ostertag W, et al. (1982) A study of added GM-CSF independent granulocyte and macrophage precursors in mouse spleen infected with myeloproliferative sarcoma virus (MPSV). Exp Hematol 10: 373-382.
    • (1982) Exp Hematol , vol.10 , pp. 373-382
    • Klein, B.1    Le Bousse-Kerdiles, C.2    Smadja-Joffe, F.3    Pragnell, I.4    Ostertag, W.5
  • 27
    • 0033028635 scopus 로고    scopus 로고
    • Granulocyte-macrophage colony-stimulating factor: Potential therapeutic, immunological and antiretroviral effects in HIV infection
    • Deresinski SC, (1999) Granulocyte-macrophage colony-stimulating factor: potential therapeutic, immunological and antiretroviral effects in HIV infection. AIDS 13: 633-643.
    • (1999) AIDS , vol.13 , pp. 633-643
    • Deresinski, S.C.1
  • 28
    • 77954666119 scopus 로고    scopus 로고
    • Systematic Cytokine Receptor Profiling Reveals GM-CSF As a Novel TLR-independent Activator of Human Plasmacytoid Predendritic Cells
    • blood-2010-01-266932 [pii];10.1182/blood-2010-01-266932 [doi]
    • Ghirelli C, Zollinger R, Soumelis V (2010) Systematic cytokine receptor profiling reveals GM-CSF as a novel TLR-independent activator of human plasmacytoid predendritic cells. Blood 115: 5037-5040. blood-2010-01-266932 [pii];10.1182/blood-2010-01-266932 [doi].
    • (2010) Blood , vol.115 , pp. 5037-5040
    • Ghirelli, C.1    Zollinger, R.2    Soumelis, V.3
  • 30
    • 57349153146 scopus 로고    scopus 로고
    • Only five of 10 strictly conserved disulfide bonds are essential for folding and eight for function of the HIV-1 envelope glycoprotein
    • E07-12-1282 [pii];10.1091/mbc.E07-12-1282 [doi]
    • van Anken E, Sanders RW, Liscaljet IM, Land A, Bontjer I, et al. (2008) Only five of 10 strictly conserved disulfide bonds are essential for folding and eight for function of the HIV-1 envelope glycoprotein. Mol Biol Cell 19: 4298-4309. E07-12-1282 [pii];10.1091/mbc.E07-12-1282 [doi].
    • (2008) Mol Biol Cell , vol.19 , pp. 4298-4309
    • van Anken, E.1    Sanders, R.W.2    Liscaljet, I.M.3    Land, A.4    Bontjer, I.5
  • 31
    • 0025264198 scopus 로고
    • Granulocyte-macrophage colony stimulating factor from human lymphocytes. The effect of glycosylation on receptor binding and biological activity
    • Cebon J, Nicola N, Ward M, Gardner I, Dempsey P, et al. (1990) Granulocyte-macrophage colony stimulating factor from human lymphocytes. The effect of glycosylation on receptor binding and biological activity. J Biol Chem 265: 4483-4491.
    • (1990) J Biol Chem , vol.265 , pp. 4483-4491
    • Cebon, J.1    Nicola, N.2    Ward, M.3    Gardner, I.4    Dempsey, P.5
  • 32
    • 0036184790 scopus 로고    scopus 로고
    • Enhancing the proteolytic maturation of human immunodeficiency virus type 1 envelope glycoproteins
    • Binley JM, Sanders RW, Master A, Cayanan CS, Wiley CL, et al. (2002) Enhancing the proteolytic maturation of human immunodeficiency virus type 1 envelope glycoproteins. J Virol 76: 2606-2616.
    • (2002) J Virol , vol.76 , pp. 2606-2616
    • Binley, J.M.1    Sanders, R.W.2    Master, A.3    Cayanan, C.S.4    Wiley, C.L.5
  • 33
    • 79958086672 scopus 로고    scopus 로고
    • Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected
    • JVI.00154-11 [pii];10.1128/JVI.00154-11 [doi]
    • 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. J Virol 85: 5825-5839. JVI.00154-11 [pii];10.1128/JVI.00154-11 [doi].
    • (2011) J Virol , vol.85 , pp. 5825-5839
    • Crooks, E.T.1    Tong, T.2    Osawa, K.3    Binley, J.M.4
  • 34
    • 0031027984 scopus 로고    scopus 로고
    • Antibodies against HIV-1 from phage display libraries: Mapping of an immune response and progress towards antiviral immunotherapy
    • Parren PW, Burton DR, (1997) Antibodies against HIV-1 from phage display libraries: mapping of an immune response and progress towards antiviral immunotherapy. Chem Immunol 65: 18-56.
    • (1997) Chem Immunol , vol.65 , pp. 18-56
    • Parren, P.W.1    Burton, D.R.2
  • 35
    • 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.
    • (2002) J Virol , vol.76 , pp. 8875-8889
    • Sanders, R.W.1    Vesanen, M.2    Schuelke, N.3    Master, A.4    Schiffner, L.5
  • 36
    • 77951988965 scopus 로고    scopus 로고
    • Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function
    • S0042-6822(10)00128-5 [pii];10.1016/j.virol.2010.02.019 [doi]
    • Eggink D, Melchers M, Wuhrer M, van Montfort T, Dey AK, et al. (2010) Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function. Virology 401: 236-247. S0042-6822(10)00128-5 [pii];10.1016/j.virol.2010.02.019 [doi].
    • (2010) Virology , vol.401 , pp. 236-247
    • Eggink, D.1    Melchers, M.2    Wuhrer, M.3    van Montfort, T.4    Dey, A.K.5
  • 37
    • 79959217462 scopus 로고    scopus 로고
    • A stabilized HIV-1 envelope glycoprotein trimer fused to CD40 ligand targets and activates dendritic cells
    • In press
    • Melchers M, Matthews K, de Vries RP, Eggink D, van Montfort T, et al. (2011) A stabilized HIV-1 envelope glycoprotein trimer fused to CD40 ligand targets and activates dendritic cells. Retrovirology. In press.
    • (2011) Retrovirology
    • Melchers, M.1    Matthews, K.2    de Vries, R.P.3    Eggink, D.4    van Montfort, T.5
  • 38
    • 84863393454 scopus 로고    scopus 로고
    • Targeting HIV-1 envelope glycoprotein trimers to B cells by using APRIL improves antibody responses
    • JVI.06259-11 [pii];10.1128/JVI.06259-11 [doi]
    • Melchers M, Bontjer I, Tong T, Chung NP, Klasse PJ, et al. (2012) Targeting HIV-1 envelope glycoprotein trimers to B cells by using APRIL improves antibody responses. J Virol 86: 2488-2500. JVI.06259-11 [pii];10.1128/JVI.06259-11 [doi].
    • (2012) J Virol , vol.86 , pp. 2488-2500
    • Melchers, M.1    Bontjer, I.2    Tong, T.3    Chung, N.P.4    Klasse, P.J.5
  • 39
    • 0029177469 scopus 로고
    • Differential regulation of the mannose and SP-A receptors on macrophages
    • Chroneos Z, Shepherd VL, (1995) Differential regulation of the mannose and SP-A receptors on macrophages. Am J Physiol 269: L721-L726.
    • (1995) Am J Physiol , vol.269
    • Chroneos, Z.1    Shepherd, V.L.2
  • 40
    • 84868291996 scopus 로고    scopus 로고
    • Differential expression of HIV-1 interfering factors in monocyte-derived macrophages stimulated with polarizing cytokines or interferons
    • 101038/srep00763 [doi]
    • Cobos Jiménez V, Booiman T, de Taeye SW, van Dort KA, Rits MA, et al. (2012) Differential expression of HIV-1 interfering factors in monocyte-derived macrophages stimulated with polarizing cytokines or interferons. Sci Rep 2: 763 101038/srep00763 [doi].
    • (2012) Sci Rep , vol.2 , pp. 763
    • Cobos Jiménez, V.1    Booiman, T.2    de Taeye, S.W.3    van Dort, K.A.4    Rits, M.A.5
  • 41
    • 7644231561 scopus 로고    scopus 로고
    • The chemokine system in diverse forms of macrophage activation and polarization
    • S1471-4906(04)00295-9 [pii];10.1016/j.it.2004.09.015 [doi]
    • Mantovani A, Sica A, Sozzani S, Allavena P, Vecchi A, et al. (2004) The chemokine system in diverse forms of macrophage activation and polarization. Trends Immunol 25: 677-686. S1471-4906(04)00295-9 [pii];10.1016/j.it.2004.09.015 [doi].
    • (2004) Trends Immunol , vol.25 , pp. 677-686
    • Mantovani, A.1    Sica, A.2    Sozzani, S.3    Allavena, P.4    Vecchi, A.5
  • 42
    • 0035577475 scopus 로고    scopus 로고
    • Immunization with an interferon-gamma-gp120 fusion protein induces enhanced immune responses to human immunodeficiency virus gp120
    • JID010413 [pii];10.1086/324371 [doi]
    • McCormick AL, Thomas MS, Heath AW (2001) Immunization with an interferon-gamma-gp120 fusion protein induces enhanced immune responses to human immunodeficiency virus gp120. J Infect Dis 184: 1423-1430. JID010413 [pii];10.1086/324371 [doi].
    • (2001) J Infect Dis , vol.184 , pp. 1423-1430
    • McCormick, A.L.1    Thomas, M.S.2    Heath, A.W.3
  • 43
    • 19444368802 scopus 로고    scopus 로고
    • An interferon gamma-gp120 fusion delivered as a DNA vaccine induces enhanced priming
    • S0264-410X(05)00335-X [pii];10.1016/j.vaccine.2005.01.160 [doi]
    • Nimal S, McCormick AL, Thomas MS, Heath AW (2005) An interferon gamma-gp120 fusion delivered as a DNA vaccine induces enhanced priming. Vaccine 23: 3984-3990. S0264-410X(05)00335-X [pii];10.1016/j.vaccine.2005.01.160 [doi].
    • (2005) Vaccine , vol.23 , pp. 3984-3990
    • Nimal, S.1    McCormick, A.L.2    Thomas, M.S.3    Heath, A.W.4
  • 44
    • 33645050385 scopus 로고    scopus 로고
    • Enhancement of immune responses to an HIV gp120 DNA vaccine by fusion to TNF alpha cDNA
    • S0264-410X(06)00035-1 [pii];10.1016/j.vaccine.2006.01.020 [doi]
    • Nimal S, Heath AW, Thomas MS (2006) Enhancement of immune responses to an HIV gp120 DNA vaccine by fusion to TNF alpha cDNA. Vaccine 24: 3298-3308. S0264-410X(06)00035-1 [pii];10.1016/j.vaccine.2006.01.020 [doi].
    • (2006) Vaccine , vol.24 , pp. 3298-3308
    • Nimal, S.1    Heath, A.W.2    Thomas, M.S.3
  • 45
    • 70349336496 scopus 로고    scopus 로고
    • The Granulocyte-macrophage Colony-stimulating Factor Receptor: Linking Its Structure to Cell Signaling and Its Role In Disease
    • blood-2008-12-164004 [pii];10.1182/blood-2008-12-164004 [doi]
    • Hercus TR, Thomas D, Guthridge MA, Ekert PG, King-Scott J, et al. (2009) The granulocyte-macrophage colony-stimulating factor receptor: linking its structure to cell signaling and its role in disease. Blood 114: 1289-1298. blood-2008-12-164004 [pii];10.1182/blood-2008-12-164004 [doi].
    • (2009) Blood , pp. 1289-1298
    • Hercus, T.R.1    Thomas, D.2    Guthridge, M.A.3    Ekert, P.G.4    King-Scott, J.5
  • 46
    • 77955911496 scopus 로고    scopus 로고
    • Molecular basis of cytokine receptor activation
    • 101002/iub.350 [doi]
    • Lopez AF, Hercus TR, Ekert P, Littler DR, Guthridge M, et al. (2010) Molecular basis of cytokine receptor activation. IUBMB Life 62: 509-518 101002/iub.350 [doi].
    • (2010) IUBMB Life , vol.62 , pp. 509-518
    • Lopez, A.F.1    Hercus, T.R.2    Ekert, P.3    Littler, D.R.4    Guthridge, M.5
  • 47
    • 0035838984 scopus 로고    scopus 로고
    • Dendritic cells: Specialized and regulated antigen processing machines
    • S0092-8674(01)00449-4 [pii]
    • Mellman I, Steinman RM (2001) Dendritic cells: specialized and regulated antigen processing machines. Cell 106: 255-258. S0092-8674(01)00449-4 [pii].
    • (2001) Cell , vol.106 , pp. 255-258
    • Mellman, I.1    Steinman, R.M.2
  • 48
    • 79956116032 scopus 로고    scopus 로고
    • RORgammat drives production of the cytokine GM-CSF in helper T cells, which is essential for the effector phase of autoimmune neuroinflammation
    • ni.2027 [pii];10.1038/ni.2027 [doi]
    • Codarri L, Gyulveszi G, Tosevski V, Hesske L, Fontana A, et al. (2011) RORgammat drives production of the cytokine GM-CSF in helper T cells, which is essential for the effector phase of autoimmune neuroinflammation. Nat Immunol 12: 560-567. ni.2027 [pii];10.1038/ni.2027 [doi].
    • (2011) Nat Immunol , vol.12 , pp. 560-567
    • Codarri, L.1    Gyulveszi, G.2    Tosevski, V.3    Hesske, L.4    Fontana, A.5
  • 49
    • 0024353942 scopus 로고
    • Identification of critical regions in mouse granulocyte-macrophage colony-stimulating factor by scanning-deletion analysis
    • Shanafelt AB, Kastelein RA, (1989) Identification of critical regions in mouse granulocyte-macrophage colony-stimulating factor by scanning-deletion analysis. Proc Natl Acad Sci U S A 86: 4872-4876.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 4872-4876
    • Shanafelt, A.B.1    Kastelein, R.A.2
  • 50
    • 0023190642 scopus 로고
    • Increased biological activity of deglycosylated recombinant human granulocyte/macrophage colony-stimulating factor produced by yeast or animal cells
    • Moonen P, Mermod JJ, Ernst JF, Hirschi M, DeLamarter JF, (1987) Increased biological activity of deglycosylated recombinant human granulocyte/macrophage colony-stimulating factor produced by yeast or animal cells. Proc Natl Acad Sci U S A 84: 4428-4431.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 4428-4431
    • Moonen, P.1    Mermod, J.J.2    Ernst, J.F.3    Hirschi, M.4    Delamarter, J.F.5
  • 51
    • 84864603281 scopus 로고    scopus 로고
    • Structural mechanism of trimeric HIV-1 envelope glycoprotein activation
    • 101371/journal.ppat.1002797 [doi];PPATHOGENS-D-12-01032 [pii]
    • Tran EE, Borgnia MJ, Kuybeda O, Schauder DM, Bartesaghi A, et al. (2012) Structural mechanism of trimeric HIV-1 envelope glycoprotein activation. PLoS Pathog 8: e1002797 101371/journal.ppat.1002797 [doi];PPATHOGENS-D-12-01032 [pii].
    • (2012) PLoS Pathog , vol.8
    • Tran, E.E.1    Borgnia, M.J.2    Kuybeda, O.3    Schauder, D.M.4    Bartesaghi, A.5
  • 52
    • 0029119783 scopus 로고
    • Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding
    • Wyatt R, Moore J, Accola M, Desjardin E, Robinson J, et al. (1995) Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding. J Virol 69: 5723-5733.
    • (1995) J Virol , vol.69 , pp. 5723-5733
    • Wyatt, R.1    Moore, J.2    Accola, M.3    Desjardin, E.4    Robinson, J.5
  • 53
    • 0029805606 scopus 로고    scopus 로고
    • AID-PROT6>3.0.CO;2-D [pii];10.1002/(SICI)1097-0134(199611)26:3<304::AID-PROT6>3.0.CO;2-D [doi]
    • Rozwarski DA, Diederichs K, Hecht R, Boone T, Karplus PA (1996) AID-PROT6>3.0.CO;2-D [pii];10.1002/(SICI)1097-0134(199611)26:3<304::AID-PROT6>3.0.CO;2-D [doi].
    • (1996)
    • Rozwarski, D.A.1    Diederichs, K.2    Hecht, R.3    Boone, T.4    Karplus, P.A.5
  • 54
    • 0141521564 scopus 로고    scopus 로고
    • Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1
    • Labrijn AF, Poignard P, Raja A, Zwick MB, Delgado K, et al. (2003) Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1. J Virol 77: 10557-10565.
    • (2003) J Virol , vol.77 , pp. 10557-10565
    • Labrijn, A.F.1    Poignard, P.2    Raja, A.3    Zwick, M.B.4    Delgado, K.5
  • 55
    • 0037225412 scopus 로고    scopus 로고
    • Rabbit immune repertoires as sources for therapeutic monoclonal antibodies: The impact of kappa allotype-correlated variation in cysteine content on antibody libraries selected by phage display
    • S0022283602012329 [pii]
    • Popkov M, Mage RG, Alexander CB, Thundivalappil S, Barbas CF, et al. (2003) Rabbit immune repertoires as sources for therapeutic monoclonal antibodies: the impact of kappa allotype-correlated variation in cysteine content on antibody libraries selected by phage display. J Mol Biol 325: 325-335. S0022283602012329 [pii].
    • (2003) J Mol Biol , vol.325 , pp. 325-335
    • Popkov, M.1    Mage, R.G.2    Alexander, C.B.3    Thundivalappil, S.4    Barbas, C.F.5
  • 56
    • 77954982131 scopus 로고    scopus 로고
    • Crystal structure of PG16 and chimeric dissection with somatically related PG9: Structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1
    • JVI.00966-10 [pii]; doi:10.1128/JVI.00966-10
    • Pancera M, McLellan JS, Wu X, Zhu J, Changela A, et al. (2010) Crystal structure of PG16 and chimeric dissection with somatically related PG9: structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1. J Virol 84: 8098-8110. JVI.00966-10 [pii]; doi: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
  • 57
    • 77954912140 scopus 로고    scopus 로고
    • Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1
    • 100460010 [pii]; doi:10.1073/pnas.1004600107
    • Pejchal R, Walker LM, Stanfield RL, Phogat SK, Koff WC, et al. (2010) Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1. Proc Natl Acad Sci U S A 107: 11483-11488 100460010 [pii]; doi:10.1073/pnas.1004600107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 11483-11488
    • Pejchal, R.1    Walker, L.M.2    Stanfield, R.L.3    Phogat, S.K.4    Koff, W.C.5
  • 58
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • 117874 [pii]; doi:10.1126/science.1178746
    • 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 117874 [pii]; doi:10.1126/science.1178746.
    • (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
  • 59
    • 84867653590 scopus 로고    scopus 로고
    • Increased HIV-1 vaccine efficacy against viruses with genetic signatures in Env V2
    • nature11519 [pii]; doi:10.1038/nature11519
    • Rolland M, Edlefsen PT, Larsen BB, Tovanabutra S, Sanders-Buell E, et al. (2012) Increased HIV-1 vaccine efficacy against viruses with genetic signatures in Env V2. Nature 490: 417-420. nature11519 [pii]; doi:10.1038/nature11519.
    • (2012) Nature , vol.490 , pp. 417-420
    • Rolland, M.1    Edlefsen, P.T.2    Larsen, B.B.3    Tovanabutra, S.4    Sanders-Buell, E.5
  • 60
    • 7244232761 scopus 로고    scopus 로고
    • Characterization of glycopeptides from HIV-I(SF2) gp120 by liquid chromatography mass spectrometry
    • S1044-0305(04)00480-5 [pii]; doi:10.1016/j.jasms.2004.07.008
    • Cutalo JM, Deterding LJ, Tomer KB (2004) Characterization of glycopeptides from HIV-I(SF2) gp120 by liquid chromatography mass spectrometry. J Am Soc Mass Spectrom 15: 1545-1555. S1044-0305(04)00480-5 [pii]; doi:10.1016/j.jasms.2004.07.008.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 1545-1555
    • Cutalo, J.M.1    Deterding, L.J.2    Tomer, K.B.3
  • 61
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, et al. (1990) Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J Biol Chem 265: 10373-10382.
    • (1990) J Biol Chem , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5
  • 62
    • 0034687168 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells
    • bi000432m [pii]
    • Zhu X, Borchers C, Bienstock RJ, Tomer KB (2000) Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells. Biochemistry 39: 11194-11204. bi000432m [pii].
    • (2000) Biochemistry , vol.39 , pp. 11194-11204
    • Zhu, X.1    Borchers, C.2    Bienstock, R.J.3    Tomer, K.B.4
  • 63
    • 1542314755 scopus 로고    scopus 로고
    • N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line
    • 3993 [pii]
    • Forno G, Bollati FM, Oggero M, Kratje R, Etcheverrigaray M, et al.(2004) N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line. Eur J Biochem 271: 907-919 3993 [pii].
    • (2004) Eur J Biochem , vol.271 , pp. 907-919
    • Forno, G.1    Bollati, F.M.2    Oggero, M.3    Kratje, R.4    Etcheverrigaray, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.