메뉴 건너뛰기




Volumn 21, Issue 8, 2013, Pages 397-404

Catching HIV 'in the act' with 3D electron microscopy

Author keywords

Cryo electron tomography; Focused ion beam scanning electron microscopy (FIB SEM); Ion abrasion scanning electron microscopy (IA SEM); Vaccine design; Virus cell interaction

Indexed keywords

CD209 ANTIGEN; CD4 ANTIGEN; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; NEUTRALIZING ANTIBODY; VIRUS ENVELOPE PROTEIN;

EID: 84881028558     PISSN: 0966842X     EISSN: 18784380     Source Type: Journal    
DOI: 10.1016/j.tim.2013.06.004     Document Type: Review
Times cited : (19)

References (72)
  • 1
    • 51349162563 scopus 로고    scopus 로고
    • Molecular architecture of native HIV-1 gp120 trimers
    • Liu J., et al. Molecular architecture of native HIV-1 gp120 trimers. Nature 2008, 455:109-113.
    • (2008) Nature , vol.455 , pp. 109-113
    • Liu, J.1
  • 2
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens
    • Wyatt R., Sodroski J. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 1998, 280:1884-1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 3
    • 0021751840 scopus 로고
    • The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
    • Dalgleish A.G., et al. The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature 1984, 312:763-767.
    • (1984) Nature , vol.312 , pp. 763-767
    • Dalgleish, A.G.1
  • 4
    • 36048945481 scopus 로고    scopus 로고
    • The interaction of HIV with dendritic cells: outcomes and pathways
    • Piguet V., Steinman R.M. The interaction of HIV with dendritic cells: outcomes and pathways. Trends Immunol. 2007, 28:503-510.
    • (2007) Trends Immunol. , vol.28 , pp. 503-510
    • Piguet, V.1    Steinman, R.M.2
  • 5
    • 80052507145 scopus 로고    scopus 로고
    • Progress in the rational design of an AIDS vaccine
    • Nabel G.J., et al. Progress in the rational design of an AIDS vaccine. Philos. Trans. R. Soc. B 2011, 366:2759-2765.
    • (2011) Philos. Trans. R. Soc. B , vol.366 , pp. 2759-2765
    • Nabel, G.J.1
  • 6
    • 0027985431 scopus 로고
    • Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody
    • Burton D.R., et al. Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 1994, 266:1024-1027.
    • (1994) Science , vol.266 , pp. 1024-1027
    • Burton, D.R.1
  • 7
    • 0027378573 scopus 로고
    • A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1
    • Muster T., et al. A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J. Virol. 1993, 67:6642-6647.
    • (1993) J. Virol. , vol.67 , pp. 6642-6647
    • Muster, T.1
  • 8
    • 0028865465 scopus 로고
    • Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG
    • Trkola A., et al. Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG. J. Virol. 1995, 69:6609-6617.
    • (1995) J. Virol. , vol.69 , pp. 6609-6617
    • Trkola, A.1
  • 9
    • 34249950588 scopus 로고    scopus 로고
    • Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors
    • Dhillon A.K., et al. Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. J. Virol. 2007, 81:6548-6562.
    • (2007) J. Virol. , vol.81 , pp. 6548-6562
    • Dhillon, A.K.1
  • 10
    • 34948854718 scopus 로고    scopus 로고
    • Broad HIV-1 neutralization mediated by CD4-binding site antibodies
    • Li Y., et al. Broad HIV-1 neutralization mediated by CD4-binding site antibodies. Nat. Med. 2007, 13:1032-1034.
    • (2007) Nat. Med. , vol.13 , pp. 1032-1034
    • Li, Y.1
  • 11
    • 58149487645 scopus 로고    scopus 로고
    • Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection
    • Sather D.N., et al. Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J. Virol. 2009, 83:757-769.
    • (2009) J. Virol. , vol.83 , pp. 757-769
    • Sather, D.N.1
  • 12
    • 58149399396 scopus 로고    scopus 로고
    • Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies
    • Doria-Rose N.A., et al. Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies. J. Virol. 2009, 83:188-199.
    • (2009) J. Virol. , vol.83 , pp. 188-199
    • Doria-Rose, N.A.1
  • 13
    • 69149083668 scopus 로고    scopus 로고
    • Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine?
    • Stamatatos L., et al. Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine?. Nat. Med. 2009, 15:866-870.
    • (2009) Nat. Med. , vol.15 , pp. 866-870
    • Stamatatos, L.1
  • 14
    • 67650453747 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 elite neutralizers: individuals with broad and potent neutralizing activity identified by using a high-throughput neutralization assay together with an analytical selection algorithm
    • Simek M.D., et al. Human immunodeficiency virus type 1 elite neutralizers: individuals with broad and potent neutralizing activity identified by using a high-throughput neutralization assay together with an analytical selection algorithm. J. Virol. 2009, 83:7337-7348.
    • (2009) J. Virol. , vol.83 , pp. 7337-7348
    • Simek, M.D.1
  • 15
    • 63849131879 scopus 로고    scopus 로고
    • Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals
    • Scheid J.F., et al. Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals. Nature 2009, 458:636-640.
    • (2009) Nature , vol.458 , pp. 636-640
    • Scheid, J.F.1
  • 16
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid J.F., et al. Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 2011, 333:1633-1637.
    • (2011) Science , vol.333 , pp. 1633-1637
    • Scheid, J.F.1
  • 17
    • 84866495323 scopus 로고    scopus 로고
    • Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies
    • Kwong P.D., Mascola J.R. Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies. Immunity 2012, 37:412-425.
    • (2012) Immunity , vol.37 , pp. 412-425
    • Kwong, P.D.1    Mascola, J.R.2
  • 18
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T., et al. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 2010, 329:811-817.
    • (2010) Science , vol.329 , pp. 811-817
    • Zhou, T.1
  • 19
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • McLellan J.S., et al. Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 2011, 480:336-343.
    • (2011) Nature , vol.480 , pp. 336-343
    • McLellan, J.S.1
  • 20
    • 84866493348 scopus 로고    scopus 로고
    • Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
    • Huang J., et al. Broad and potent neutralization of HIV-1 by a gp41-specific human antibody. Nature 2012, 491:406-412.
    • (2012) Nature , vol.491 , pp. 406-412
    • Huang, J.1
  • 21
    • 77954912140 scopus 로고    scopus 로고
    • Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1
    • Pejchal R., et al. 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. 2010, 107:11483-11488.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 11483-11488
    • Pejchal, R.1
  • 23
    • 78651241895 scopus 로고    scopus 로고
    • Molecular architectures of trimeric SIV and HIV-1 envelope glycoproteins on intact viruses: strain-dependent variation in quaternary structure
    • White T.A., et al. Molecular architectures of trimeric SIV and HIV-1 envelope glycoproteins on intact viruses: strain-dependent variation in quaternary structure. PLoS Pathog. 2010, 6:e1001249.
    • (2010) PLoS Pathog. , vol.6
    • White, T.A.1
  • 24
    • 79960974710 scopus 로고    scopus 로고
    • Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures
    • Harris A., et al. Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:11440-11445.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 11440-11445
    • Harris, A.1
  • 25
    • 84872189908 scopus 로고    scopus 로고
    • Molecular structures of trimeric HIV-1 Env in complex with small antibody derivatives
    • Meyerson J.R., et al. Molecular structures of trimeric HIV-1 Env in complex with small antibody derivatives. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:513-518.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 513-518
    • Meyerson, J.R.1
  • 26
    • 84860584093 scopus 로고    scopus 로고
    • Computational separation of conformational heterogeneity using cryo-electron tomography and 3D sub-volume averaging
    • Frank G.A., et al. Computational separation of conformational heterogeneity using cryo-electron tomography and 3D sub-volume averaging. J. Struct. Biol. 2012, 178:165-176.
    • (2012) J. Struct. Biol. , vol.178 , pp. 165-176
    • Frank, G.A.1
  • 27
    • 57149107577 scopus 로고    scopus 로고
    • Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs
    • Zhu P., et al. Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs. PLoS Pathog. 2008, 4:e1000203.
    • (2008) PLoS Pathog. , vol.4
    • Zhu, P.1
  • 28
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X., et al. Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 2010, 329:856-861.
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1
  • 29
    • 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., et al. Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals. PLoS ONE 2010, 5:e8805.
    • (2010) PLoS ONE , vol.5
    • Corti, D.1
  • 30
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker L.M., et al. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 2009, 326:285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1
  • 31
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker L.M., et al. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 2011, 477:466-470.
    • (2011) Nature , vol.477 , pp. 466-470
    • Walker, L.M.1
  • 32
    • 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., et al. 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. 2011, 85:9998-10009.
    • (2011) J. Virol. , vol.85 , pp. 9998-10009
    • Bonsignori, M.1
  • 33
    • 84864603281 scopus 로고    scopus 로고
    • Structural mechanism of trimeric HIV-1 envelope glycoprotein activation
    • Tran E.E., et al. Structural mechanism of trimeric HIV-1 envelope glycoprotein activation. PLoS Pathog. 2012, 8:e1002797.
    • (2012) PLoS Pathog. , vol.8
    • Tran, E.E.1
  • 34
    • 4544379899 scopus 로고    scopus 로고
    • Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope
    • Ofek G., et al. Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J. Virol. 2004, 78:10724-10737.
    • (2004) J. Virol. , vol.78 , pp. 10724-10737
    • Ofek, G.1
  • 35
    • 13844255333 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41
    • Cardoso R.M., et al. Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity 2005, 22:163-173.
    • (2005) Immunity , vol.22 , pp. 163-173
    • Cardoso, R.M.1
  • 36
    • 69249220320 scopus 로고    scopus 로고
    • A conformational switch in human immunodeficiency virus gp41 revealed by the structures of overlapping epitopes recognized by neutralizing antibodies
    • Pejchal R., et al. A conformational switch in human immunodeficiency virus gp41 revealed by the structures of overlapping epitopes recognized by neutralizing antibodies. J. Virol. 2009, 83:8451-8462.
    • (2009) J. Virol. , vol.83 , pp. 8451-8462
    • Pejchal, R.1
  • 37
    • 0030962291 scopus 로고    scopus 로고
    • Atomic structure of the ectodomain from HIV-1 gp41
    • Weissenhorn W., et al. Atomic structure of the ectodomain from HIV-1 gp41. Nature 1997, 387:426-430.
    • (1997) Nature , vol.387 , pp. 426-430
    • Weissenhorn, W.1
  • 38
    • 77954059555 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions
    • Buzon V., et al. Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathog. 2010, 6:e1000880.
    • (2010) PLoS Pathog. , vol.6
    • Buzon, V.1
  • 39
    • 84878608643 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 membrane-proximal external-region-directed broadly neutralizing antibody Z13e1
    • Harris A.K., et al. HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 membrane-proximal external-region-directed broadly neutralizing antibody Z13e1. J. Virol. 2013, 87:7191-7196.
    • (2013) J. Virol. , vol.87 , pp. 7191-7196
    • Harris, A.K.1
  • 40
    • 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., et al. Neutralizing antibody directed against the HIV-1 envelope glycoprotein can completely block HIV-1/SIV chimeric virus infections of macaque monkeys. Nat. Med. 1999, 5:204-210.
    • (1999) Nat. Med. , vol.5 , pp. 204-210
    • Shibata, R.1
  • 41
    • 0033951746 scopus 로고    scopus 로고
    • Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies
    • Mascola J.R., et al. Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies. Nat. Med. 2000, 6:207-210.
    • (2000) Nat. Med. , vol.6 , pp. 207-210
    • Mascola, J.R.1
  • 42
    • 67249131966 scopus 로고    scopus 로고
    • Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers
    • Hessell A.J., et al. Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers. PLoS Pathog. 2009, 5:e1000433.
    • (2009) PLoS Pathog. , vol.5
    • Hessell, A.J.1
  • 43
    • 84867847173 scopus 로고    scopus 로고
    • T cell virological synapses and HIV-1 pathogenesis
    • Chen B.K. T cell virological synapses and HIV-1 pathogenesis. Immunol. Res. 2012, 54:133-139.
    • (2012) Immunol. Res. , vol.54 , pp. 133-139
    • Chen, B.K.1
  • 44
    • 22744433225 scopus 로고    scopus 로고
    • Macrophages archive HIV-1 virions for dissemination in trans
    • Sharova N., et al. Macrophages archive HIV-1 virions for dissemination in trans. EMBO J. 2005, 24:2481-2489.
    • (2005) EMBO J. , vol.24 , pp. 2481-2489
    • Sharova, N.1
  • 45
    • 0033590168 scopus 로고    scopus 로고
    • Rapid and efficient cell-to-cell transmission of human immunodeficiency virus infection from monocyte-derived macrophages to peripheral blood lymphocytes
    • Carr J.M., et al. Rapid and efficient cell-to-cell transmission of human immunodeficiency virus infection from monocyte-derived macrophages to peripheral blood lymphocytes. Virology 1999, 265:319-329.
    • (1999) Virology , vol.265 , pp. 319-329
    • Carr, J.M.1
  • 46
    • 0026625135 scopus 로고
    • Dendritic cells exposed to human immunodeficiency virus type-1 transmit a vigorous cytopathic infection to CD4+ T cells
    • Cameron P.U., et al. Dendritic cells exposed to human immunodeficiency virus type-1 transmit a vigorous cytopathic infection to CD4+ T cells. Science 1992, 257:383-387.
    • (1992) Science , vol.257 , pp. 383-387
    • Cameron, P.U.1
  • 47
    • 0029070088 scopus 로고
    • Infection of human fetal astrocytes with HIV-1: viral tropism and the role of cell to cell contact in viral transmission
    • Nath A., et al. Infection of human fetal astrocytes with HIV-1: viral tropism and the role of cell to cell contact in viral transmission. J. Neuropathol. Exp. Neurol. 1995, 54:320-330.
    • (1995) J. Neuropathol. Exp. Neurol. , vol.54 , pp. 320-330
    • Nath, A.1
  • 48
    • 85047690554 scopus 로고    scopus 로고
    • Dangerous liaisons at the virological synapse
    • Piguet V., Sattentau Q. Dangerous liaisons at the virological synapse. J. Clin. Invest. 2004, 114:605-610.
    • (2004) J. Clin. Invest. , vol.114 , pp. 605-610
    • Piguet, V.1    Sattentau, Q.2
  • 49
    • 70349686333 scopus 로고    scopus 로고
    • Ion-abrasion scanning electron microscopy reveals surface-connected tubular conduits in HIV-infected macrophages
    • Bennett A.E., et al. Ion-abrasion scanning electron microscopy reveals surface-connected tubular conduits in HIV-infected macrophages. PLoS Pathog. 2009, 5:e1000591.
    • (2009) PLoS Pathog. , vol.5
    • Bennett, A.E.1
  • 50
    • 77956643036 scopus 로고    scopus 로고
    • Virus cell-to-cell transmission
    • Mothes W., et al. Virus cell-to-cell transmission. J. Virol. 2010, 84:8360-8368.
    • (2010) J. Virol. , vol.84 , pp. 8360-8368
    • Mothes, W.1
  • 51
    • 36049037370 scopus 로고    scopus 로고
    • Predominant mode of human immunodeficiency virus transfer between T cells is mediated by sustained Env-dependent neutralization-resistant virological synapses
    • Chen P., et al. Predominant mode of human immunodeficiency virus transfer between T cells is mediated by sustained Env-dependent neutralization-resistant virological synapses. J. Virol. 2007, 81:12582-12595.
    • (2007) J. Virol. , vol.81 , pp. 12582-12595
    • Chen, P.1
  • 52
    • 0027468750 scopus 로고
    • Quantitation of human immunodeficiency virus type 1 infection kinetics
    • Dimitrov D.S., et al. Quantitation of human immunodeficiency virus type 1 infection kinetics. J. Virol. 1993, 67:2182-2190.
    • (1993) J. Virol. , vol.67 , pp. 2182-2190
    • Dimitrov, D.S.1
  • 53
    • 0036883678 scopus 로고    scopus 로고
    • Long-term survival and virus production in human primary macrophages infected by human immunodeficiency virus
    • Aquaro S., et al. Long-term survival and virus production in human primary macrophages infected by human immunodeficiency virus. J. Med. Virol. 2002, 68:479-488.
    • (2002) J. Med. Virol. , vol.68 , pp. 479-488
    • Aquaro, S.1
  • 54
    • 33750486534 scopus 로고    scopus 로고
    • In vitro modeling of the HIV-macrophage reservoir
    • Brown A., et al. In vitro modeling of the HIV-macrophage reservoir. J. Leukoc. Biol. 2006, 80:1127-1135.
    • (2006) J. Leukoc. Biol. , vol.80 , pp. 1127-1135
    • Brown, A.1
  • 55
    • 33646179354 scopus 로고    scopus 로고
    • Viral piracy: HIV-1 targets dendritic cells for transmission
    • Lekkerkerker A.N., et al. Viral piracy: HIV-1 targets dendritic cells for transmission. Curr. HIV Res. 2006, 4:169-176.
    • (2006) Curr. HIV Res. , vol.4 , pp. 169-176
    • Lekkerkerker, A.N.1
  • 56
    • 34548162813 scopus 로고    scopus 로고
    • Functionally distinct transmission of human immunodeficiency virus type 1 mediated by immature and mature dendritic cells
    • Wang J.H., et al. Functionally distinct transmission of human immunodeficiency virus type 1 mediated by immature and mature dendritic cells. J. Virol. 2007, 81:8933-8943.
    • (2007) J. Virol. , vol.81 , pp. 8933-8943
    • Wang, J.H.1
  • 57
    • 9244255812 scopus 로고    scopus 로고
    • DC-SIGN-mediated infectious synapse formation enhances X4 HIV-1 transmission from dendritic cells to T cells
    • Arrighi J.F., et al. DC-SIGN-mediated infectious synapse formation enhances X4 HIV-1 transmission from dendritic cells to T cells. J. Exp. Med. 2004, 200:1279-1288.
    • (2004) J. Exp. Med. , vol.200 , pp. 1279-1288
    • Arrighi, J.F.1
  • 58
    • 77951288057 scopus 로고    scopus 로고
    • HIV-1 exploits innate signaling by TLR8 and DC-SIGN for productive infection of dendritic cells
    • Gringhuis S.I., et al. HIV-1 exploits innate signaling by TLR8 and DC-SIGN for productive infection of dendritic cells. Nat. Immunol. 2010, 11:419-426.
    • (2010) Nat. Immunol. , vol.11 , pp. 419-426
    • Gringhuis, S.I.1
  • 59
    • 79952092894 scopus 로고    scopus 로고
    • HIV-1 virological synapse is not simply a copycat of the immunological synapse
    • Vasiliver-Shamis G., et al. HIV-1 virological synapse is not simply a copycat of the immunological synapse. Viruses 2010, 2:1239-1260.
    • (2010) Viruses , vol.2 , pp. 1239-1260
    • Vasiliver-Shamis, G.1
  • 60
    • 0038025223 scopus 로고    scopus 로고
    • Recruitment of HIV and its receptors to dendritic cell-T cell junctions
    • McDonald D., et al. Recruitment of HIV and its receptors to dendritic cell-T cell junctions. Science 2003, 300:1295-1297.
    • (2003) Science , vol.300 , pp. 1295-1297
    • McDonald, D.1
  • 61
    • 77955781209 scopus 로고    scopus 로고
    • 3D visualization of HIV transfer at the virological synapse between dendritic cells and T cells
    • Felts R.L., et al. 3D visualization of HIV transfer at the virological synapse between dendritic cells and T cells. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:13336-13341.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 13336-13341
    • Felts, R.L.1
  • 62
    • 80051790266 scopus 로고    scopus 로고
    • HIV-1 activates Cdc42 and induces membrane extensions in immature dendritic cells to facilitate cell-to-cell virus propagation
    • Nikolic D.S., et al. HIV-1 activates Cdc42 and induces membrane extensions in immature dendritic cells to facilitate cell-to-cell virus propagation. Blood 2011, 118:4841-4852.
    • (2011) Blood , vol.118 , pp. 4841-4852
    • Nikolic, D.S.1
  • 63
    • 84874648730 scopus 로고    scopus 로고
    • Cell-to-cell transmission of viruses
    • Zhong P., et al. Cell-to-cell transmission of viruses. Curr. Opin. Virol. 2013, 3:44-50.
    • (2013) Curr. Opin. Virol. , vol.3 , pp. 44-50
    • Zhong, P.1
  • 64
    • 84870372472 scopus 로고    scopus 로고
    • HIV entry and envelope glycoprotein-mediated fusion
    • Blumenthal R., et al. HIV entry and envelope glycoprotein-mediated fusion. J. Biol. Chem. 2012, 287:40841-40849.
    • (2012) J. Biol. Chem. , vol.287 , pp. 40841-40849
    • Blumenthal, R.1
  • 65
    • 34249672782 scopus 로고    scopus 로고
    • Electron tomography of the contact between T cells and SIV/HIV-1: implications for viral entry
    • Sougrat R., et al. Electron tomography of the contact between T cells and SIV/HIV-1: implications for viral entry. PLoS Pathog. 2007, 3:e63.
    • (2007) PLoS Pathog. , vol.3
    • Sougrat, R.1
  • 66
    • 78049292402 scopus 로고    scopus 로고
    • Organization of cellular receptors into a nanoscale junction during HIV-1 adhesion
    • Dobrowsky T.M., et al. Organization of cellular receptors into a nanoscale junction during HIV-1 adhesion. PLoS Comput. Biol. 2010, 6:e1000855.
    • (2010) PLoS Comput. Biol. , vol.6
    • Dobrowsky, T.M.1
  • 67
    • 84865093951 scopus 로고    scopus 로고
    • Lessons in nonhuman primate models for AIDS vaccine research: from minefields to milestones
    • Lifson J.D., Haigwood N.L. Lessons in nonhuman primate models for AIDS vaccine research: from minefields to milestones. Cold Spring Harb. Perspect. Med. 2012, 2:a007310.
    • (2012) Cold Spring Harb. Perspect. Med. , vol.2
    • Lifson, J.D.1    Haigwood, N.L.2
  • 68
    • 13944254982 scopus 로고    scopus 로고
    • Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection
    • Flynn N.M., et al. Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection. J. Infect. Dis. 2005, 191:654-665.
    • (2005) J. Infect. Dis. , vol.191 , pp. 654-665
    • Flynn, N.M.1
  • 69
    • 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., et al. 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. 2006, 194:1661-1671.
    • (2006) J. Infect. Dis. , vol.194 , pp. 1661-1671
    • Pitisuttithum, P.1
  • 70
    • 73349094086 scopus 로고    scopus 로고
    • Vaccination with ALVAC and AIDSVAX to prevent HIV-1 infection in Thailand
    • Rerks-Ngarm S., et al. Vaccination with ALVAC and AIDSVAX to prevent HIV-1 infection in Thailand. N. Engl. J. Med. 2009, 361:2209-2220.
    • (2009) N. Engl. J. Med. , vol.361 , pp. 2209-2220
    • Rerks-Ngarm, S.1
  • 72
    • 84868589536 scopus 로고    scopus 로고
    • The Thai Phase III HIV Type 1 Vaccine trial (RV144) regimen induces antibodies that target conserved regions within the V2 loop of gp120
    • Karasavvas N., et al. The Thai Phase III HIV Type 1 Vaccine trial (RV144) regimen induces antibodies that target conserved regions within the V2 loop of gp120. AIDS Res. Hum. Retroviruses 2012, 28:1444-1457.
    • (2012) AIDS Res. Hum. Retroviruses , vol.28 , pp. 1444-1457
    • Karasavvas, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.