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Volumn 9, Issue 11, 2014, Pages

Nef neutralizes the ability of exosomes from CD4+ T cells to act as decoys during HIV-1 infection

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; NEF PROTEIN; VIRUS ENVELOPE PROTEIN;

EID: 84912535422     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0113691     Document Type: Article
Times cited : (91)

References (74)
  • 1
    • 33645414100 scopus 로고    scopus 로고
    • HIV-1 coreceptors and their inhibitors
    • Ray N, Doms RW (2006) HIV-1 coreceptors and their inhibitors. Curr Top Microbiol Immunol 303: 97-120.
    • (2006) Curr Top Microbiol Immunol , vol.303 , pp. 97-120
    • Ray, N.1    Doms, R.W.2
  • 2
    • 84887289231 scopus 로고    scopus 로고
    • HIV entry: A game of hide-and-fuse?
    • Melikyan GB (2013) HIV entry: a game of hide-and-fuse? Curr Opin Virol 4C: 1-7.
    • (2013) Curr Opin Virol , vol.4 C , pp. 1-7
    • Melikyan, G.B.1
  • 3
    • 0027158904 scopus 로고
    • Downregulation of cell-surface CD4 expression by simian immunodeficiency virus Nef prevents viral super infection
    • Benson RE, Sanfridson A, Ottinger JS, Doyle C, Cullen BR (1993) Downregulation of cell-surface CD4 expression by simian immunodeficiency virus Nef prevents viral super infection. J Exp Med 177: 1561-1566.
    • (1993) J Exp Med , vol.177 , pp. 1561-1566
    • Benson, R.E.1    Sanfridson, A.2    Ottinger, J.S.3    Doyle, C.4    Cullen, B.R.5
  • 4
    • 77955695562 scopus 로고    scopus 로고
    • Ibalizumab: An anti-CD4 monoclonal antibody for the treatment of HIV- 1 infection
    • Bruno CJ, Jacobson JM (2010) Ibalizumab: an anti-CD4 monoclonal antibody for the treatment of HIV- 1 infection. J Antimicrob Chemother 65: 1839-1841.
    • (2010) J Antimicrob Chemother , vol.65 , pp. 1839-1841
    • Bruno, C.J.1    Jacobson, J.M.2
  • 5
    • 66349110542 scopus 로고    scopus 로고
    • Soluble CD4 and CD4-mimetic compounds inhibit HIV-1 infection by induction of a short-lived activated state
    • Haim H, Si Z, Madani N, Wang L, Courter JR, et al. (2009) Soluble CD4 and CD4-mimetic compounds inhibit HIV-1 infection by induction of a short-lived activated state. PLoS Pathog 5: e1000360.
    • (2009) PLoS Pathog , vol.5 , pp. e1000360
    • Haim, H.1    Si, Z.2    Madani, N.3    Wang, L.4    Courter, J.R.5
  • 6
    • 0025016076 scopus 로고
    • High concentrations of recombinant soluble CD4 are required to neutralize primary human immunodeficiency virus type 1 isolates
    • Daar ES, Li XL, Moudgil T, Ho DD (1990) High concentrations of recombinant soluble CD4 are required to neutralize primary human immunodeficiency virus type 1 isolates. Proc Natl Acad Sci U S A 87: 6574-6578.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 6574-6578
    • Daar, E.S.1    Li, X.L.2    Moudgil, T.3    Ho, D.D.4
  • 7
    • 0025853347 scopus 로고
    • Kinetics of expression of multiply spliced RNA in early human immunodeficiency virus type 1 infection of lymphocytes and monocytes
    • Klotman ME, Kim S, Buchbinder A, DeRossi A, Baltimore D, et al. (1991) Kinetics of expression of multiply spliced RNA in early human immunodeficiency virus type 1 infection of lymphocytes and monocytes. Proc Natl Acad Sci U S A 88: 5011-5015.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 5011-5015
    • Klotman, M.E.1    Kim, S.2    Buchbinder, A.3    DeRossi, A.4    Baltimore, D.5
  • 8
    • 0028804160 scopus 로고
    • Genomic structure of an attenuated quasi species of HIV-1 from a blood transfusion donor and recipients
    • Deacon NJ, Tsykin A, Solomon A, Smith K, Ludford-Menting M, et al. (1995) Genomic structure of an attenuated quasi species of HIV-1 from a blood transfusion donor and recipients. Science 270: 988-991.
    • (1995) Science , vol.270 , pp. 988-991
    • Deacon, N.J.1    Tsykin, A.2    Solomon, A.3    Smith, K.4    Ludford-Menting, M.5
  • 9
    • 0025743306 scopus 로고
    • Importance of the nef gene for maintenance of high virus loads and for development of AIDS
    • Kestler HW 3rd, Ringler DJ, Mori K, Panicali DL, Sehgal PK, et al. (1991) Importance of the nef gene for maintenance of high virus loads and for development of AIDS. Cell 65: 651-662.
    • (1991) Cell , vol.65 , pp. 651-662
    • Kestler, H.W.1    Ringler, D.J.2    Mori, K.3    Panicali, D.L.4    Sehgal, P.K.5
  • 10
    • 0028835788 scopus 로고
    • Brief report: Absence of intact nef sequences in a long-term survivor with nonprogressive HIV-1 infection
    • Kirchhoff F, Greenough TC, Brettler DB, Sullivan JL, Desrosiers RC (1995) Brief report: absence of intact nef sequences in a long-term survivor with nonprogressive HIV-1 infection. N Engl J Med 332: 228-232.
    • (1995) N Engl J Med , vol.332 , pp. 228-232
    • Kirchhoff, F.1    Greenough, T.C.2    Brettler, D.B.3    Sullivan, J.L.4    Desrosiers, R.C.5
  • 11
    • 0029846223 scopus 로고    scopus 로고
    • High frequency of defective nef alleles in a long-term survivor with nonprogressive human immunodeficiency virus type 1 infection
    • Mariani R, Kirchhoff F, Greenough TC, Sullivan JL, Desrosiers RC, et al. (1996) High frequency of defective nef alleles in a long-term survivor with nonprogressive human immunodeficiency virus type 1 infection. J Virol 70: 7752-7764.
    • (1996) J Virol , vol.70 , pp. 7752-7764
    • Mariani, R.1    Kirchhoff, F.2    Greenough, T.C.3    Sullivan, J.L.4    Desrosiers, R.C.5
  • 12
    • 0028006247 scopus 로고
    • The human immunodeficiency virus-1 nef gene product: A positive factor for viral infection and replication in primary lymphocytes and macrophages
    • Miller MD, Warmerdam MT, Gaston I, Greene WC, Feinberg MB (1994) The human immunodeficiency virus-1 nef gene product: a positive factor for viral infection and replication in primary lymphocytes and macrophages. J Exp Med 179: 101-113.
    • (1994) J Exp Med , vol.179 , pp. 101-113
    • Miller, M.D.1    Warmerdam, M.T.2    Gaston, I.3    Greene, W.C.4    Feinberg, M.B.5
  • 13
    • 0030852135 scopus 로고    scopus 로고
    • Association of human immunodeficiency virus Nef protein with actin is myristoylation dependent and influences its subcellular localization
    • Fackler OT, Kienzle N, Kremmer E, Boese A, Schramm B, et al. (1997) Association of human immunodeficiency virus Nef protein with actin is myristoylation dependent and influences its subcellular localization. Eur J Biochem 247: 843-851.
    • (1997) Eur J Biochem , vol.247 , pp. 843-851
    • Fackler, O.T.1    Kienzle, N.2    Kremmer, E.3    Boese, A.4    Schramm, B.5
  • 14
    • 33745122662 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef: Adapting to intracellular trafficking pathways
    • Roeth JF, Collins KL (2006) Human immunodeficiency virus type 1 Nef: adapting to intracellular trafficking pathways. Microbiol Mol Biol Rev 70: 548-563.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 548-563
    • Roeth, J.F.1    Collins, K.L.2
  • 16
    • 62749181801 scopus 로고    scopus 로고
    • A basic patch on alpha-adaptin is required for binding of human immunodeficiency virus type 1 Nef and cooperative assembly of a CD4-Nef-AP-2 complex
    • Chaudhuri R, Mattera R, Lindwasser O, Robinson M, Bonifacino J (2009) A basic patch on alpha-adaptin is required for binding of human immunodeficiency virus type 1 Nef and cooperative assembly of a CD4-Nef-AP-2 complex. J Virol 83: 2518-2530.
    • (2009) J Virol , vol.83 , pp. 2518-2530
    • Chaudhuri, R.1    Mattera, R.2    Lindwasser, O.3    Robinson, M.4    Bonifacino, J.5
  • 17
    • 84898733948 scopus 로고    scopus 로고
    • How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4
    • Ren X, Park SY, Bonifacino JS, Hurley JH (2014) How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4. Elife 3: e01754.
    • (2014) Elife , vol.3 , pp. e01754
    • Ren, X.1    Park, S.Y.2    Bonifacino, J.S.3    Hurley, J.H.4
  • 18
    • 0030684068 scopus 로고    scopus 로고
    • Co-localization of HIV-1 Nef with the AP-2 adaptor protein complex correlates with Nef-induced CD4 down-regulation
    • Greenberg ME, Bronson S, Lock M, Neumann M, Pavlakis GN, et al. (1997) Co-localization of HIV-1 Nef with the AP-2 adaptor protein complex correlates with Nef-induced CD4 down-regulation. Embo J 16: 6964-6976.
    • (1997) Embo J , vol.16 , pp. 6964-6976
    • Greenberg, M.E.1    Bronson, S.2    Lock, M.3    Neumann, M.4    Pavlakis, G.N.5
  • 19
    • 33845513921 scopus 로고    scopus 로고
    • Dynamic interaction of HIV-1 Nef with the clathrin-mediated endocytic pathway at the plasma membrane
    • Burtey A, Rappoport JZ, Bouchet J, Basmaciogullari S, Guatelli J, et al. (2007) Dynamic interaction of HIV-1 Nef with the clathrin-mediated endocytic pathway at the plasma membrane. Traffic 8: 61-76.
    • (2007) Traffic , vol.8 , pp. 61-76
    • Burtey, A.1    Rappoport, J.Z.2    Bouchet, J.3    Basmaciogullari, S.4    Guatelli, J.5
  • 20
    • 10344258588 scopus 로고    scopus 로고
    • HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail
    • Roeth JF, Williams M, Kasper MR, Filzen TM, Collins KL (2004) HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail. J Cell Biol 167: 903-913.
    • (2004) J Cell Biol , vol.167 , pp. 903-913
    • Roeth, J.F.1    Williams, M.2    Kasper, M.R.3    Filzen, T.M.4    Collins, K.L.5
  • 21
    • 34548510349 scopus 로고    scopus 로고
    • HIV-1 Nef-induced down-regulation of MHC class I requires AP-1 and clathrin but not PACS-1 and is impeded by AP-2
    • Lubben NB, Sahlender DA, Motley AM, Lehner PJ, Benaroch P, et al. (2007) HIV-1 Nef-induced down-regulation of MHC class I requires AP-1 and clathrin but not PACS-1 and is impeded by AP-2. Mol Biol Cell 18: 3351-3365.
    • (2007) Mol Biol Cell , vol.18 , pp. 3351-3365
    • Lubben, N.B.1    Sahlender, D.A.2    Motley, A.M.3    Lehner, P.J.4    Benaroch, P.5
  • 22
    • 81255200501 scopus 로고    scopus 로고
    • ADP ribosylation factor 1 activity is required to recruit AP-1 to the major histocompatibility complex class I (MHC-I) cytoplasmic tail and disrupt MHC-I trafficking in HIV-1-infected primary T cells
    • Wonderlich ER, Leonard JA, Kulpa DA, Leopold KE, Norman JM, et al. (2011) ADP ribosylation factor 1 activity is required to recruit AP-1 to the major histocompatibility complex class I (MHC-I) cytoplasmic tail and disrupt MHC-I trafficking in HIV-1-infected primary T cells. J Virol 85: 12216-12226.
    • (2011) J Virol , vol.85 , pp. 12216-12226
    • Wonderlich, E.R.1    Leonard, J.A.2    Kulpa, D.A.3    Leopold, K.E.4    Norman, J.M.5
  • 23
    • 79960391235 scopus 로고    scopus 로고
    • HIV-1 Nef disrupts intracellular trafficking of major histocompatibility complex class I, CD4, CD8, and CD28 by distinct pathways that share common elements
    • Leonard JA, Filzen T, Carter CC, Schaefer M, Collins KL (2011) HIV-1 Nef disrupts intracellular trafficking of major histocompatibility complex class I, CD4, CD8, and CD28 by distinct pathways that share common elements. J Virol 85: 6867-6881.
    • (2011) J Virol , vol.85 , pp. 6867-6881
    • Leonard, J.A.1    Filzen, T.2    Carter, C.C.3    Schaefer, M.4    Collins, K.L.5
  • 24
    • 38349127341 scopus 로고    scopus 로고
    • Cooperative binding of the class I major histocompatibility complex cytoplasmic domain and human immunodeficiency virus type 1 Nef to the endosomal AP-1 complex via its mu subunit
    • Noviello C, Benichou S, Guatelli J (2008) Cooperative binding of the class I major histocompatibility complex cytoplasmic domain and human immunodeficiency virus type 1 Nef to the endosomal AP-1 complex via its mu subunit. J Virol 82: 1249-1258.
    • (2008) J Virol , vol.82 , pp. 1249-1258
    • Noviello, C.1    Benichou, S.2    Guatelli, J.3
  • 25
    • 41249090191 scopus 로고    scopus 로고
    • The tyrosine binding pocket in the adaptor protein 1 (AP-1) mu1 subunit is necessary for Nef to recruit AP-1 to the major histocompatibility complex class I cytoplasmic tail
    • Wonderlich ER, Williams M, Collins KL (2008) The tyrosine binding pocket in the adaptor protein 1 (AP-1) mu1 subunit is necessary for Nef to recruit AP-1 to the major histocompatibility complex class I cytoplasmic tail. J Biol Chem 283: 3011-3022.
    • (2008) J Biol Chem , vol.283 , pp. 3011-3022
    • Wonderlich, E.R.1    Williams, M.2    Collins, K.L.3
  • 26
    • 34147169409 scopus 로고    scopus 로고
    • HIV-1 Nef assembles a Src family kinase-ZAP-70/Syk-PI3K cascade to downregulate cell-surface MHC-I
    • Hung CH, Thomas L, Ruby CE, Atkins KM, Morris NP, et al. (2007) HIV-1 Nef assembles a Src family kinase-ZAP-70/Syk-PI3K cascade to downregulate cell-surface MHC-I. Cell Host Microbe 1: 121-133.
    • (2007) Cell Host Microbe , vol.1 , pp. 121-133
    • Hung, C.H.1    Thomas, L.2    Ruby, C.E.3    Atkins, K.M.4    Morris, N.P.5
  • 27
    • 44649173294 scopus 로고    scopus 로고
    • HIV-1 Nef binds PACS-2 to assemble a multikinase cascade that triggers major histocompatibility complex class I (MHC-I) downregulation: Analysis using short interfering RNA and knock-out mice
    • Atkins KM, Thomas L, Youker RT, Harriff MJ, Pissani F, et al. (2008) HIV-1 Nef binds PACS-2 to assemble a multikinase cascade that triggers major histocompatibility complex class I (MHC-I) downregulation: analysis using short interfering RNA and knock-out mice. J Biol Chem 283: 11772-11784.
    • (2008) J Biol Chem , vol.283 , pp. 11772-11784
    • Atkins, K.M.1    Thomas, L.2    Youker, R.T.3    Harriff, M.J.4    Pissani, F.5
  • 28
    • 0037074008 scopus 로고    scopus 로고
    • HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway
    • Blagoveshchenskaya AD, Thomas L, Feliciangeli SF, Hung CH, Thomas G (2002) HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway. Cell 111: 853-866.
    • (2002) Cell , vol.111 , pp. 853-866
    • Blagoveshchenskaya, A.D.1    Thomas, L.2    Feliciangeli, S.F.3    Hung, C.H.4    Thomas, G.5
  • 29
    • 50849129910 scopus 로고    scopus 로고
    • HIV-1 Nef targets MHC-I and CD4 for degradation via a final common beta-COP-dependent pathway in T cells
    • Schaefer MR, Wonderlich ER, Roeth JF, Leonard JA, Collins KL (2008) HIV-1 Nef targets MHC-I and CD4 for degradation via a final common beta-COP-dependent pathway in T cells. PLoS Pathog 4: e1000131.
    • (2008) PLoS Pathog , vol.4 , pp. e1000131
    • Schaefer, M.R.1    Wonderlich, E.R.2    Roeth, J.F.3    Leonard, J.A.4    Collins, K.L.5
  • 30
    • 67449092266 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef protein targets CD4 to the multivesicular body pathway
    • daSilva L, Sougrat R, Burgos P, Janvier K, Mattera R, et al. (2009) Human immunodeficiency virus type 1 Nef protein targets CD4 to the multivesicular body pathway. J Virol 83: 6578-6590.
    • (2009) J Virol , vol.83 , pp. 6578-6590
    • DaSilva, L.1    Sougrat, R.2    Burgos, P.3    Janvier, K.4    Mattera, R.5
  • 31
    • 0028200761 scopus 로고
    • Human immunodeficiency virus type 1 Nef-induced down-modulation of CD4 is due to rapid internalization and degradation of surface CD4
    • Rhee SS, Marsh JW (1994) Human immunodeficiency virus type 1 Nef-induced down-modulation of CD4 is due to rapid internalization and degradation of surface CD4. J Virol 68: 5156-5163.
    • (1994) J Virol , vol.68 , pp. 5156-5163
    • Rhee, S.S.1    Marsh, J.W.2
  • 32
    • 0028216346 scopus 로고
    • The cytoplasmic domain of CD4 is sufficient for its down-regulation from the cell surface by human immunodeficiency virus type 1 Nef
    • Anderson SJ, Lenburg M, Landau NR, Garcia JV (1994) The cytoplasmic domain of CD4 is sufficient for its down-regulation from the cell surface by human immunodeficiency virus type 1 Nef. J Virol 68: 3092-3101.
    • (1994) J Virol , vol.68 , pp. 3092-3101
    • Anderson, S.J.1    Lenburg, M.2    Landau, N.R.3    Garcia, J.V.4
  • 33
    • 0027968920 scopus 로고
    • The simian immunodeficiency virus Nef protein promotes degradation of CD4 in human T cells
    • Sanfridson A, Cullen BR, Doyle C (1994) The simian immunodeficiency virus Nef protein promotes degradation of CD4 in human T cells. J Biol Chem 269: 3917-3920.
    • (1994) J Biol Chem , vol.269 , pp. 3917-3920
    • Sanfridson, A.1    Cullen, B.R.2    Doyle, C.3
  • 34
    • 84907494171 scopus 로고    scopus 로고
    • Interaction of HIV-1 Nef Protein with the Host Protein Alix Promotes Lysosomal Targeting of CD4 Receptor
    • Amorim NA, da Silva EM, de Castro RO, da Silva-Januário ME, Mendonc¸a LM, et al. (2014) Interaction of HIV-1 Nef Protein with the Host Protein Alix Promotes Lysosomal Targeting of CD4 Receptor. J Biol Chem 289: 27744-27756.
    • (2014) J Biol Chem , vol.289 , pp. 27744-27756
    • Amorim, N.A.1    Da Silva, E.M.2    De Castro, R.O.3    Da Silva-Januário, M.E.4    Mendonc¸a, L.M.5
  • 35
    • 20044362379 scopus 로고    scopus 로고
    • Nef-induced alteration of the early/ recycling endosomal compartment correlates with enhancement of HIV-1 infectivity
    • Madrid R, Janvier K, Hitchin D, Day J, Coleman S, et al. (2005) Nef-induced alteration of the early/ recycling endosomal compartment correlates with enhancement of HIV-1 infectivity. J Biol Chem 280: 5032-5044.
    • (2005) J Biol Chem , vol.280 , pp. 5032-5044
    • Madrid, R.1    Janvier, K.2    Hitchin, D.3    Day, J.4    Coleman, S.5
  • 36
    • 0344875506 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1 Nef expression induces intracellular accumulation of multivesicular bodies and major histocompatibility complex class II complexes: Potential role of phosphatidylinositol 3-kinase
    • Stumptner-Cuvelette P, Jouve M, Helft J, Dugast M, Glouzman A, et al. (2003) Human immunodeficiency virus-1 Nef expression induces intracellular accumulation of multivesicular bodies and major histocompatibility complex class II complexes: potential role of phosphatidylinositol 3-kinase. Mol Biol Cell 14: 4857-4870.
    • (2003) Mol Biol Cell , vol.14 , pp. 4857-4870
    • Stumptner-Cuvelette, P.1    Jouve, M.2    Helft, J.3    Dugast, M.4    Glouzman, A.5
  • 37
    • 33746907799 scopus 로고    scopus 로고
    • Interactions between Nef and AIP1 proliferate multivesicular bodies and facilitate egress of HIV-1
    • Costa L, Chen N, Lopes A, Aguiar R, Tanuri A, et al. (2006) Interactions between Nef and AIP1 proliferate multivesicular bodies and facilitate egress of HIV-1. Retrovirology 3: 33.
    • (2006) Retrovirology , vol.3 , pp. 33
    • Costa, L.1    Chen, N.2    Lopes, A.3    Aguiar, R.4    Tanuri, A.5
  • 38
    • 0031034161 scopus 로고    scopus 로고
    • Nef proteins encoded by human and simian immunodeficiency viruses induce the accumulation of endosomes and lysosomes in human T cells
    • Sanfridson A, Hester S, Doyle C (1997) Nef proteins encoded by human and simian immunodeficiency viruses induce the accumulation of endosomes and lysosomes in human T cells. Proc Natl Acad Sci U S A 94: 873-878.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 873-878
    • Sanfridson, A.1    Hester, S.2    Doyle, C.3
  • 39
    • 71849085384 scopus 로고    scopus 로고
    • HIV Nef is secreted in exosomes and triggers apoptosis in bystander CD4+ T cells
    • Lenassi M, Cagney G, Liao M, Vaupotic T, Bartholomeeusen K, et al. (2010) HIV Nef is secreted in exosomes and triggers apoptosis in bystander CD4+ T cells. Traffic 11: 110-122.
    • (2010) Traffic , vol.11 , pp. 110-122
    • Lenassi, M.1    Cagney, G.2    Liao, M.3    Vaupotic, T.4    Bartholomeeusen, K.5
  • 40
    • 69949128211 scopus 로고    scopus 로고
    • Massive secretion by T cells is caused by HIV Nef in infected cells and by Nef transfer to bystander cells
    • Muratori C, Cavallin LE, Krätzel K, Tinari A, De Milito A, et al. (2009) Massive secretion by T cells is caused by HIV Nef in infected cells and by Nef transfer to bystander cells. Cell Host Microbe 6: 218-230.
    • (2009) Cell Host Microbe , vol.6 , pp. 218-230
    • Muratori, C.1    Cavallin, L.E.2    Krätzel, K.3    Tinari, A.4    De Milito, A.5
  • 41
    • 43149120419 scopus 로고    scopus 로고
    • Exosome function: From tumor immunology to pathogen biology
    • Schorey JS, Bhatnagar S (2008) Exosome function: from tumor immunology to pathogen biology. Traffic 9: 871-881.
    • (2008) Traffic , vol.9 , pp. 871-881
    • Schorey, J.S.1    Bhatnagar, S.2
  • 42
    • 68849129712 scopus 로고    scopus 로고
    • Membrane vesicles as conveyors of immune responses
    • Théry C, Ostrowski M, Segura E (2009) Membrane vesicles as conveyors of immune responses. Nat Rev Immunol 9: 581-593.
    • (2009) Nat Rev Immunol , vol.9 , pp. 581-593
    • Théry, C.1    Ostrowski, M.2    Segura, E.3
  • 43
    • 40149109751 scopus 로고    scopus 로고
    • The low affinity IgG receptor Fc gamma RIIB contributes to the binding of the mast cell specific antibody, mAb BGD6
    • Guiraldelli MF, Berenstein EH, Grodzki AC, Siraganian RP, Jamur MC, et al. (2008) The low affinity IgG receptor Fc gamma RIIB contributes to the binding of the mast cell specific antibody, mAb BGD6. Mol Immunol 45: 2411-2418.
    • (2008) Mol Immunol , vol.45 , pp. 2411-2418
    • Guiraldelli, M.F.1    Berenstein, E.H.2    Grodzki, A.C.3    Siraganian, R.P.4    Jamur, M.C.5
  • 44
    • 0022580049 scopus 로고
    • Induction of HTLV-III/LAV from a nonvirus-producing T-cell line: Implications for latency
    • Folks T, Powell DM, Lightfoote MM, Benn S, Martin MA, et al. (1986) Induction of HTLV-III/LAV from a nonvirus-producing T-cell line: implications for latency. Science 231: 600-602.
    • (1986) Science , vol.231 , pp. 600-602
    • Folks, T.1    Powell, D.M.2    Lightfoote, M.M.3    Benn, S.4    Martin, M.A.5
  • 45
    • 0038782491 scopus 로고
    • Characterization of a continuous Tcell line susceptible to the cytopathic effects of the acquired immunodeficiency syndrome (AIDS)- associated retrovirus
    • Folks T, Benn S, Rabson A, Theodore T, Hoggan MD, et al. (1985) Characterization of a continuous Tcell line susceptible to the cytopathic effects of the acquired immunodeficiency syndrome (AIDS)- associated retrovirus. Proc Natl Acad Sci U S A 82: 4539-4543.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 4539-4543
    • Folks, T.1    Benn, S.2    Rabson, A.3    Theodore, T.4    Hoggan, M.D.5
  • 46
    • 0024508058 scopus 로고
    • HIV with reduced sensitivity to zidovudine (AZT) isolated during prolonged therapy
    • Larder BA, Darby G, Richman DD (1989) HIV with reduced sensitivity to zidovudine (AZT) isolated during prolonged therapy. Science 243: 1731-1734.
    • (1989) Science , vol.243 , pp. 1731-1734
    • Larder, B.A.1    Darby, G.2    Richman, D.D.3
  • 47
    • 0022404296 scopus 로고
    • Infection of HTLV-III/LAV in HTLV-I-carrying cells MT-2 and MT-4 and application in a plaque assay
    • Harada S, Koyanagi Y, Yamamoto N (1985) Infection of HTLV-III/LAV in HTLV-I-carrying cells MT-2 and MT-4 and application in a plaque assay. Science 229: 563-566.
    • (1985) Science , vol.229 , pp. 563-566
    • Harada, S.1    Koyanagi, Y.2    Yamamoto, N.3
  • 50
    • 43249109372 scopus 로고    scopus 로고
    • Isolation and characterization of exosomes from cell culture supernatants and biological fluids
    • Chapter 3: Unit 3.22
    • Théry C, Amigorena S, Raposo G, Clayton A (2006) Isolation and characterization of exosomes from cell culture supernatants and biological fluids. Curr Protoc Cell Biol Chapter 3: Unit 3.22.
    • (2006) Curr Protoc Cell Biol
    • Théry, C.1    Amigorena, S.2    Raposo, G.3    Clayton, A.4
  • 51
    • 52649114611 scopus 로고
    • The use of lead citrate at high pH as an electron-opaque stain in electron microscopy
    • Reynolds ES (1963) The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol 17: 208-212.
    • (1963) J Cell Biol , vol.17 , pp. 208-212
    • Reynolds, E.S.1
  • 52
    • 0033145510 scopus 로고    scopus 로고
    • Late endosomal membranes rich in lysobisphosphatidic acid regulate cholesterol transport
    • Kobayashi T, Beuchat MH, Lindsay M, Frias S, Palmiter RD, et al. (1999) Late endosomal membranes rich in lysobisphosphatidic acid regulate cholesterol transport. Nat Cell Biol 1: 113-118.
    • (1999) Nat Cell Biol , vol.1 , pp. 113-118
    • Kobayashi, T.1    Beuchat, M.H.2    Lindsay, M.3    Frias, S.4    Palmiter, R.D.5
  • 53
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
    • Kobayashi T, Stang E, Fang KS, de Moerloose P, Parton RG, et al. (1998) A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature 392: 193-197.
    • (1998) Nature , vol.392 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    Fang, K.S.3    De Moerloose, P.4    Parton, R.G.5
  • 54
    • 84890875112 scopus 로고    scopus 로고
    • ALIX and the multivesicular endosome: ALIX in Wonderland
    • Bissig C, Gruenberg J (2014) ALIX and the multivesicular endosome: ALIX in Wonderland. Trends Cell Biol 24: 19-25.
    • (2014) Trends Cell Biol , vol.24 , pp. 19-25
    • Bissig, C.1    Gruenberg, J.2
  • 55
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann DJ, Odorizzi G, Emr SD (2002) Receptor downregulation and multivesicular-body sorting. Nat Rev Mol Cell Biol 3: 893-905.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 56
    • 39149132089 scopus 로고    scopus 로고
    • ESCRTcomplexes and the biogenesis of multivesicular bodies
    • Hurley JH (2008) ESCRTcomplexes and the biogenesis of multivesicular bodies. Curr Opin Cell Biol 20: 4-11.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 4-11
    • Hurley, J.H.1
  • 57
    • 9144273746 scopus 로고    scopus 로고
    • Role of LBPA and Alix in multivesicular liposome formation and endosome organization
    • Matsuo H, Chevallier J, Mayran N, Le Blanc I, Ferguson C, et al. (2004) Role of LBPA and Alix in multivesicular liposome formation and endosome organization. Science 303: 531-534.
    • (2004) Science , vol.303 , pp. 531-534
    • Matsuo, H.1    Chevallier, J.2    Mayran, N.3    Le Blanc, I.4    Ferguson, C.5
  • 58
    • 70350449455 scopus 로고    scopus 로고
    • ExoCarta: A compendium of exosomal proteins and RNA
    • Mathivanan S, Simpson RJ (2009) ExoCarta: A compendium of exosomal proteins and RNA. Proteomics 9: 4997-5000.
    • (2009) Proteomics , vol.9 , pp. 4997-5000
    • Mathivanan, S.1    Simpson, R.J.2
  • 59
    • 84867653559 scopus 로고    scopus 로고
    • Short-range exosomal transfer of viral RNA from infected cells to plasmacytoid dendritic cells triggers innate immunity
    • Dreux M, Garaigorta U, Boyd B, Décembre E, Chung J, et al. (2012) Short-range exosomal transfer of viral RNA from infected cells to plasmacytoid dendritic cells triggers innate immunity. Cell Host Microbe 12: 558-570.
    • (2012) Cell Host Microbe , vol.12 , pp. 558-570
    • Dreux, M.1    Garaigorta, U.2    Boyd, B.3    Décembre, E.4    Chung, J.5
  • 60
    • 77957195392 scopus 로고    scopus 로고
    • Exosome release of b-catenin: A novel mechanism that antagonizes Wnt signaling
    • Chairoungdua A, Smith DL, Pochard P, Hull M, Caplan MJ (2010) Exosome release of b-catenin: a novel mechanism that antagonizes Wnt signaling. J Cell Biol 190: 1079-1091.
    • (2010) J Cell Biol , vol.190 , pp. 1079-1091
    • Chairoungdua, A.1    Smith, D.L.2    Pochard, P.3    Hull, M.4    Caplan, M.J.5
  • 61
    • 77952920881 scopus 로고    scopus 로고
    • Secretory mechanisms and intercellular transfer of microRNAs in living cells
    • Kosaka N, Iguchi H, Yoshioka Y, Takeshita F, Matsuki Y, et al. (2010) Secretory mechanisms and intercellular transfer of microRNAs in living cells. J Biol Chem 285: 17442-17452.
    • (2010) J Biol Chem , vol.285 , pp. 17442-17452
    • Kosaka, N.1    Iguchi, H.2    Yoshioka, Y.3    Takeshita, F.4    Matsuki, Y.5
  • 62
    • 40049112564 scopus 로고    scopus 로고
    • Ceramide triggers budding of exosome vesicles into multivesicular endosomes
    • Trajkovic K, Hsu C, Chiantia S, Rajendran L, Wenzel D, et al. (2008) Ceramide triggers budding of exosome vesicles into multivesicular endosomes. Science 319: 1244-1247.
    • (2008) Science , vol.319 , pp. 1244-1247
    • Trajkovic, K.1    Hsu, C.2    Chiantia, S.3    Rajendran, L.4    Wenzel, D.5
  • 63
    • 84859499570 scopus 로고    scopus 로고
    • Sphingolipid-modulated exosome secretion promotes clearance of amyloid-b by microglia
    • Yuyama K, Sun H, Mitsutake S, Igarashi Y (2012) Sphingolipid-modulated exosome secretion promotes clearance of amyloid-b by microglia. J Biol Chem 287: 10977-10989.
    • (2012) J Biol Chem , vol.287 , pp. 10977-10989
    • Yuyama, K.1    Sun, H.2    Mitsutake, S.3    Igarashi, Y.4
  • 64
    • 80052161955 scopus 로고    scopus 로고
    • HIV-Nef and AIDS pathogenesis: Are we barking up the wrong tree?
    • Baur AS (2011) HIV-Nef and AIDS pathogenesis: are we barking up the wrong tree? Trends Microbiol 19: 435-440.
    • (2011) Trends Microbiol , vol.19 , pp. 435-440
    • Baur, A.S.1
  • 65
    • 33644927263 scopus 로고    scopus 로고
    • Exosomes and HIV Gag bud from endosome-like domains of the T cell plasma membrane
    • Booth AM, Fang Y, Fallon JK, Yang JM, Hildreth JE, et al. (2006) Exosomes and HIV Gag bud from endosome-like domains of the T cell plasma membrane. J Cell Biol 172: 923-935.
    • (2006) J Cell Biol , vol.172 , pp. 923-935
    • Booth, A.M.1    Fang, Y.2    Fallon, J.K.3    Yang, J.M.4    Hildreth, J.E.5
  • 66
    • 0033578072 scopus 로고    scopus 로고
    • Cell-surface expression of CD4 reduces HIV-1 infectivity by blocking Env incorporation in a Nef- and Vpu-inhibitable manner
    • Lama J, Mangasarian A, Trono D (1999) Cell-surface expression of CD4 reduces HIV-1 infectivity by blocking Env incorporation in a Nef- and Vpu-inhibitable manner. Curr Biol 9: 622-631.
    • (1999) Curr Biol , vol.9 , pp. 622-631
    • Lama, J.1    Mangasarian, A.2    Trono, D.3
  • 67
    • 0026096522 scopus 로고
    • Direct measurement of soluble CD4 binding to human immunodeficiency virus type 1 virions: Gp120 dissociation and its implications for viruscell binding and fusion reactions and their neutralization by soluble CD4
    • Moore JP, McKeating JA, Norton WA, Sattentau QJ (1991) Direct measurement of soluble CD4 binding to human immunodeficiency virus type 1 virions: gp120 dissociation and its implications for viruscell binding and fusion reactions and their neutralization by soluble CD4. J Virol 65: 1133-1140.
    • (1991) J Virol , vol.65 , pp. 1133-1140
    • Moore, J.P.1    McKeating, J.A.2    Norton, W.A.3    Sattentau, Q.J.4
  • 68
    • 0027399209 scopus 로고
    • Two mechanisms of soluble CD4 (sCD4)-mediated inhibition of human immunodeficiency virus type 1 (HIV-1) infectivity and their relation to primary HIV-1 isolates with reduced sensitivity to sCD4
    • Orloff SL, Kennedy MS, Belperron AA, Maddon PJ, McDougal JS (1993) Two mechanisms of soluble CD4 (sCD4)-mediated inhibition of human immunodeficiency virus type 1 (HIV-1) infectivity and their relation to primary HIV-1 isolates with reduced sensitivity to sCD4. J Virol 67: 1461-1471.
    • (1993) J Virol , vol.67 , pp. 1461-1471
    • Orloff, S.L.1    Kennedy, M.S.2    Belperron, A.A.3    Maddon, P.J.4    McDougal, J.S.5
  • 70
    • 31144445302 scopus 로고    scopus 로고
    • Pregnancy-associated exosomes and their modulation of T cell signaling
    • Taylor DD, Akyol S, Gercel-Taylor C (2006) Pregnancy-associated exosomes and their modulation of T cell signaling. J Immunol 176: 1534-1542.
    • (2006) J Immunol , vol.176 , pp. 1534-1542
    • Taylor, D.D.1    Akyol, S.2    Gercel-Taylor, C.3
  • 71
    • 84901650316 scopus 로고    scopus 로고
    • T-cells play the classics with a different spin
    • Dustin ML (2014) T-cells play the classics with a different spin. Mol Biol Cell 25: 1699-1703.
    • (2014) Mol Biol Cell , vol.25 , pp. 1699-1703
    • Dustin, M.L.1
  • 72
    • 84895891752 scopus 로고    scopus 로고
    • Polarized release of T-cell-receptor-enriched microvesicles at the immunological synapse
    • Choudhuri K, Llodrá J, Roth EW, Tsai J, Gordo S, et al. (2014) Polarized release of T-cell-receptor-enriched microvesicles at the immunological synapse. Nature 507: 118-123.
    • (2014) Nature , vol.507 , pp. 118-123
    • Choudhuri, K.1    Llodrá, J.2    Roth, E.W.3    Tsai, J.4    Gordo, S.5
  • 73
    • 0032556872 scopus 로고    scopus 로고
    • HIV-1 Nef protein protects infected primary cells against killing by cytotoxic T lymphocytes
    • Collins K, Chen B, Kalams S, Walker B, Baltimore D (1998) HIV-1 Nef protein protects infected primary cells against killing by cytotoxic T lymphocytes. Nature 391: 397-401.
    • (1998) Nature , vol.391 , pp. 397-401
    • Collins, K.1    Chen, B.2    Kalams, S.3    Walker, B.4    Baltimore, D.5
  • 74
    • 84892175747 scopus 로고    scopus 로고
    • Exosomes from breast milk inhibit HIV-1 infection of dendritic cells and subsequent viral transfer to CD4+ T cells
    • Näslund TI, Paquin-Proulx D, Paredes PT, Vallhov H, Sandberg JK, et al. (2014) Exosomes from breast milk inhibit HIV-1 infection of dendritic cells and subsequent viral transfer to CD4+ T cells. AIDS 28: 171-180.
    • (2014) AIDS , vol.28 , pp. 171-180
    • Näslund, T.I.1    Paquin-Proulx, D.2    Paredes, P.T.3    Vallhov, H.4    Sandberg, J.K.5


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