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Volumn 107, Issue Part A, 2014, Pages 22-27

Membrane organization of virus and target cell plays a role in HIV entry

Author keywords

HIV; Lipids; Membrane dynamics

Indexed keywords

CD4 ANTIGEN RECEPTOR; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR4; RECEPTOR; UNCLASSIFIED DRUG; CCR5 PROTEIN, HUMAN; CD4 ANTIGEN; GLYCOPROTEIN GP 120; GP120 PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; PROTEIN BINDING;

EID: 84915827879     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2014.08.015     Document Type: Short Survey
Times cited : (13)

References (92)
  • 1
    • 0034848936 scopus 로고    scopus 로고
    • Syndecans serve as attachment receptors for human immunodeficiency virus type 1 on macrophages
    • A.C. Saphire, M.D. Bobardt, Z. Zhang, G. David, P.A. Gallay, Syndecans serve as attachment receptors for human immunodeficiency virus type 1 on macrophages, J. Virol. 75 (2001) 9187-9200.
    • (2001) J. Virol. , vol.75 , pp. 9187-9200
    • Saphire, A.C.1    Bobardt, M.D.2    Zhang, Z.3    David, G.4    Gallay, P.A.5
  • 3
    • 0028293288 scopus 로고
    • Differences in CD4 dependence for infectivity of laboratory-adapted and primary patient isolates of human immunodeficiency virus type 1
    • D. Kabat, S.L. Kozak, K. Wehrly, B. Chesebro, Differences in CD4 dependence for infectivity of laboratory-adapted and primary patient isolates of human immunodeficiency virus type 1, J. Virol. 68 (1994) 2570-2577.
    • (1994) J. Virol. , vol.68 , pp. 2570-2577
    • Kabat, D.1    Kozak, S.L.2    Wehrly, K.3    Chesebro, B.4
  • 4
    • 0031031452 scopus 로고    scopus 로고
    • CD4, CXCR-4, and CCR-5 dependencies for infections by primary patient and laboratory-adapted isolates of human immunodeficiency virus type 1
    • S.L. Kozak, et al., CD4, CXCR-4, and CCR-5 dependencies for infections by primary patient and laboratory-adapted isolates of human immunodeficiency virus type 1, J. Virol. 71 (1997) 873-882.
    • (1997) J. Virol. , vol.71 , pp. 873-882
    • Kozak, S.L.1
  • 5
    • 0031954686 scopus 로고    scopus 로고
    • Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1
    • E.J. Platt, K. Wehrly, S.E. Kuhmann, B. Chesebro, D. Kabat, Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1, J. Virol. 72 (1998) 2855-2864.
    • (1998) J. Virol. , vol.72 , pp. 2855-2864
    • Platt, E.J.1    Wehrly, K.2    Kuhmann, S.E.3    Chesebro, B.4    Kabat, D.5
  • 6
    • 0024427545 scopus 로고
    • Variations in CD4 expression by human monocytes and macrophages and their relationships to infection with the human immunodeficiency virus
    • F. Kazazi, J.M. Mathijs, P. Foley, A.L. Cunningham, Variations in CD4 expression by human monocytes and macrophages and their relationships to infection with the human immunodeficiency virus, J. Gen. Virol. 70 (Pt 10) (1989) 2661-2672.
    • (1989) J. Gen. Virol. , vol.70 , pp. 2661-2672
    • Kazazi, F.1    Mathijs, J.M.2    Foley, P.3    Cunningham, A.L.4
  • 7
    • 79251519651 scopus 로고    scopus 로고
    • Asymmetric HIV-1 co-receptor use and replication in CD4(+) T lymphocytes
    • S.A. Mariani, E. Vicenzi, G. Poli, Asymmetric HIV-1 co-receptor use and replication in CD4(+) T lymphocytes, J. Transl. Med. 9 (Suppl. 1) (2011) S8.
    • (2011) J. Transl. Med. , vol.9 , pp. S8
    • Mariani, S.A.1    Vicenzi, E.2    Poli, G.3
  • 8
    • 84896055631 scopus 로고    scopus 로고
    • Is the fluid mosaic (and the accompanying raft hypothesis) a suitable model to describe fundamental features of biological membranes? What may be missing?
    • L.A. Bagatolli, O.G. Mouritsen, Is the fluid mosaic (and the accompanying raft hypothesis) a suitable model to describe fundamental features of biological membranes? What may be missing? Front. Plant Sci. 4 (2013) 457.
    • (2013) Front. Plant Sci. , vol.4 , pp. 457
    • Bagatolli, L.A.1    Mouritsen, O.G.2
  • 9
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • D.M. Engelman, Membranes are more mosaic than fluid, Nature 438 (2005) 578-580.
    • (2005) Nature , vol.438 , pp. 578-580
    • Engelman, D.M.1
  • 10
    • 0032877355 scopus 로고    scopus 로고
    • Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions?
    • F. Dumas, M.C. Lebrun, J.F. Tocanne, Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions? FEBS Lett. 458 (1999) 271-277.
    • (1999) FEBS Lett. , vol.458 , pp. 271-277
    • Dumas, F.1    Lebrun, M.C.2    Tocanne, J.F.3
  • 11
    • 36849019932 scopus 로고    scopus 로고
    • CD4 interacts constitutively with multiple CCR5 at the plasma membrane of living cells. A fluorescence recovery after photobleaching at variable radii approach
    • A.M. Baker, et al., CD4 interacts constitutively with multiple CCR5 at the plasma membrane of living cells. A fluorescence recovery after photobleaching at variable radii approach, J. Biol. Chem. 282 (2007) 35163-35168.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35163-35168
    • Baker, A.M.1
  • 12
    • 84855780534 scopus 로고    scopus 로고
    • Single particle tracking reveals two distinct environments for CD4 receptors at the surface of living T lymphocytes
    • P. Mascalchi, A.S. Lamort, L. Salomé, F. Dumas, Single particle tracking reveals two distinct environments for CD4 receptors at the surface of living T lymphocytes, Biochem. Biophys. Res. Commun. 417 (2012) 409-413.
    • (2012) Biochem. Biophys. Res. Commun. , vol.417 , pp. 409-413
    • Mascalchi, P.1    Lamort, A.S.2    Salomé, L.3    Dumas, F.4
  • 13
    • 0035082676 scopus 로고    scopus 로고
    • CCR5, CXCR4, and CD4 are clustered and closely apposed on microvilli of human macrophages and T cells
    • I.I. Singer, et al., CCR5, CXCR4, and CD4 are clustered and closely apposed on microvilli of human macrophages and T cells, J. Virol. 75 (2001) 3779-3790.
    • (2001) J. Virol. , vol.75 , pp. 3779-3790
    • Singer, I.I.1
  • 14
    • 0037474303 scopus 로고    scopus 로고
    • HIV-1 entry into T-cells is not dependent on CD4 and CCR5 localization to sphingolipid-enriched, detergent-resistant, raft membrane domains
    • Y. Percherancier, et al., HIV-1 entry into T-cells is not dependent on CD4 and CCR5 localization to sphingolipid-enriched, detergent-resistant, raft membrane domains, J. Biol. Chem. 278 (2003) 3153-3161.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3153-3161
    • Percherancier, Y.1
  • 15
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • D. Lingwood, K. Simons, Lipid rafts as a membrane-organizing principle, Science 327 (2010) 46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 16
    • 33746085241 scopus 로고    scopus 로고
    • Rafts defined: A report on the keystone symposium on lipid rafts and cell function
    • L.J. Pike, Rafts defined: a report on the keystone symposium on lipid rafts and cell function, J. Lipid Res. 47 (2006) 1597-1598.
    • (2006) J. Lipid Res. , vol.47 , pp. 1597-1598
    • Pike, L.J.1
  • 17
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons, E. Ikonen, Functional rafts in cell membranes, Nature 387 (1997) 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 18
    • 79251568648 scopus 로고    scopus 로고
    • Measuring the strength of interaction between the ebola fusion peptide and lipid rafts: Implications for membrane fusion and virus infection
    • M.S. Freitas, et al., Measuring the strength of interaction between the ebola fusion peptide and lipid rafts: implications for membrane fusion and virus infection, PLoS One 6 (2011) e15756.
    • (2011) PLoS One , vol.6 , pp. e15756
    • Freitas, M.S.1
  • 19
    • 0042890360 scopus 로고    scopus 로고
    • Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry
    • F.C. Bender, et al., Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry, J. Virol. 77 (2003) 9542-9552.
    • (2003) J. Virol. , vol.77 , pp. 9542-9552
    • Bender, F.C.1
  • 20
    • 78650663541 scopus 로고    scopus 로고
    • {alpha}V{beta}3-integrin routes herpes simplex virus to an entry pathway dependent on cholesterol-rich lipid rafts and dynamin2
    • T. Gianni, V. Gatta, G. Campadelli-Fiume, {alpha}V{beta}3-integrin routes herpes simplex virus to an entry pathway dependent on cholesterol-rich lipid rafts and dynamin2, Proc. Natl. Acad. Sci. U. S. A. 107 (2010) 22260-22265.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 22260-22265
    • Gianni, T.1    Gatta, V.2    Campadelli-Fiume, G.3
  • 21
    • 22544463108 scopus 로고    scopus 로고
    • Murine coronavirus requires lipid rafts for virus entry and cell-cell fusion but not for virus release
    • K.S. Choi, H. Aizaki, M.M.C. Lai, Murine coronavirus requires lipid rafts for virus entry and cell-cell fusion but not for virus release, J. Virol. 79 (2005) 9862-9871.
    • (2005) J. Virol. , vol.79 , pp. 9862-9871
    • Choi, K.S.1    Aizaki, H.2    Lai, M.M.C.3
  • 22
    • 0036148171 scopus 로고    scopus 로고
    • Segregation of CD4 and CXCR4 into distinct lipid microdomains in T lymphocytes suggests a mechanism for membrane destabilization by human immunodeficiency virus
    • S.L. Kozak, J.M. Heard, D. Kabat, Segregation of CD4 and CXCR4 into distinct lipid microdomains in T lymphocytes suggests a mechanism for membrane destabilization by human immunodeficiency virus, J. Virol. 76 (2002) 1802-1815.
    • (2002) J. Virol. , vol.76 , pp. 1802-1815
    • Kozak, S.L.1    Heard, J.M.2    Kabat, D.3
  • 23
    • 0034834457 scopus 로고    scopus 로고
    • Lipid rafts and HIV pathogenesis: Host membrane cholesterol is required for infection by HIV type 1
    • Z. Liao, L.M. Cimakasky, R. Hampton, D.H. Nguyen, J.E. Hildreth, Lipid rafts and HIV pathogenesis: host membrane cholesterol is required for infection by HIV type 1, AIDS Res. Hum. Retroviruses 17 (2001) 1009-1019.
    • (2001) AIDS Res. Hum. Retroviruses , vol.17 , pp. 1009-1019
    • Liao, Z.1    Cimakasky, L.M.2    Hampton, R.3    Nguyen, D.H.4    Hildreth, J.E.5
  • 24
    • 0036239931 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 uses lipid raft-colocalized CD4 and chemokine receptors for productive entry into CD4(+) T cells
    • W. Popik, T.M. Alce, W.C. Au, Human immunodeficiency virus type 1 uses lipid raft-colocalized CD4 and chemokine receptors for productive entry into CD4(+) T cells, J. Virol. 76 (2002) 4709-4722.
    • (2002) J. Virol. , vol.76 , pp. 4709-4722
    • Popik, W.1    Alce, T.M.2    Au, W.C.3
  • 25
    • 0033934279 scopus 로고    scopus 로고
    • Glycosphingolipids promote entry of a broad range of human immunodeficiency virus type 1 isolates into cell lines expressing CD4, CXCR4, and/or CCR5
    • P. Hug, et al., Glycosphingolipids promote entry of a broad range of human immunodeficiency virus type 1 isolates into cell lines expressing CD4, CXCR4, and/or CCR5, J. Virol. 74 (2000) 6377-6385.
    • (2000) J. Virol. , vol.74 , pp. 6377-6385
    • Hug, P.1
  • 26
    • 0037025989 scopus 로고    scopus 로고
    • Blocking of HIV-1 infection by targeting CD4 to nonraft membrane domains
    • G. Del Real, et al., Blocking of HIV-1 infection by targeting CD4 to nonraft membrane domains, J. Exp. Med. 196 (2002) 293-301.
    • (2002) J. Exp. Med. , vol.196 , pp. 293-301
    • Del Real, G.1
  • 27
    • 0347052860 scopus 로고    scopus 로고
    • CD4 receptor localized to non-raft membrane microdomains supports HIV-1 entry identification of a novel raft localization marker in CD4
    • W. Popik, T.M. Alce, CD4 receptor localized to non-raft membrane microdomains supports HIV-1 entry identification of a novel raft localization marker in CD4, J. Biol. Chem. 279 (2004) 704-712.
    • (2004) J. Biol. Chem. , vol.279 , pp. 704-712
    • Popik, W.1    Alce, T.M.2
  • 28
    • 37549047226 scopus 로고    scopus 로고
    • Restricted lateral mobility of plasma membrane CD4 impairs HIV-1 envelope glycoprotein mediated fusion
    • S.S. Rawat, et al., Restricted lateral mobility of plasma membrane CD4 impairs HIV-1 envelope glycoprotein mediated fusion, Mol. Membr. Biol. 25 (2008) 83-94.
    • (2008) Mol. Membr. Biol. , vol.25 , pp. 83-94
    • Rawat, S.S.1
  • 29
    • 22944446447 scopus 로고    scopus 로고
    • Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells
    • M.J. Lehmann, N.M. Sherer, C.B. Marks, M. Pypaert, W. Mothes, Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells, J. Cell. Biol. 170 (2005) 317-325.
    • (2005) J. Cell. Biol. , vol.170 , pp. 317-325
    • Lehmann, M.J.1    Sherer, N.M.2    Marks, C.B.3    Pypaert, M.4    Mothes, W.5
  • 30
    • 0042376485 scopus 로고    scopus 로고
    • A new classification for HIV-1
    • E.A. Berger, et al., A new classification for HIV-1, Nature 391 (1998) 240.
    • (1998) Nature , vol.391 , pp. 240
    • Berger, E.A.1
  • 31
    • 12644288298 scopus 로고    scopus 로고
    • Evolution of HIV-1 coreceptor usage through interactions with distinct CCR5 and CXCR4 domains
    • Z. Lu, et al., Evolution of HIV-1 coreceptor usage through interactions with distinct CCR5 and CXCR4 domains, Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 6426-6431.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 6426-6431
    • Lu, Z.1
  • 33
    • 0033941573 scopus 로고    scopus 로고
    • Cooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1
    • S.E. Kuhmann, E.J. Platt, S.L. Kozak, D. Kabat, Cooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1, J. Virol. 74 (2000) 7005-7015.
    • (2000) J. Virol. , vol.74 , pp. 7005-7015
    • Kuhmann, S.E.1    Platt, E.J.2    Kozak, S.L.3    Kabat, D.4
  • 34
    • 0025315836 scopus 로고
    • HIV requires multiple gp120 molecules for CD4-mediated infection
    • S.P. Layne, M.J. Merges, M. Dembo, J.L. Spouge, P.L. Nara, HIV requires multiple gp120 molecules for CD4-mediated infection, Nature 346 (1990) 277-279.
    • (1990) Nature , vol.346 , pp. 277-279
    • Layne, S.P.1    Merges, M.J.2    Dembo, M.3    Spouge, J.L.4    Nara, P.L.5
  • 35
    • 79957590948 scopus 로고    scopus 로고
    • Estimating the threshold surface density of Gp120-CCR5 complexes necessary for HIV-1 envelope-mediated cell-cell fusion
    • S.N. Mulampaka, N.M. Dixit, Estimating the threshold surface density of Gp120-CCR5 complexes necessary for HIV-1 envelope-mediated cell-cell fusion, PLoS One 6 (2011) e19941.
    • (2011) PLoS One , vol.6 , pp. e19941
    • Mulampaka, S.N.1    Dixit, N.M.2
  • 36
    • 34249672782 scopus 로고    scopus 로고
    • Electron tomography of the contact between T cells and SIV/HIV-1: Implications for viral entry
    • R. Sougrat, et al., Electron tomography of the contact between T cells and SIV/HIV-1: implications for viral entry, PLoS Pathog. 3 (2007) e63.
    • (2007) PLoS Pathog. , vol.3 , pp. e63
    • Sougrat, R.1
  • 37
    • 27744491701 scopus 로고    scopus 로고
    • Single-Molecule analysis of human immunodeficiency virus type 1 gp120-receptor interactions in living cells
    • M.I. Chang, P. Panorchan, T.M. Dobrowsky, Y. Tseng, D. Wirtz, Single-Molecule analysis of human immunodeficiency virus type 1 gp120-receptor interactions in living cells, J. Virol. 79 (2005) 14748-14755.
    • (2005) J. Virol. , vol.79 , pp. 14748-14755
    • Chang, M.I.1    Panorchan, P.2    Dobrowsky, T.M.3    Tseng, Y.4    Wirtz, D.5
  • 38
    • 47049113731 scopus 로고    scopus 로고
    • Monitoring early fusion dynamics of human immunodeficiency virus type 1 at single-molecule resolution
    • T.M. Dobrowsky, Y. Zhou, S.X. Sun, R.F. Siliciano, D. Wirtz, Monitoring early fusion dynamics of human immunodeficiency virus type 1 at single-molecule resolution, J. Virol. 82 (2008) 7022-7033.
    • (2008) J. Virol. , vol.82 , pp. 7022-7033
    • Dobrowsky, T.M.1    Zhou, Y.2    Sun, S.X.3    Siliciano, R.F.4    Wirtz, D.5
  • 39
    • 13044317266 scopus 로고    scopus 로고
    • Constitutive cell surface association between CD4 and CCR5
    • X. Xiao, et al., Constitutive cell surface association between CD4 and CCR5, Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 7496-7501.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7496-7501
    • Xiao, X.1
  • 40
    • 33747875258 scopus 로고    scopus 로고
    • Specific interaction of CXCR4 with CD4 and CD8alpha: Functional analysis of the CD4/CXCR4 interaction in the context of HIV-1 envelope glycoprotein-mediated membrane fusion
    • S. Basmaciogullari, B. Pacheco, S. Bour, J. Sodroski, Specific interaction of CXCR4 with CD4 and CD8alpha: functional analysis of the CD4/CXCR4 interaction in the context of HIV-1 envelope glycoprotein-mediated membrane fusion, Virology 353 (2006) 52-67.
    • (2006) Virology , vol.353 , pp. 52-67
    • Basmaciogullari, S.1    Pacheco, B.2    Bour, S.3    Sodroski, J.4
  • 41
    • 33846026369 scopus 로고    scopus 로고
    • CD4 and CCR5 constitutively interact at the plasma membrane of living cells: A confocal fluorescence resonance energy transfer-based approach
    • G. Gaibelet, et al., CD4 and CCR5 constitutively interact at the plasma membrane of living cells: a confocal fluorescence resonance energy transfer-based approach, J. Biol. Chem. 281 (2006) 37921-37929.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37921-37929
    • Gaibelet, G.1
  • 42
    • 4143105734 scopus 로고    scopus 로고
    • Mobility of the human immunode ficiency virus (HIV) receptor CD4 and coreceptor CCR5 in living cells: Implications for HIV fusion and entry events
    • C.M. Steffens, T.J. Hope, Mobility of the human immunode ficiency virus (HIV) receptor CD4 and coreceptor CCR5 in living cells: implications for HIV fusion and entry events, J. Virol. 78 (2004) 9573-9578.
    • (2004) J. Virol. , vol.78 , pp. 9573-9578
    • Steffens, C.M.1    Hope, T.J.2
  • 43
    • 84883184655 scopus 로고    scopus 로고
    • The puzzling role of CXCR4 in human immunodeficiency virus infection
    • E. Vicenzi, P. Liò, G. Poli, The puzzling role of CXCR4 in human immunodeficiency virus infection, Theranostics 3 (2013) 18-25.
    • (2013) Theranostics , vol.3 , pp. 18-25
    • Vicenzi, E.1    Liò, P.2    Poli, G.3
  • 44
    • 84872968392 scopus 로고    scopus 로고
    • CXCR4-tropic, but not CCR5-tropic, human immunodeficiency virus infection is inhibited by the lipid raft-associated factors, acyclic retinoid analogs, and cholera toxin B subunit
    • H. Kamiyama, et al., CXCR4-tropic, but not CCR5-tropic, human immunodeficiency virus infection is inhibited by the lipid raft-associated factors, acyclic retinoid analogs, and cholera toxin B subunit, AIDS Res. Hum. Retroviruses 29 (2013) 279-288.
    • (2013) AIDS Res. Hum. Retroviruses , vol.29 , pp. 279-288
    • Kamiyama, H.1
  • 45
    • 61649116903 scopus 로고    scopus 로고
    • Raft localization of CXCR4 is primarily required for X4-tropic human immunodeficiency virus type 1 infection
    • H. Kamiyama, et al., Raft localization of CXCR4 is primarily required for X4-tropic human immunodeficiency virus type 1 infection, Virology 386 (2009) 23-31.
    • (2009) Virology , vol.386 , pp. 23-31
    • Kamiyama, H.1
  • 46
    • 0343674087 scopus 로고    scopus 로고
    • Coreceptor competition for association with CD4 may change the susceptibility of human cells to infection with T-tropic and macrophagetropic isolates of human immunodeficiency virus type 1
    • S. Lee, et al., Coreceptor competition for association with CD4 may change the susceptibility of human cells to infection with T-tropic and macrophagetropic isolates of human immunodeficiency virus type 1, J. Virol. 74 (2000) 5016-5023.
    • (2000) J. Virol. , vol.74 , pp. 5016-5023
    • Lee, S.1
  • 47
    • 38349137271 scopus 로고    scopus 로고
    • Statins Disrupt CCR5 and RANTES expression levels in CD4+ T lymphocytes in vitro and preferentially decrease infection of R5 versus X4 HIV-1
    • A.A. Nabatov, G. Pollakis, T. Linnemann, W.A. Paxton, M.P. de Baar, Statins Disrupt CCR5 and RANTES expression levels in CD4+ T lymphocytes in vitro and preferentially decrease infection of R5 versus X4 HIV-1, PLoS One 2 (2007).
    • (2007) PLoS One , vol.2
    • Nabatov, A.A.1    Pollakis, G.2    Linnemann, T.3    Paxton, W.A.4    De Baar, M.P.5
  • 48
    • 4344566427 scopus 로고    scopus 로고
    • Statins inhibit HIV-1 infection by down-regulating rho activity
    • G. Del Real, et al., Statins inhibit HIV-1 infection by down-regulating rho activity, J. Exp. Med. 200 (2004) 541-547.
    • (2004) J. Exp. Med. , vol.200 , pp. 541-547
    • Del Real, G.1
  • 49
    • 70350316187 scopus 로고    scopus 로고
    • A quantitative af finity-profiling system that reveals distinct CD4/CCR5 usage patterns among human immunodeficiency virus type 1 and simian immunodeficiency virus strains
    • S.H. Johnston, et al., A quantitative af finity-profiling system that reveals distinct CD4/CCR5 usage patterns among human immunodeficiency virus type 1 and simian immunodeficiency virus strains, J. Virol. 83 (2009) 11016-11026.
    • (2009) J. Virol. , vol.83 , pp. 11016-11026
    • Johnston, S.H.1
  • 50
    • 84870700527 scopus 로고    scopus 로고
    • Affinofile profiling: How efficiency of CD4/CCR5 usage impacts the biological and pathogenic phenotype of HIV
    • K. Chikere, T. Chou, P.R. Gorry, B. Lee, Affinofile profiling: how efficiency of CD4/CCR5 usage impacts the biological and pathogenic phenotype of HIV, Virology 435 (2013) 81-91.
    • (2013) Virology , vol.435 , pp. 81-91
    • Chikere, K.1    Chou, T.2    Gorry, P.R.3    Lee, B.4
  • 51
    • 84896539438 scopus 로고    scopus 로고
    • CCR5 conformations are dynamic and modulated by localization, trafficking and G Protein association
    • A.J. Flegler, G.C. Cianci, T.J. Hope, CCR5 conformations are dynamic and modulated by localization, trafficking and G Protein association, PLoS One 9 (2014).
    • (2014) PLoS One , vol.9
    • Flegler, A.J.1    Cianci, G.C.2    Hope, T.J.3
  • 52
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • D.C. Chan, D. Fass, J.M. Berger, P.S. Kim, Core structure of gp41 from the HIV envelope glycoprotein, Cell 89 (1997) 263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 54
    • 84870372472 scopus 로고    scopus 로고
    • HIV entry and envelope glycoprotein-mediated fusion
    • R. Blumenthal, S. Durell, M. Viard, HIV entry and envelope glycoprotein-mediated fusion, J. Biol. Chem. 287 (2012) 40841-40849.
    • (2012) J. Biol. Chem. , vol.287 , pp. 40841-40849
    • Blumenthal, R.1    Durell, S.2    Viard, M.3
  • 55
    • 59849107898 scopus 로고    scopus 로고
    • Common principles and intermediates of viral protein-mediated fusion: The HIV-1 paradigm
    • G.B. Melikyan, Common principles and intermediates of viral protein-mediated fusion: the HIV-1 paradigm, Retrovirology 5 (2008) 111.
    • (2008) Retrovirology , vol.5 , pp. 111
    • Melikyan, G.B.1
  • 56
    • 0037077229 scopus 로고    scopus 로고
    • Sphingomyelin and cholesterol promote HIV-1 gp41 pretransmembrane sequence surface aggregation and membrane restructuring
    • A. Sáez-Cirión, et al., Sphingomyelin and cholesterol promote HIV-1 gp41 pretransmembrane sequence surface aggregation and membrane restructuring, J. Biol. Chem. 277 (2002) 21776-21785.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21776-21785
    • Sáez-Cirión, A.1
  • 57
    • 84859123277 scopus 로고    scopus 로고
    • Analysis of the subunit stoichiometries in viral entry
    • C. Magnus, R.R. Regoes, Analysis of the subunit stoichiometries in viral entry, PLoS One 7 (2012) e33441.
    • (2012) PLoS One , vol.7 , pp. e33441
    • Magnus, C.1    Regoes, R.R.2
  • 58
    • 0037164705 scopus 로고    scopus 로고
    • Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups
    • N. Vincent, C. Genin, E. Malvoisin, Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups, Biochim. Biophys. Acta 1567 (2002) 157-164.
    • (2002) Biochim. Biophys. Acta , vol.1567 , pp. 157-164
    • Vincent, N.1    Genin, C.2    Malvoisin, E.3
  • 59
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for env-mediated fusion and virus infectivity
    • K. Salzwedel, J.T. West, E. Hunter, A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for env-mediated fusion and virus infectivity, J. Virol. 73 (1999) 2469-2480.
    • (1999) J. Virol. , vol.73 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 60
    • 33744512299 scopus 로고    scopus 로고
    • Cholesterol and the interaction of proteins with membrane domains
    • R.M. Epand, Cholesterol and the interaction of proteins with membrane domains, Prog. Lipid Res. 45 (2006) 279-294.
    • (2006) Prog. Lipid Res. , vol.45 , pp. 279-294
    • Epand, R.M.1
  • 61
    • 34748864084 scopus 로고    scopus 로고
    • The influence of cholesterol on the interaction of HIV gp41 membrane proximal region-derived peptides with lipid bilayers
    • A.S. Veiga, M.A.R.B. Castanho, The influence of cholesterol on the interaction of HIV gp41 membrane proximal region-derived peptides with lipid bilayers, FEBS J. 274 (2007) 5096-5104.
    • (2007) FEBS J. , vol.274 , pp. 5096-5104
    • Veiga, A.S.1    Castanho, M.A.R.B.2
  • 62
    • 84891846958 scopus 로고    scopus 로고
    • HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion
    • A.L. Lai, J.H. Freed, HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion, Biophys. J. 106 (2014) 172-181.
    • (2014) Biophys. J. , vol.106 , pp. 172-181
    • Lai, A.L.1    Freed, J.H.2
  • 63
    • 84862778676 scopus 로고    scopus 로고
    • Fusion activity of HIV gp41 fusion domain is related to its secondary structure and depth of membrane insertion in a cholesterol-dependent fashion
    • A.L. Lai, A.E. Moorthy, Y. Li, L.K. Tamm, Fusion activity of HIV gp41 fusion domain is related to its secondary structure and depth of membrane insertion in a cholesterol-dependent fashion, J. Mol. Biol. 418 (2012) 3-15.
    • (2012) J. Mol. Biol. , vol.418 , pp. 3-15
    • Lai, A.L.1    Moorthy, A.E.2    Li, Y.3    Tamm, L.K.4
  • 64
    • 70349304444 scopus 로고    scopus 로고
    • A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide
    • W. Qiang, Y. Sun, D.P. Weliky, A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide, Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 15314-15319.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 15314-15319
    • Qiang, W.1    Sun, Y.2    Weliky, D.P.3
  • 66
    • 55549118226 scopus 로고    scopus 로고
    • Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides
    • R. Chan, et al., Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides, J. Virol. 82 (2008) 11228-11238.
    • (2008) J. Virol. , vol.82 , pp. 11228-11238
    • Chan, R.1
  • 67
    • 84861910758 scopus 로고    scopus 로고
    • Cholesterol mediates membrane curvature during fusion events
    • A. Ivankin, I. Kuzmenko, D. Gidalevitz, Cholesterol mediates membrane curvature during fusion events, Phys. Rev. Lett. 108 (2012) 238103.
    • (2012) Phys. Rev. Lett. , vol.108 , pp. 238103
    • Ivankin, A.1    Kuzmenko, I.2    Gidalevitz, D.3
  • 68
    • 77957861153 scopus 로고    scopus 로고
    • Spatial regulation of membrane fusion controlled by modification of phosphoinositides
    • F. Dumas, et al., Spatial regulation of membrane fusion controlled by modification of phosphoinositides, PLoS One 5 (2010) e12208.
    • (2010) PLoS One , vol.5 , pp. e12208
    • Dumas, F.1
  • 69
    • 34248343803 scopus 로고    scopus 로고
    • Sphingomyelinase restricts the lateral diffusion of CD4 and inhibits human immunodeficiency virus fusion
    • C.M. Finnegan, et al., Sphingomyelinase restricts the lateral diffusion of CD4 and inhibits human immunodeficiency virus fusion, J. Virol. 81 (2007) 45294-45304.
    • (2007) J. Virol. , vol.81 , pp. 45294-45304
    • Finnegan, C.M.1
  • 70
    • 82655186589 scopus 로고    scopus 로고
    • Inhibition of HIV-1 endocytosis allows lipid mixing at the plasma membrane, but not complete fusion
    • M. De la Vega, et al., Inhibition of HIV-1 endocytosis allows lipid mixing at the plasma membrane, but not complete fusion, Retrovirology 8 (2011) 99.
    • (2011) Retrovirology , vol.8 , pp. 99
    • De La Vega, M.1
  • 71
    • 84887289231 scopus 로고    scopus 로고
    • HIV entry: A game of hide-and-fuse?
    • G.B. Melikyan, HIV entry: a game of hide-and-fuse? Curr. Opin. Virol. 4 (2014) 1-7.
    • (2014) Curr. Opin. Virol. , vol.4 , pp. 1-7
    • Melikyan, G.B.1
  • 72
    • 0034710564 scopus 로고    scopus 로고
    • Endocytic entry of HIV-1
    • O.T. Fackler, B.M. Peterlin, Endocytic entry of HIV-1, Curr. Biol. 10 (2000) 1005-1008.
    • (2000) Curr. Biol. , vol.10 , pp. 1005-1008
    • Fackler, O.T.1    Peterlin, B.M.2
  • 74
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • K. Miyauchi, Y. Kim, O. Latinovic, V. Morozov, G.B. Melikyan, HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes, Cell 137 (2009) 433-444.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 77
    • 78650267415 scopus 로고    scopus 로고
    • HIV-1 infects macrophages by exploiting an endocytic route dependent on dynamin, Rac1 and Pak1
    • G.C. Carter, L. Bernstone, D. Baskaran, W. James, HIV-1 infects macrophages by exploiting an endocytic route dependent on dynamin, Rac1 and Pak1, Virology 409 (2011) 234-250.
    • (2011) Virology , vol.409 , pp. 234-250
    • Carter, G.C.1    Bernstone, L.2    Baskaran, D.3    James, W.4
  • 78
    • 84872003613 scopus 로고    scopus 로고
    • Macropinocytosis-like HIV-1 internalization in macrophages is CCR5 dependent and leads to efficient but delayed degradation in endosomal compartments
    • L.A. Gobeil, R. Lodge, M.J. Tremblay, Macropinocytosis-like HIV-1 internalization in macrophages is CCR5 dependent and leads to efficient but delayed degradation in endosomal compartments, J. Virol. 87 (2013) 735-745.
    • (2013) J. Virol. , vol.87 , pp. 735-745
    • Gobeil, L.A.1    Lodge, R.2    Tremblay, M.J.3
  • 79
    • 0031023496 scopus 로고    scopus 로고
    • Transcytosis of infectious human immunodeficiency virus across tight human epithelial cell line barrier
    • M. Bomsel, Transcytosis of infectious human immunodeficiency virus across tight human epithelial cell line barrier, Nat. Med. 3 (1997) 42-47.
    • (1997) Nat. Med. , vol.3 , pp. 42-47
    • Bomsel, M.1
  • 80
    • 0034755158 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 entry into macrophages mediated by macropinocytosis
    • V. Maréchal, et al., Human immunodeficiency virus type 1 entry into macrophages mediated by macropinocytosis, J. Virol. 75 (2001) 11166-11177.
    • (2001) J. Virol. , vol.75 , pp. 11166-11177
    • Maréchal, V.1
  • 81
    • 84868130969 scopus 로고    scopus 로고
    • Differential HIV-1 endocytosis and susceptibility to virus infection in human macrophages correlate with cell activation status
    • L.A. Gobeil, R. Lodge, M.J. Tremblay, Differential HIV-1 endocytosis and susceptibility to virus infection in human macrophages correlate with cell activation status, J. Virol. 86 (2012) 10399-10407.
    • (2012) J. Virol. , vol.86 , pp. 10399-10407
    • Gobeil, L.A.1    Lodge, R.2    Tremblay, M.J.3
  • 82
    • 28644442495 scopus 로고    scopus 로고
    • Time-resolved imaging of HIV-env-mediated lipid and content mixing between a single virion and cell membrane
    • R.M. Markosyan, F.S. Cohen, G.B. Melikyan, Time-resolved imaging of HIV-env-mediated lipid and content mixing between a single virion and cell membrane, Mol. Biol. Cell. 16 (2005) 5502-5513.
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 5502-5513
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 83
    • 61649098778 scopus 로고    scopus 로고
    • HIV entry in macrophages is dependent on intact lipid rafts
    • G.C. Carter, et al., HIV entry in macrophages is dependent on intact lipid rafts, Virology 386 (2009) 192-202.
    • (2009) Virology , vol.386 , pp. 192-202
    • Carter, G.C.1
  • 84
    • 84899884558 scopus 로고    scopus 로고
    • The productive entry pathway of HIV-1 in macrophages is dependent on endocytosis through lipid rafts containing CD4
    • B. Van Wilgenburg, M.D. Moore, W.S. James, S.A. Cowley, The productive entry pathway of HIV-1 in macrophages is dependent on endocytosis through lipid rafts containing CD4, PLoS One 9 (2014) e86071.
    • (2014) PLoS One , vol.9 , pp. e86071
    • Van Wilgenburg, B.1    Moore, M.D.2    James, W.S.3    Cowley, S.A.4
  • 85
    • 0027503454 scopus 로고
    • The galactosyl ceramide/sulfatide receptor binding region HIV-1 gp120 maps to amino acids 206-275
    • S. Bhat, et al., The galactosyl ceramide/sulfatide receptor binding region HIV-1 gp120 maps to amino acids 206-275, AIDS Res. Hum. Retroviruses (1993) 175-181.
    • (1993) AIDS Res. Hum. Retroviruses , pp. 175-181
    • Bhat, S.1
  • 86
    • 28244464389 scopus 로고    scopus 로고
    • Sphingolipids: Modulators of HIV-1 infection and pathogenesis
    • S.S. Rawat, B.T. Johnson, A. Puri, Sphingolipids: modulators of HIV-1 infection and pathogenesis, Biosci. Rep. 25 (2005) 329-343.
    • (2005) Biosci. Rep. , vol.25 , pp. 329-343
    • Rawat, S.S.1    Johnson, B.T.2    Puri, A.3
  • 87
    • 2642678478 scopus 로고    scopus 로고
    • Specific interaction of HIV-1 and HIV-2 surface envelope glycoproteins with monolayers of galactosylceramide and ganglioside GM3
    • D. Hammache, et al., Specific interaction of HIV-1 and HIV-2 surface envelope glycoproteins with monolayers of galactosylceramide and ganglioside GM3, J. Biol. Chem. 273 (1998) 7967-7971.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7967-7971
    • Hammache, D.1
  • 88
    • 84903265715 scopus 로고    scopus 로고
    • Early and late HIV-1 membrane fusion events are impaired sphinganine lipidated peptides that target the fusion site
    • Y.A. Klug, et al., Early and late HIV-1 membrane fusion events are impaired sphinganine lipidated peptides that target the fusion site, Biochem. J. 461 (2014) 213-222.
    • (2014) Biochem. J. , vol.461 , pp. 213-222
    • Klug, Y.A.1
  • 91
    • 20144387029 scopus 로고    scopus 로고
    • Elimination of retroviral infectivity by N-ethylmaleimide with preservation of functional envelope glycoproteins
    • D.R. Morcock, et al., Elimination of retroviral infectivity by N-ethylmaleimide with preservation of functional envelope glycoproteins, J. Virol. 79 (2005) 1533-1542.
    • (2005) J. Virol. , vol.79 , pp. 1533-1542
    • Morcock, D.R.1
  • 92
    • 0031694872 scopus 로고    scopus 로고
    • Inactivation of human immunodeficiency virus type infectivity with preservation of conformational and functional integrity virion surface proteins
    • J.L. Rossio, et al., Inactivation of human immunodeficiency virus type infectivity with preservation of conformational and functional integrity virion surface proteins, J. Virol. 72 (1998) 7992-8001.
    • (1998) J. Virol. , vol.72 , pp. 7992-8001
    • Rossio, J.L.1


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