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CD4 activation of HIV fusion

International journal of cell cloning, v.10 no.6, 1992년, pp.323 - 332  

Sattentau, Quentin J. (Centre d'Immunologie de Marseille‐)

Abstract AI-Helper 아이콘AI-Helper

The primary cellular receptor for the human immunodeficiency viruses type 1 (HIV-1) and type 2 (HIV-2) is the CD4 antigen. HIV infection of CD4+ cells is initiated by binding of the virus to the cell surface, via a high affinity interaction between CD4 and the HIV outer envelope glycoprotein, gp120....

참고문헌 (71)

  1. Marsh, Mark, Helenius, Ari. Virus Entry into Animal Cells. Advances in virus research, vol.36, 107-151.

  2. Sommerfelt, M.A., Marsh, M.. Binding and entry of animal viruses. Advanced drug delivery reviews, vol.4, no.1, 1-26.

  3. The Retroviruses Weiss RA 

  4. J Acq Immun Def Synd Grewe C 965 3 1990 HIV: early virus‐cell interactions 

  5. Stein, B.S., Gowda, S.D., Lifson, J.D., Penhallow, R.C., Bensch, K.G., Engleman, E.G.. pH-independent HIV entry into CD4-positive T cells via virus envelope fusion to the plasma membrane. Cell, vol.49, no.5, 659-668.

  6. McClure, M. O., Marsh, M., Weiss, R. A.. Human immunodeficiency virus infection of CD4-bearing cells occurs by a pH-independent mechanism.. The EMBO journal, vol.7, no.2, 513-518.

  7. Dalgleish, Angus G., Beverley, Peter C. L., Clapham, Paul R., Crawford, Dorothy H., Greaves, Melvyn F., Weiss, Robin A.. The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature, vol.312, no.5996, 763-767.

  8. McCune, J.M., Rabin, L.B., Feinberg, M.B., Lieberman, M., Kosek, J.C., Reyes, G.R., Weissman, I.L.. Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus. Cell, vol.53, no.1, 55-67.

  9. J Virol Freed EO 4670 63 1989 10.1128/jvi.63.11.4670-4675.1989 Mutational analysis of the cleavage sequence of the human immunodeficiency virus type 1 envelope glycoprotein precursor 

  10. BRASSEUR, R., CORNET, B., BURNY, A., VANDENBRANDEN, M., RUYSSCHAERT, J.M.. Mode of Insertion into a Lipid Membrane of the N-Terminal HIV gp41 Peptide Segment. AIDS research and human retroviruses, vol.4, no.2, 83-90.

  11. Gallaher, W.R.. Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell, vol.50, no.3, 327-328.

  12. GONZALEZ-SCARANO, FRANCISCO, WAXHAM, M. NEAL, ROSS, ANDREW M., HOXIE, JAMES A.. Sequence Similarities Between Human Immunodeficiency Virus gp41 and Paramyxovirus Fusion Proteins. AIDS research and human retroviruses, vol.3, no.3, 245-252.

  13. Kowalski, M, Potz, J, Basiripour, L, Dorfman, T, Goh, WC, Terwilliger, E, Dayton, A, Rosen, C, Haseltine, W, Sodroski, J. Functional regions of the envelope glycoprotein of human immunodeficiency virus type 1. Science, vol.237, no.4820, 1351-1355.

  14. Freed, E O, Myers, D J, Risser, R. Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41.. Proceedings of the National Academy of Sciences of the United States of America, vol.87, no.12, 4650-4654.

  15. Freed, E O, Myers, D J. Identification and characterization of fusion and processing domains of the human immunodeficiency virus type 2 envelope glycoprotein. Journal of virology, vol.66, no.9, 5472-5478.

  16. Bergeron, L, Sullivan, N, Sodroski, J. Target cell-specific determinants of membrane fusion within the human immunodeficiency virus type 1 gp120 third variable region and gp41 amino terminus. Journal of virology, vol.66, no.4, 2389-2397.

  17. SchultzTF JamesonBA LopalcoL SiccardiAG WeissRA MooreJP.Conserved structural features in the interaction between retroviral surface and transmembrane glycoproteins?AIDS Res Human Retroviruses (in press). 

  18. Gelderblom, H., Reupke, H., Pauli, G.. LOSS OF ENVELOPE ANTIGENS OF HTLV-III/LAV, A FACTOR IN AIDS PATHOGENESIS?. The Lancet, vol.326, no.8462, 1016-1017.

  19. Schneider, J., Kaaden, O., Copeland, T. D., Oroszlan, S., Hunsmann, G.. Shedding and Interspecies Type Sero-reactivity of the Envelope Glycopolypeptide gp120 of the Human Immunodeficiency Virus. The Journal of general virology, vol.67, no.11, 2533-2538.

  20. J Virol McKeating JA 852 65 1991 10.1128/jvi.65.2.852-860.1991 Differential loss of envelope glycoprotein gp120 from virions of human immunodeficiency virus type 1 isolates: effect on infectivity and neutralization 

  21. White, J M, Wilson, I A. Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin. The Journal of cell biology, vol.105, no.6, 2887-2896.

  22. Skehel, J J, Bayley, P M, Brown, E B, Martin, S R, Waterfield, M D, White, J M, Wilson, I A, Wiley, D C. Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion.. Proceedings of the National Academy of Sciences of the United States of America, vol.79, no.4, 968-972.

  23. Allan, JS. Receptor-mediated activation of immunodeficiency viruses in viral fusion. Science, vol.252, no.5010, 1322-1323.

  24. MOORE, JOHN P., MCKEATING, JANE A., WEISS, ROBIN A., CLAPHAM, PAUL R., SATTENTAU, QUENTIN J.. Response. Science, vol.252, no.5010, 1322-1323.

  25. Viral Fusion Mechanisms Moore JP 

  26. Sweet, R.W., Truneh, A., Hendrickson, W.A.. CD4: Its structure, role in immune function and AIDS pathogenesis, and potential as a pharmacological target. Current opinion in biotechnology, vol.2, no.4, 622-633.

  27. Arthos, J., Deen, K.C., Chaikin, M.A., Fornwald, J.A., Sathe, G., Sattentau, Q.J., Clapham, P.R., Weiss, R.A., McDougal, J.S., Pietropaolo, C., Axel, R., Truneh, A., Maddon, P.J., Sweet, R.W.. Identification of the residues in human CD4 critical for the binding of HIV. Cell, vol.57, no.3, 469-481.

  28. J Biol Chem Chao BH 5812 264 1989 10.1016/S0021-9258(18)83622-5 A 113‐amino acid fragment of CD4 produced in Escherichia coli blocks human immunodeficiency virus‐induced cell fusion 

  29. Moore, JP, McKeating, JA, Weiss, RA, Sattentau, QJ. Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science, vol.250, no.4984, 1139-1142.

  30. KIRSH, RICHARD, HART, TIMOTHY K., ELLENS, HARMA, MILLER, JOANNE, PETTEWAY JR., STEPHEN A., LAMBERT, DENNIS M., LEARY, JEFFRY, BUGELSKI, PETER J.. Morphometric Analysis of Recombinant Soluble CD4-Mediated Release of the Envelope Glycoprotein gp120 from HIV-1. AIDS research and human retroviruses, vol.6, no.10, 1209-1212.

  31. Hart, T K, Kirsh, R, Ellens, H, Sweet, R W, Lambert, D M, Petteway Jr, S R, Leary, J, Bugelski, P J. Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120.. Proceedings of the National Academy of Sciences of the United States of America, vol.88, no.6, 2189-2193.

  32. J Virol Moore JP 1133 65 1991 10.1128/jvi.65.3.1133-1140.1991 Direct measurement of soluble CD4 binding to human immunodeficiency virus type 1 virion: gp120 dissociation and its implications for virus‐cell binding and fusion reactions and their neutralization by soluble CD4 

  33. Layne, Scott P., Merges, Michael J., Dembo, Micah, Spouge, John L., Nara, Peter L.. HIV requires multiple gp120 molecules for CD4-mediated infection. Nature, vol.346, no.6281, 277-279.

  34. J Virol Earl PL 5610 66 1992 10.1128/jvi.66.9.5610-5614.1992 Multimeric CD4 binding exhibited by human and simian immunodeficiency virus enveloped protein dimers 

  35. MOORE, JOHN P., KLASSE, PER JOHAN. Thermodynamic and Kinetic Analysis of sCD4 Binding to HIV-1 Virions and of gp120 Dissociation. AIDS research and human retroviruses, vol.8, no.4, 443-450.

  36. J Virol Dimitrov DS 132 66 1992 10.1128/jvi.66.1.132-138.1992 Kinetics of soluble CD4 binding to cells expressing human immunodeficiency virus type 1 envelope glycoprotein 

  37. AIDS Dimitrov DS 249 6 1992 10.1097/00002030-199203000-00001 Correlation between kinetics of sCD4 interactions with HIV‐1 envelope expressing cells and inhibition of syncytia formation: implications for mechanisms of cell fusion and therapy of AIDS 

  38. Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. The Journal of experimental medicine, vol.174, no.2, 407-415.

  39. Daar, E S, Li, X L, Moudgil, T, Ho, D D. High concentrations of recombinant soluble CD4 are required to neutralize primary human immunodeficiency virus type 1 isolates.. Proceedings of the National Academy of Sciences of the United States of America, vol.87, no.17, 6574-6578.

  40. Brighty, D W, Rosenberg, M, Chen, I S, Ivey-Hoyle, M. Envelope proteins from clinical isolates of human immunodeficiency virus type 1 that are refractory to neutralization by soluble CD4 possess high affinity for the CD4 receptor.. Proceedings of the National Academy of Sciences of the United States of America, vol.88, no.17, 7802-7805.

  41. J Virol Moore JP 235 66 1992 10.1128/jvi.66.1.235-243.1992 Virions of primary human immunodeficiency virus type 1 isolates resistant to soluble CD4 (sCD4) neutralization differ in sCD4 binding and glycoprotein gp120 retention from sCD4 sensitive isolates 

  42. Asjo, B., Albert, J., Karlsson, A., Morfeldt-Manson, L., Biberfeld, G., Lidman, K., Fenyo, E.. REPLICATIVE CAPACITY OF HUMAN IMMUNODEFICIENCY VIRUS FROM PATIENTS WITH VARYING SEVERITY OF HIV INFECTION. The Lancet, vol.328, no.8508, 660-662.

  43. Miedema, F., Tersmette, M., van Lier, R.W.. AIDS pathogenesis: a dynamic interaction between HIV and the immune system. Immunology today, vol.11, 293-297.

  44. Moore, John P.. Simple methods for monitoring HIV-1 and HIV-2 gp120 binding to soluble CD4 by enzyme-linked immunosorbent assay : HIV-2 has a 25-fold lower affinity than HIV-1 for soluble CD4. AIDS, vol.4, no.4, 297-306.

  45. Mulligan, M.J., Ritter, G.D., Chaikinj, M.A., Yamshchikov, G.V., Kumar, P., Hahn, B.H., Sweet, R.W., Compans, R.W.. Human immunodeficiency virus type 2 envelope glycoprotein: Differential CD4 interactions of soluble gpl20 versus the assembled envelope complex. Virology, vol.187, no.1, 233-241.

  46. Clapham, P.R., Blanc, D., Weiss, R.A.. Specific cell surface requirements for the infection of CD4-positive cells by human immunodeficiency virus types 1 and 2 and by simian immunodeficiency virus. Virology, vol.181, no.2, 703-715.

  47. Clapham, P R, McKnight, A, Weiss, R A. Human immunodeficiency virus type 2 infection and fusion of CD4-negative human cell lines: induction and enhancement by soluble CD4. Journal of virology, vol.66, no.6, 3531-3537.

  48. J Virol Thali M 5516 66 1992 10.1128/jvi.66.9.5516-5524.1992 Lack of correlation between soluble CD4‐induced shedding of the human immunodeficiency virus type 1 exterior envelope glycoprotein and subsequent membrane fusion events 

  49. Bedinger, Patricia, Moriarty, Ann, von Borstel II, Robert C., Donovan, Nancy J., Steimer, Kathelyn S., Littman, Dan R.. Internalization of the human immunodeficiency virus does not require the cytoplasmic domain of CD4. Nature, vol.334, no.6178, 162-165.

  50. J Virol Jasin M 440 65 1991 10.1128/jvi.65.1.440-444.1991 Glycosylphosphati‐dylinositol‐anchored CD4/thy‐1 chimaeric molecules serve as human immunodeficiency virus receptors in human, but not mouse, cells and are modulated by gangliosides 

  51. Lifson, JD, Hwang, KM, Nara, PL, Fraser, B, Padgett, M, Dunlop, NM, Eiden, LE. Synthetic CD4 peptide derivatives that inhibit HIV infection and cytopathicity. Science, vol.241, no.4866, 712-716.

  52. Nara, P L, Hwang, K M, Rausch, D M, Lifson, J D, Eiden, L E. CD4 antigen-based antireceptor peptides inhibit infectivity of human immunodeficiency virus in vitro at multiple stages of the viral life cycle.. Proceedings of the National Academy of Sciences of the United States of America, vol.86, no.18, 7139-7143.

  53. Wang, Jiahuai, Yan, Youwei, Garrett, Thomas P. J., Liu, Jinhuan, Rodgers, David W., Garlick, Robert L., Tarr, George E., Husain, Yasmin, Reinherz, Ellis L., Harrison, Stephen C.. Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. Nature, vol.348, no.6300, 411-418.

  54. Ryu, Seong-Eon, Kwong, Peter D., Truneh, Alemseged, Porter, Terence G., Arthos, James, Rosenberg, Martin, Dai, Xiaoping, Xuong, Nguyen-huu, Axel, Richard, Sweet, Raymond W., Hendrickson, Wayne A.. Crystal structure of an HIV-binding recombinant fragment of human CD4. Nature, vol.348, no.6300, 419-426.

  55. Camerini, D., Seed, B.. A CD4 domain important for HIV-mediated syncytium formation lies outside the virus binding site. Cell, vol.60, no.5, 747-754.

  56. J Biol Chem Truneh A 5942 266 1991 10.1016/S0021-9258(19)67689-1 A region in domain 1 of CD4 distinct from the primary gp120 binding site is involved in HIV infection and virus mediated fusion 

  57. Berger, E A, Lifson, J D, Eiden, L E. Stimulation of glycoprotein gp120 dissociation from the envelope glycoprotein complex of human immunodeficiency virus type 1 by soluble CD4 and CD4 peptide derivatives: implications for the role of the complementarity-determining region 3-like region in membrane fusion.. Proceedings of the National Academy of Sciences of the United States of America, vol.88, no.18, 8082-8086.

  58. Eiden, L.E., Lifson, J.D.. HIV interactions with CD4: a continuum of conformations and consequences. Immunology today, vol.13, no.6, 201-206.

  59. BrodenCC BergerEA.CD4 molecules with a diversity of mutations in the CDR‐3 region. J Cell Biochem1992; (suppl 16e):18. 

  60. Construction of a binding site for human immunodeficiency virus type 1 gp120 in rat CD4. The Journal of experimental medicine, vol.175, no.1, 301-304.

  61. J Immunol Repke H 1809 149 1992 10.4049/jimmunol.149.5.1809 Effects of CD4 synthetic peptides on human immunodeficiency virus type 1 envelope glycoprotein function 

  62. Antibody raised against soluble CD4-rgp120 complex recognizes the CD4 moiety and blocks membrane fusion without inhibiting CD4-gp120 binding. The Journal of experimental medicine, vol.172, no.4, 1143-1150.

  63. Novel anti-CD4 monoclonal antibodies separate human immunodeficiency virus infection and fusion of CD4+ cells from virus binding. The Journal of experimental medicine, vol.172, no.4, 1233-1242.

  64. J Immunol Hasunuma T 1841 148 1992 10.4049/jimmunol.148.6.1841 Regions of the CD4 molecule not involved in virus binding or syncytia formation are required for HIV‐1 infection of lymphocytes 

  65. J Immunol Burkly LC 1779 149 1992 Inhibition of HIV entry by a CD4 domain 2 specific monoclonal antibody: evidence for structural alterations upon CD4/HIV gp120 binding 

  66. J Virol Moore JP 4784 66 1992 10.1128/jvi.66.8.4784-4793.1992 A monoclonal antibody to CD4 domain 2 blocks soluble CD4‐induced conformational changes in the envelope glycoproteins of human immunodeficiency virus type 1 (HIV‐1) and HIV‐1 infection of CD4+ cells 

  67. Moore, John P., Nara, Peter L.. The role of the V3 loop of gp 120 in HIV infection :. AIDS, vol.5, no.suppl, 21-34.

  68. Hwang, SS, Boyle, TJ, Lyerly, HK, Cullen, BR. Identification of envelope V3 loop as the major determinant of CD4 neutralization sensitivity of HIV-1. Science, vol.257, no.5069, 535-537.

  69. Hwang, SS, Boyle, TJ, Lyerly, HK, Cullen, BR. Identification of the envelope V3 loop as the primary determinant of cell tropism in HIV-1. Science, vol.253, no.5015, 71-74.

  70. STEPHENS, P. E., CLEMENTS, G., YARRANTON, G. T., MOORE, J.. A chink in HIV's armour?. Nature, vol.343, no.6255, 219-219.

  71. Hildreth, JE, Orentas, RJ. Involvement of a leukocyte adhesion receptor (LFA-1) in HIV-induced syncytium formation. Science, vol.244, no.4908, 1075-1078.

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