Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies.

Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies.

We have probed the structures of monomeric and oligomeric gp120 glycoproteins from the LAI isolate of human immunodeficiency virus type 1 (HIV-1) with a panel of monoclonal antibodies (MAbs); most of these MAbs are directed against continuous epitopes. On native monomeric gp120, most of the first co...

Disgrifiad llawn

Manylion Llyfryddiaeth
Prif Awduron:	Moore, J, Sattentau, Q, Wyatt, R, Sodroski, J
Fformat:	Journal article
Iaith:	English
Cyhoeddwyd:	1994

Eitemau Tebyg

Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus.
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Monoclonal antibodies to HIV-1 gp120: a request.
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Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation.
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STRUCTURAL-ANALYSIS OF THE HIV-1 ENVELOPE GLYCOPROTEIN GP120
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Probing the structure of the V2 domain of human immunodeficiency virus type 1 surface glycoprotein gp120 with a panel of eight monoclonal antibodies: human immune response to the V1 and V2 domains.
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CD4-Induced conformational changes in the human immunodeficiency virus type 1 gp120 glycoprotein: consequences for virus entry and neutralization.
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Primary isolates of human immunodeficiency virus type 1 are relatively resistant to neutralization by monoclonal antibodies to gp120, and their neutralization is not predicted by studies with monomeric gp120.
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Towards a structure of the HIV-1 envelope glycoprotein gp120: an immunochemical approach.
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Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer.
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Selective interactions of polyanions with basic surfaces on human immunodeficiency virus type 1 gp120.
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Identification and characterization of monoclonal antibodies specific for polymorphic antigenic determinants within the V2 region of the human immunodeficiency virus type 1 envelope glycoprotein.
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Enhancement of soluble CD4-mediated HIV neutralization and gp 120 binding by CD4 autoantibodies and monoclonal antibodies.
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Interactions among HIV gp120, CD4, and CXCR4: dependence on CD4 expression level, gp120 viral origin, conservation of the gp120 COOH- and NH2-termini and V1/V2 and V3 loops, and sensitivity to neutralizing antibodies.
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Conformational transitions in CD4 due to complexation with HIV envelope glycoprotein gp120.
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Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity.
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Kinetic Analysis of Monoclonal Antibody Binding to HIV-1 gp120-derived Hyperglycosylated Cores
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Detecting SIV gp120 and its interaction with soluble CD4 by ELISA.
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Heparan sulfate targets the HIV-1 envelope glycoprotein gp120 coreceptor binding site.
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Correction: Antigenic Properties of the Human Immunodeficiency Virus Envelope Glycoprotein Gp120 on Virions Bound to Target Cells.
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Cyanovirin-N binds to gp120 to interfere with CD4-dependent human immunodeficiency virus type 1 virion binding, fusion, and infectivity but does not affect the CD4 binding site on gp120 or soluble CD4-induced conformational changes in gp120.
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Cyhoeddwyd: (1999)

Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding.
gan: Sattentau, Q, et al.
Cyhoeddwyd: (1991)

SOLUBLE CD4 BINDING TO HIV-1 VIRIONS CAUSES GP120 TO DISSOCIATE FROM GP41
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Cyhoeddwyd: (1991)

Direct measurement of soluble CD4 binding to human immunodeficiency virus type 1 virions: gp120 dissociation and its implications for virus-cell binding and fusion reactions and their neutralization by soluble CD4.
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Role of CD4 epitopes outside the gp120-binding site during entry of human immunodeficiency virus type 1.
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Cyhoeddwyd: (1997)

Inhibition of HIV Env binding to cellular receptors by monoclonal antibody 2G12 as probed by Fc-tagged gp120
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Production and characterization of high-affinity human monoclonal antibodies to human immunodeficiency virus type 1 envelope glycoproteins in a mouse model expressing human immunoglobulins.
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Shaping T cell - B cell collaboration in the response to human immunodeficiency virus type 1 envelope glycoprotein gp120 by peptide priming.
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Neutralization of infectivity of diverse R5 clinical isolates of human immunodeficiency virus type 1 by gp120-binding 2'F-RNA aptamers.
gan: Khati, M, et al.
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Human immunodeficiency virus type 1 attachment to HeLa CD4 cells is CD4 independent and gp120 dependent and requires cell surface heparans.
gan: Mondor, I, et al.
Cyhoeddwyd: (1998)

HIV gp120: double lock strategy foils host defences.
gan: Sattentau, Q
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Immunochemical analysis of the gp120 surface glycoprotein of human immunodeficiency virus type 1: probing the structure of the C4 and V4 domains and the interaction of the C4 domain with the V3 loop.
gan: Moore, J, et al.
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Corrections: Inhibition of HIV Env binding to cellular receptors by monoclonal antibody 2G12 as probed by Fc-tagged gp120
gan: Wilson Ian A, et al.
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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.
gan: Moore, J, et al.
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Dissociation of gp120 from HIV-1 virions induced by soluble CD4.
gan: Moore, J, et al.
Cyhoeddwyd: (1990)

Interactions of HIV gp120 with the CD4 molecule on lymphocytes and in the nervous system.
gan: Sattentau, Q
Cyhoeddwyd: (1990)

INTERACTIONS OF HIV GP120 WITH THE CD4 MOLECULE ON LYMPHOCYTES AND IN THE NERVOUS-SYSTEM
gan: Sattentau, Q
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Conservation of HIV-1 gp120 neutralizing epitopes after formalin inactivation.
gan: Sattentau, Q
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The recognition of chimeras of rat and human CD4 by HIV-1 gp120 and by monoclonal antibodies.
gan: Davis, S, et al.
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Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding.
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Release of gp120 Restraints Leads to an Entry-Competent Intermediate State of the HIV-1 Envelope Glycoproteins
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