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  • 1
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    Uncoupling of immune complex formation and kidney damage in autoimmune glomerulonephritis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-07
    Description: The generation of autoantibody and subsequent tissue deposition of immune complexes (IC) is thought to trigger the pathogenic consequences of systemic autoimmune disease. Modulation of the autoantibody response disrupts pathogenesis by preventing the formation of ICs; however, uncoupling IC formation from subsequent inflammatory responses seems unlikely because of the apparent complexity of the IC-triggered inflammatory cascade. However, the disruption of a single gene, which encodes the gamma chain of the Fc receptor, was found to achieve this uncoupling in a spontaneous model of lupus nephritis, the New Zealand Black/New Zealand White (NZB/NZW) mouse. Gamma chain-deficient NZB/NZW mice generated and deposited IC and activated complement, but were protected from severe nephritis, thus defining another potential pathway for therapeutic intervention in autoimmune disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clynes, R -- Dumitru, C -- Ravetch, J V -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):1052-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9461440" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Antinuclear/blood ; Antigen-Antibody Complex/blood/*immunology ; *Complement Activation ; Complement System Proteins/analysis ; Crosses, Genetic ; Disease Models, Animal ; Glomerular Mesangium/immunology/pathology ; Kidney Glomerulus/*immunology/*pathology ; Lupus Nephritis/*immunology/pathology ; Mice ; Mice, Inbred C57BL ; Mice, Inbred Strains ; Receptors, IgG/genetics/*immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Immune inhibitory receptors (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-06
    Description: With the detailed description and analysis of several inhibitory receptor systems on lymphoid and myeloid cells, a central paradigm has emerged in which the pairing of activation and inhibition is necessary to initiate, amplify, and then terminate immune responses. In some cases, the activating and inhibitory receptors recognize similar ligands, and the net outcome is determined by the relative strength of these opposing signals. The importance of this modulation is demonstrated by the sometimes fatal autoimmune disorders observed in mice with targeted disruption of inhibitory receptors. The significance of these receptors is further evidenced by the conservation of immunoreceptor tyrosine-based inhibitory motifs during their evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ravetch, J V -- Lanier, L L -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):84-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics and Immunology, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11021804" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Animals ; Antigens, CD/chemistry/immunology/metabolism ; Antigens, Differentiation/immunology ; Autoimmune Diseases/immunology ; B-Lymphocytes/immunology ; Blood Cells/immunology ; CTLA-4 Antigen ; Histocompatibility Antigens Class I/immunology/metabolism ; Humans ; *Immunity, Cellular ; *Immunoconjugates ; Killer Cells, Natural/immunology ; Lymphocyte Activation ; Phagocytes/immunology ; Receptors, IgG/immunology/metabolism ; Receptors, Immunologic/chemistry/*immunology/metabolism ; Signal Transduction ; T-Lymphocytes/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-13
    Description: The molecular basis for the anti-inflammatory property of intravenous gamma globulin (IVIG) was investigated in a murine model of immune thrombocytopenia. Administration of clinically protective doses of intact antibody or monomeric Fc fragments to wild-type or Fcgamma receptor-humanized mice prevented platelet consumption triggered by a pathogenic autoantibody. The inhibitory Fc receptor, FcgammaRIIB, was required for protection, because disruption either by genetic deletion or with a blocking monoclonal antibody reversed the therapeutic effect of IVIG. Protection was associated with the ability of IVIG administration to induce surface expression of FcgammaRIIB on splenic macrophages. Modulation of inhibitory signaling is thus a potent therapeutic strategy for attenuating autoantibody-triggered inflammatory diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Samuelsson, A -- Towers, T L -- Ravetch, J V -- New York, N.Y. -- Science. 2001 Jan 19;291(5503):484-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics and Immunology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11161202" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Inflammatory Agents, Non-Steroidal/pharmacology/*therapeutic use ; Antigens, CD/immunology/*metabolism ; Autoantibodies/immunology ; Blood Platelets/immunology ; Complement System Proteins/immunology ; Humans ; Immunoglobulin Fc Fragments/pharmacology/therapeutic use ; Immunoglobulins, Intravenous/pharmacology/*therapeutic use ; Macrophages/*immunology ; Mice ; Mice, Inbred BALB C ; Mice, Transgenic ; Opsonin Proteins ; Phagocytosis ; Phosphatidylinositol Phosphates/metabolism ; Phosphoric Monoester Hydrolases/metabolism ; Purpura, Thrombocytopenic, Idiopathic/immunology/*prevention & control ; Receptors, IgG/genetics/immunology/*metabolism ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-03-17
    Description: Antibodies to conserved epitopes on the human immunodeficiency virus (HIV) surface protein gp140 can protect against infection in non-human primates, and some infected individuals show high titres of broadly neutralizing immunoglobulin (Ig)G antibodies in their serum. However, little is known about the specificity and activity of these antibodies. To characterize the memory antibody responses to HIV, we cloned 502 antibodies from HIV envelope-binding memory B cells from six HIV-infected patients with broadly neutralizing antibodies and low to intermediate viral loads. We show that in these patients, the B-cell memory response to gp140 is composed of up to 50 independent clones expressing high affinity neutralizing antibodies to the gp120 variable loops, the CD4-binding site, the co-receptor-binding site, and to a new neutralizing epitope that is in the same region of gp120 as the CD4-binding site. Thus, the IgG memory B-cell compartment in the selected group of patients with broad serum neutralizing activity to HIV is comprised of multiple clonal responses with neutralizing activity directed against several epitopes on gp120.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scheid, Johannes F -- Mouquet, Hugo -- Feldhahn, Niklas -- Seaman, Michael S -- Velinzon, Klara -- Pietzsch, John -- Ott, Rene G -- Anthony, Robert M -- Zebroski, Henry -- Hurley, Arlene -- Phogat, Adhuna -- Chakrabarti, Bimal -- Li, Yuxing -- Connors, Mark -- Pereyra, Florencia -- Walker, Bruce D -- Wardemann, Hedda -- Ho, David -- Wyatt, Richard T -- Mascola, John R -- Ravetch, Jeffrey V -- Nussenzweig, Michel C -- Howard Hughes Medical Institute/ -- Intramural NIH HHS/ -- England -- Nature. 2009 Apr 2;458(7238):636-40. doi: 10.1038/nature07930. Epub 2009 Mar 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Immunology, The Rockefeller University, New York, New York 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19287373" target="_blank"〉PubMed〈/a〉
    Keywords: Antibody Affinity ; Antigens, CD4/metabolism ; B-Lymphocytes/*immunology ; Binding Sites ; Enzyme-Linked Immunosorbent Assay ; Epitope Mapping ; Epitopes, B-Lymphocyte/chemistry/immunology ; HIV Antibodies/*analysis/*immunology/isolation & purification ; HIV Envelope Protein gp120/chemistry/immunology/metabolism ; HIV Envelope Protein gp41/chemistry/immunology ; HIV Infections/*immunology ; Humans ; Immunologic Memory/*immunology ; Neutralization Tests ; Receptors, HIV/metabolism ; Viral Load ; env Gene Products, Human Immunodeficiency Virus/chemistry/*immunology/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
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    Organization of the human and mouse low-affinity Fc gamma R genes: duplication and recombination (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-11
    Description: Receptors for immunoglobulin G immune complexes (Fc gamma RII and Fc gamma RIII) are expressed on most hematopoietic cells and show much structural and functional diversity. In order to determine the genetic basis for this diversity, a family of genes encoding the human and mouse receptors was isolated and characterized. Humans have five distinct genes for low-affinity Fc gamma Rs, in contrast to two in the mouse. With the use of yeast artificial chromosomes, the genes encoding the human receptors were oriented and linked, which established the structure of this complex locus. Comparison of the human and mouse genes generated a model for the evolutionary amplification of this locus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Qiu, W Q -- de Bruin, D -- Brownstein, B H -- Pearse, R -- Ravetch, J V -- GM 36306/GM/NIGMS NIH HHS/ -- GM 39256/GM/NIGMS NIH HHS/ -- K23 AG022476/AG/NIA NIH HHS/ -- R01 AG031171/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1990 May 11;248(4956):732-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Biology, Sloan-Kettering Institute, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2139735" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Differentiation/*genetics/metabolism ; Base Sequence ; Blotting, Southern ; Exons ; Genome, Human ; Humans ; Immunoglobulin G/metabolism ; Introns ; Mice ; Molecular Sequence Data ; *Multigene Family ; Mutation ; Receptors, Fc/*genetics/metabolism ; Receptors, IgG ; Recombination, Genetic ; Restriction Mapping ; Spleen/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Restoration of tolerance in lupus by targeted inhibitory receptor expression (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-01
    Description: Lupus, a multigenic autoimmune condition in which a breakdown of tolerance results in the development of autoantibodies, leads to a variety of pathologic outcomes. Despite the heterogeneity of factors influencing disease susceptibility, we demonstrate that the partial restoration of inhibitory Fc receptor (FcgRIIB) levels on B cells in lupus-prone mouse strains is sufficient to restore tolerance and prevent autoimmunity. FcgRIIB regulates a common B cell checkpoint in genetically diverse lupus-prone mouse strains, and modest changes in its expression can result in either tolerance or autoimmunity. Therefore, increasing FcgammaRIIB levels on B cells may be an effective way to treat autoimmune diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McGaha, Tracy L -- Sorrentino, Brian -- Ravetch, Jeffrey V -- New York, N.Y. -- Science. 2005 Jan 28;307(5709):590-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics and Immunology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681388" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Antinuclear/blood ; Autoantibodies/blood ; B-Lymphocytes/*immunology ; Bone Marrow Transplantation ; Chromatin/immunology ; Female ; Genetic Vectors ; Kidney/pathology ; Lung/pathology ; Lupus Erythematosus, Systemic/*immunology/pathology/physiopathology/*therapy ; Macrophages/immunology ; Male ; Mice ; Mice, Inbred C57BL ; Myeloid Cells/immunology ; Receptors, IgG/genetics/*metabolism ; Retroviridae/genetics ; *Self Tolerance ; T-Lymphocytes/immunology ; Transduction, Genetic
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Divergent immunoglobulin g subclass activity through selective Fc receptor binding (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-03
    Description: Subclasses of immunoglobulin G (IgG) display substantial differences in their ability to mediate effector responses, contributing to variable activity of antibodies against microbes and tumors. We demonstrate that the mechanism underlying this long-standing observation of subclass dominance in function is provided by the differential affinities of IgG subclasses for specific activating IgG Fc receptors compared with their affinities for the inhibitory IgG Fc receptor. The significant differences in the ratios of activating-to-inhibitory receptor binding predicted the in vivo activity. We suggest that these highly predictable functions assigned by Fc binding will be an important consideration in the design of therapeutic antibodies and vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nimmerjahn, Falk -- Ravetch, Jeffrey V -- New York, N.Y. -- Science. 2005 Dec 2;310(5753):1510-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics and Immunology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16322460" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Platelets/immunology ; Cell Line ; Female ; Immunoglobulin G/*immunology/*metabolism ; Melanosomes/immunology ; Mice ; Mice, Inbred C57BL ; Protein Binding ; Receptors, IgG/classification/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-06-21
    Description: High-dose intravenous immunoglobulin is a widely used therapeutic preparation of highly purified immunoglobulin G (IgG) antibodies. It is administered at high doses (1-2 grams per kilogram) for the suppression of autoantibody-triggered inflammation in a variety of clinical settings. This anti-inflammatory activity of intravenous immunoglobulin is triggered by a minor population of IgG crystallizable fragments (Fcs), with glycans terminating in alpha2,6 sialic acids (sFc) that target myeloid regulatory cells expressing the lectin dendritic-cell-specific ICAM-3 grabbing non-integrin (DC-SIGN; also known as CD209). Here, to characterize this response in detail, we generated humanized DC-SIGN mice (hDC-SIGN), and demonstrate that the anti-inflammatory activity of intravenous immunoglobulin can be recapitulated by the transfer of bone-marrow-derived sFc-treated hDC-SIGN(+) macrophages or dendritic cells into naive recipients. Furthermore, sFc administration results in the production of IL-33, which, in turn, induces expansion of IL-4-producing basophils that promote increased expression of the inhibitory Fc receptor FcgammaRIIB on effector macrophages. Systemic administration of the T(H)2 cytokines IL-33 or IL-4 upregulates FcgammaRIIB on macrophages, and suppresses serum-induced arthritis. Consistent with these results, transfer of IL-33-treated basophils suppressed induced arthritic inflammation. This novel DC-SIGN-T(H)2 pathway initiated by an endogenous ligand, sFc, provides an intrinsic mechanism for maintaining immune homeostasis that could be manipulated to provide therapeutic benefit in autoimmune diseases.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3694429/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3694429/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anthony, Robert M -- Kobayashi, Toshihiko -- Wermeling, Fredrik -- Ravetch, Jeffrey V -- R01 AI035875/AI/NIAID NIH HHS/ -- England -- Nature. 2011 Jun 19;475(7354):110-3. doi: 10.1038/nature10134.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics and Immunology, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21685887" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arthritis/drug therapy/immunology/pathology ; Autoimmune Diseases/drug therapy/immunology ; Basophils/drug effects/immunology/metabolism ; Bone Marrow ; Cell Adhesion Molecules/genetics/immunology/metabolism ; Crystallization ; Dendritic Cells/cytology/immunology ; Humans ; Immunoglobulin G/chemistry/immunology/metabolism/pharmacology ; Immunoglobulins, Intravenous/chemistry/*immunology/metabolism/pharmacology ; Inflammation/drug therapy/*immunology ; Interleukin-33 ; Interleukin-4/immunology/metabolism ; Interleukins/immunology/metabolism/pharmacology ; Lectins, C-Type/genetics/immunology/metabolism ; Ligands ; Macrophages/cytology/immunology ; Mice ; Receptors, Cell Surface/genetics/immunology/metabolism ; Receptors, IgG/immunology/metabolism ; Th2 Cells/drug effects/*immunology
    Print ISSN: 0028-0836
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    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 9
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    Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-10-01
    Description: During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo homotypic bivalent binding. However, this type of binding is not always possible. For example, the small number of gp140 glycoprotein spikes displayed on the surface of the human immunodeficiency virus (HIV) disfavours homotypic bivalent antibody binding. Here we show that during the human antibody response to HIV, somatic mutations that increase antibody affinity also increase breadth and neutralizing potency. Surprisingly, the responding naive and memory B cells produce polyreactive antibodies, which are capable of bivalent heteroligation between one high-affinity anti-HIV-gp140 combining site and a second low-affinity site on another molecular structure on HIV. Although cross-reactivity to self-antigens or polyreactivity is strongly selected against during B-cell development, it is a common serologic feature of certain infections in humans, including HIV, Epstein-Barr virus and hepatitis C virus. Seventy-five per cent of the 134 monoclonal anti-HIV-gp140 antibodies cloned from six patients with high titres of neutralizing antibodies are polyreactive. Despite the low affinity of the polyreactive combining site, heteroligation demonstrably increases the apparent affinity of polyreactive antibodies to HIV.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3699875/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3699875/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mouquet, Hugo -- Scheid, Johannes F -- Zoller, Markus J -- Krogsgaard, Michelle -- Ott, Rene G -- Shukair, Shetha -- Artyomov, Maxim N -- Pietzsch, John -- Connors, Mark -- Pereyra, Florencia -- Walker, Bruce D -- Ho, David D -- Wilson, Patrick C -- Seaman, Michael S -- Eisen, Herman N -- Chakraborty, Arup K -- Hope, Thomas J -- Ravetch, Jeffrey V -- Wardemann, Hedda -- Nussenzweig, Michel C -- 1 P01 AI081677/AI/NIAID NIH HHS/ -- P01 AI081677/AI/NIAID NIH HHS/ -- R01 AI047770/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2010 Sep 30;467(7315):591-5. doi: 10.1038/nature09385.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Immunology, The Rockefeller University, New York, New York 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20882016" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal/immunology ; Antibodies, Neutralizing/immunology ; Antibody Affinity/genetics/*immunology ; Antigen-Antibody Reactions/genetics/*immunology ; Cardiolipins/immunology ; Cell Line, Tumor ; Cross Reactions/genetics/immunology ; Enzyme-Linked Immunosorbent Assay ; Epitopes/*chemistry/*immunology ; HIV Antibodies/genetics/*immunology ; HIV Antigens/chemistry/*immunology ; HIV-1/chemistry/*immunology ; Humans ; Immunoglobulin Fab Fragments/genetics/immunology ; Immunoglobulin Heavy Chains/genetics/immunology ; Mutation ; Surface Plasmon Resonance ; env Gene Products, Human Immunodeficiency Virus/immunology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 10
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    HIV therapy by a combination of broadly neutralizing antibodies in humanized mice (2012)
    Nature Publishing Group (NPG)
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    Publication Date: 2012-10-30
    Description: Human antibodies to human immunodeficiency virus-1 (HIV-1) can neutralize a broad range of viral isolates in vitro and protect non-human primates against infection. Previous work showed that antibodies exert selective pressure on the virus but escape variants emerge within a short period of time. However, these experiments were performed before the recent discovery of more potent anti-HIV-1 antibodies and their improvement by structure-based design. Here we re-examine passive antibody transfer as a therapeutic modality in HIV-1-infected humanized mice. Although HIV-1 can escape from antibody monotherapy, combinations of broadly neutralizing antibodies can effectively control HIV-1 infection and suppress viral load to levels below detection. Moreover, in contrast to antiretroviral therapy, the longer half-life of antibodies led to control of viraemia for an average of 60 days after cessation of therapy. Thus, combinations of potent monoclonal antibodies can effectively control HIV-1 replication in humanized mice, and should be re-examined as a therapeutic modality in HIV-1-infected individuals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3809838/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3809838/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, Florian -- Halper-Stromberg, Ariel -- Horwitz, Joshua A -- Gruell, Henning -- Scheid, Johannes F -- Bournazos, Stylianos -- Mouquet, Hugo -- Spatz, Linda A -- Diskin, Ron -- Abadir, Alexander -- Zang, Trinity -- Dorner, Marcus -- Billerbeck, Eva -- Labitt, Rachael N -- Gaebler, Christian -- Marcovecchio, Paola M -- Incesu, Reha-Baris -- Eisenreich, Thomas R -- Bieniasz, Paul D -- Seaman, Michael S -- Bjorkman, Pamela J -- Ravetch, Jeffrey V -- Ploss, Alexander -- Nussenzweig, Michel C -- 1UM1AI100663/AI/NIAID NIH HHS/ -- AI081677/AI/NIAID NIH HHS/ -- P01 AI081677/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2012 Dec 6;492(7427):118-22. doi: 10.1038/nature11604. Epub 2012 Oct 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Immunology, The Rockefeller University, New York, New York 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23103874" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology/therapeutic use ; Antibodies, Neutralizing/*immunology/*therapeutic use ; Antibody Specificity/immunology ; Disease Models, Animal ; HIV Antibodies/*immunology/*therapeutic use ; HIV Infections/*drug therapy/*immunology/virology ; HIV-1/genetics/growth & development/immunology/isolation & purification ; Half-Life ; Humans ; Immunization, Passive ; Mice ; Mice, Inbred NOD ; Time Factors ; Viral Load/drug effects
    Print ISSN: 0028-0836
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    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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