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  • 1
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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
    Published by Nature Publishing Group (NPG)
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  • 2
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    Broad and potent neutralization of HIV-1 by a gp41-specific human antibody (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-11-16
    Description: Characterization of human monoclonal antibodies is providing considerable insight into mechanisms of broad HIV-1 neutralization. Here we report an HIV-1 gp41 membrane-proximal external region (MPER)-specific antibody, named 10E8, which neutralizes approximately 98% of tested viruses. An analysis of sera from 78 healthy HIV-1-infected donors demonstrated that 27% contained MPER-specific antibodies and 8% contained 10E8-like specificities. In contrast to other neutralizing MPER antibodies, 10E8 did not bind phospholipids, was not autoreactive, and bound cell-surface envelope. The structure of 10E8 in complex with the complete MPER revealed a site of vulnerability comprising a narrow stretch of highly conserved gp41-hydrophobic residues and a critical arginine or lysine just before the transmembrane region. Analysis of resistant HIV-1 variants confirmed the importance of these residues for neutralization. The highly conserved MPER is a target of potent, non-self-reactive neutralizing antibodies, suggesting that HIV-1 vaccines should aim to induce antibodies to this region of HIV-1 envelope glycoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Jinghe -- Ofek, Gilad -- Laub, Leo -- Louder, Mark K -- Doria-Rose, Nicole A -- Longo, Nancy S -- Imamichi, Hiromi -- Bailer, Robert T -- Chakrabarti, Bimal -- Sharma, Shailendra K -- Alam, S Munir -- Wang, Tao -- Yang, Yongping -- Zhang, Baoshan -- Migueles, Stephen A -- Wyatt, Richard -- Haynes, Barton F -- Kwong, Peter D -- Mascola, John R -- Connors, Mark -- HSN261200800001E/PHS HHS/ -- Intramural NIH HHS/ -- England -- Nature. 2012 Nov 15;491(7424):406-12. doi: 10.1038/nature11544. Epub 2012 Sep 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉HIV-Specific Immunity Section, Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23151583" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Antibodies, Neutralizing/chemistry/*metabolism ; Antibody Specificity ; Cells, Cultured ; HEK293 Cells ; HIV Antibodies/chemistry/isolation & purification/*metabolism ; HIV Envelope Protein gp41/chemistry/*immunology ; HIV-1/*physiology ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Structure, Tertiary
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
    Electronic Resource
    Electronic Resource
    Some Effects of the Helical Fibrillar Structure of Vegetable Fibres (1949)
    [s.l.] : Nature Publishing Group
    Nature 163 (1949), S. 19-20 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] IN jute, the fibrils in the cell-wall are arranged in right-handed helices, that is, they show the Z twist of textile workers, and the drying-twist is counter-clockwise. In flax, with the fibrils in left-handed (or S) helices, the drying-twist is clockwise1. So far as we know, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/163019a0
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  • 4
    Electronic Resource
    Electronic Resource
    Helical Fibrillar Structure of Vegetable Fibres (1950)
    [s.l.] : Nature Publishing Group
    Nature 166 (1950), S. 198-198 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The error in reading turns per inch in the breaking-twist tests was of the order of 0-01 turn per inch in a single observation. The error in reading the diameter of twisted bundles was of the order of 0*007 cm. in a single observation ; the magnification of the projected image was 15 diameters, and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/166198a0
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