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  • 1
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    Envelope-constrained neutralization-sensitive HIV-1 after heterosexual transmission (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2004-03-27
    Beschreibung: Heterosexual transmission accounts for the majority of human immunodeficiency virus-1 (HIV-1) infections worldwide, yet the viral properties that determine transmission fitness or outgrowth have not been elucidated. Here we show, for eight heterosexual transmission pairs, that recipient viruses were monophyletic, encoding compact, glycan-restricted envelope glycoproteins. These viruses were also uniquely sensitive to neutralization by antibody from the transmitting partner. Thus, the exposure of neutralizing epitopes, which are lost in chronic infection because of immune escape, appears to be favored in the newly infected host. This reveals characteristics of the envelope glycoprotein that influence HIV-1 transmission and may have implications for vaccine design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Derdeyn, Cynthia A -- Decker, Julie M -- Bibollet-Ruche, Frederic -- Mokili, John L -- Muldoon, Mark -- Denham, Scott A -- Heil, Marintha L -- Kasolo, Francis -- Musonda, Rosemary -- Hahn, Beatrice H -- Shaw, George M -- Korber, Bette T -- Allen, Susan -- Hunter, Eric -- AI-40951/AI/NIAID NIH HHS/ -- AI-51231/AI/NIAID NIH HHS/ -- N01-85338/PHS HHS/ -- U01-AI-41530/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Mar 26;303(5666):2019-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294 USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15044802" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): AIDS Vaccines ; Amino Acid Sequence ; Cohort Studies ; Epitopes/immunology ; Female ; Genes, env ; Glycosylation ; HIV Antibodies/*immunology ; HIV Envelope Protein gp120/chemistry/genetics/*immunology ; HIV Infections/*immunology/*transmission/virology ; HIV-1/genetics/*immunology/physiology ; Heterosexuality ; Humans ; Likelihood Functions ; Male ; Molecular Sequence Data ; Neutralization Tests ; Prospective Studies ; Viral Load ; Zambia
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
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    Uromodulin (Tamm-Horsfall glycoprotein): a renal ligand for lymphokines (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1987-09-18
    Beschreibung: The protein portion of the immunosuppressive glycoprotein uromodulin is identical to the Tamm-Horsfall urinary glycoprotein and is synthesized in the kidney. Evidence that the glycoproteins are the same is based on amino acid sequence identity, immunologic cross-reactivity, and tissue localization to the thick ascending limb of Henle's loop. Nucleic acid sequencing of clones for uromodulin isolated from a complementary DNA bank from human kidney predicts a protein 639 amino acids in length, including a 24--amino acid leader sequence and a cysteine-rich mature protein with eight potential glycosylation sites. Uromodulin and preparations of Tamm-Horsfall glycoprotein bind to recombinant murine interleukin-1 (rIL-1) and human rIL-1 alpha, rIL-1 beta, and recombinant tumor necrosis factor (rTNF). Uromodulin isolated from urine of pregnant women by lectin adherence is more immunosuppressive than material isolated by the original salt-precipitation protocol of Tamm and Horsfall. Immunohistologic studies demonstrate that rIL-1 and rTNF bind to the same area of the human kidney that binds to antiserum specific for uromodulin. Thus, uromodulin (Tamm-Horsfall glycoprotein) may function as a unique renal regulatory glycoprotein that specifically binds to and regulates the circulating activity of a number of potent cytokines, including IL-1 and TNF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hession, C -- Decker, J M -- Sherblom, A P -- Kumar, S -- Yue, C C -- Mattaliano, R J -- Tizard, R -- Kawashima, E -- Schmeissner, U -- Heletky, S -- New York, N.Y. -- Science. 1987 Sep 18;237(4821):1479-84.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3498215" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Enzyme-Linked Immunosorbent Assay ; Glycoproteins/metabolism ; Humans ; Interleukin-1/metabolism ; Kidney/*metabolism ; Ligands/metabolism ; Lymphokines/*metabolism ; Molecular Weight ; Mucoproteins/*analysis/genetics ; RNA, Messenger/analysis ; Recombinant Proteins/metabolism ; Tumor Necrosis Factor-alpha ; Uromodulin
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
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    Uromodulin: a unique 85-kilodalton immunosuppressive glycoprotein isolated from urine of pregnant women (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1985-08-02
    Beschreibung: Crude fractions of urine from pregnant women are immunosuppressive in vitro. An 85-kilodalton immunosuppressive glycoprotein purified to homogeneity from such urine inhibited in vitro assays of human T-cell and monocyte activity at concentrations of 10(-9) to 10(-11) molar. This material was nontoxic and blocked early events required for normal T-cell proliferation in vitro. On the basis of its tissue source and its in vitro activity, the name "uromodulin" is proposed for this glycoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muchmore, A V -- Decker, J M -- New York, N.Y. -- Science. 1985 Aug 2;229(4712):479-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2409603" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): B-Lymphocytes/drug effects ; Chromatography/methods ; Collodion ; Cytotoxicity, Immunologic/drug effects ; Electrophoresis, Polyacrylamide Gel ; Epitopes ; Female ; Hemolytic Plaque Technique ; Humans ; Immunosuppressive Agents/isolation & purification/*urine ; In Vitro Techniques ; Isoelectric Focusing ; Lymphocyte Activation/drug effects ; Molecular Weight ; *Mucoproteins ; Pregnancy ; Pregnancy Proteins/isolation & purification/pharmacology/*urine ; T-Lymphocytes/drug effects ; Uromodulin
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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    AKTUELLE ARTIKEL
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