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  • 1
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    TDP-43 suppresses CGG repeat-induced neurotoxicity through interactions with HnRNP A2/B1 (2014)
    Oxford University Press
    Details
    Publication Date: 2014-09-10
    Description: Nucleotide repeat expansions can elicit neurodegeneration as RNA by sequestering specific RNA-binding proteins, preventing them from performing their normal functions. Conversely, mutations in RNA-binding proteins can trigger neurodegeneration at least partly by altering RNA metabolism. In Fragile X-associated tremor/ataxia syndrome (FXTAS), a CGG repeat expansion in the 5'UTR of the fragile X gene ( FMR1 ) leads to progressive neurodegeneration in patients and CGG repeats in isolation elicit toxicity in Drosophila and other animal models. Here, we identify the amyotrophic lateral sclerosis (ALS)-associated RNA-binding protein TAR DNA-binding protein (TDP-43) as a suppressor of CGG repeat-induced toxicity in a Drosophila model of FXTAS. The rescue appears specific to TDP-43, as co-expression of another ALS-associated RNA-binding protein, FUS, exacerbates the toxic effects of CGG repeats. Suppression of CGG RNA toxicity was abrogated by disease-associated mutations in TDP-43. TDP-43 does not co-localize with CGG RNA foci and its ability to bind RNA is not required for rescue. TDP-43-dependent rescue does, however, require fly hnRNP A2/B1 homologues Hrb87F and Hrb98DE. Deletions in the C-terminal domain of TDP-43 that preclude interactions with hnRNP A2/B1 abolish TDP-43-dependent rescue of CGG repeat toxicity. In contrast, suppression of CGG repeat toxicity by hnRNP A2/B1 is not affected by RNAi-mediated knockdown of the fly TDP-43 orthologue, TBPH. Lastly, TDP-43 suppresses CGG repeat-triggered mis-splicing of an hnRNP A2/B1-targeted transcript. These data support a model in which TDP-43 suppresses CGG-mediated toxicity through interactions with hnRNP A2/B1 and suggest a convergence of pathogenic cascades between repeat expansion disorders and RNA-binding proteins implicated in neurodegenerative disease.
    Print ISSN: 0964-6906
    Electronic ISSN: 1460-2083
    Topics: Biology , Medicine
    Published by Oxford University Press
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  • 2
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    Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-11-02
    Description: Respiratory syncytial virus (RSV) is the leading cause of hospitalization for children under 5 years of age. We sought to engineer a viral antigen that provides greater protection than currently available vaccines and focused on antigenic site O, a metastable site specific to the prefusion state of the RSV fusion (F) glycoprotein, as this site is targeted by extremely potent RSV-neutralizing antibodies. Structure-based design yielded stabilized versions of RSV F that maintained antigenic site O when exposed to extremes of pH, osmolality, and temperature. Six RSV F crystal structures provided atomic-level data on how introduced cysteine residues and filled hydrophobic cavities improved stability. Immunization with site O-stabilized variants of RSV F in mice and macaques elicited levels of RSV-specific neutralizing activity many times the protective threshold.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4461862/" 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/PMC4461862/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McLellan, Jason S -- Chen, Man -- Joyce, M Gordon -- Sastry, Mallika -- Stewart-Jones, Guillaume B E -- Yang, Yongping -- Zhang, Baoshan -- Chen, Lei -- Srivatsan, Sanjay -- Zheng, Anqi -- Zhou, Tongqing -- Graepel, Kevin W -- Kumar, Azad -- Moin, Syed -- Boyington, Jeffrey C -- Chuang, Gwo-Yu -- Soto, Cinque -- Baxa, Ulrich -- Bakker, Arjen Q -- Spits, Hergen -- Beaumont, Tim -- Zheng, Zizheng -- Xia, Ningshao -- Ko, Sung-Youl -- Todd, John-Paul -- Rao, Srinivas -- Graham, Barney S -- Kwong, Peter D -- ZIA AI005024-11/Intramural NIH HHS/ -- ZIA AI005061-10/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2013 Nov 1;342(6158):592-8. doi: 10.1126/science.1243283.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24179220" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Neutralizing/immunology ; Antigens, Viral/*chemistry/genetics/immunology ; Crystallography, X-Ray ; Cysteine/chemistry/genetics ; Glycoproteins/*chemistry/genetics/immunology ; Humans ; Macaca ; Mice ; Protein Engineering ; Protein Multimerization ; Protein Stability ; Protein Structure, Tertiary ; Respiratory Syncytial Virus Infections/*prevention & control ; Respiratory Syncytial Virus Vaccines/*chemistry ; Vaccination ; Viral Fusion Proteins/*chemistry/genetics/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Type I interferon responses in rhesus macaques prevent SIV infection and slow disease progression (2014)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2014-07-22
    Description: Inflammation in HIV infection is predictive of non-AIDS morbidity and death, higher set point plasma virus load and virus acquisition; thus, therapeutic agents are in development to reduce its causes and consequences. However, inflammation may simultaneously confer both detrimental and beneficial effects. This dichotomy is particularly applicable to type I interferons (IFN-I) which, while contributing to innate control of infection, also provide target cells for the virus during acute infection, impair CD4 T-cell recovery, and are associated with disease progression. Here we manipulated IFN-I signalling in rhesus macaques (Macaca mulatta) during simian immunodeficiency virus (SIV) transmission and acute infection with two complementary in vivo interventions. We show that blockade of the IFN-I receptor caused reduced antiviral gene expression, increased SIV reservoir size and accelerated CD4 T-cell depletion with progression to AIDS despite decreased T-cell activation. In contrast, IFN-alpha2a administration initially upregulated expression of antiviral genes and prevented systemic infection. However, continued IFN-alpha2a treatment induced IFN-I desensitization and decreased antiviral gene expression, enabling infection with increased SIV reservoir size and accelerated CD4 T-cell loss. Thus, the timing of IFN-induced innate responses in acute SIV infection profoundly affects overall disease course and outweighs the detrimental consequences of increased immune activation. Yet, the clinical consequences of manipulation of IFN signalling are difficult to predict in vivo and therapeutic interventions in human studies should be approached with caution.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4418221/" 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/PMC4418221/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sandler, Netanya G -- Bosinger, Steven E -- Estes, Jacob D -- Zhu, Richard T R -- Tharp, Gregory K -- Boritz, Eli -- Levin, Doron -- Wijeyesinghe, Sathi -- Makamdop, Krystelle Nganou -- del Prete, Gregory Q -- Hill, Brenna J -- Timmer, J Katherina -- Reiss, Emma -- Yarden, Ganit -- Darko, Samuel -- Contijoch, Eduardo -- Todd, John Paul -- Silvestri, Guido -- Nason, Martha -- Norgren, Robert B Jr -- Keele, Brandon F -- Rao, Srinivas -- Langer, Jerome A -- Lifson, Jeffrey D -- Schreiber, Gideon -- Douek, Daniel C -- AI-076174/AI/NIAID NIH HHS/ -- HHSN261200800001E/PHS HHS/ -- P51 OD011132/OD/NIH HHS/ -- R24 RR017444/RR/NCRR NIH HHS/ -- ZIA AI005034-13/Intramural NIH HHS/ -- England -- Nature. 2014 Jul 31;511(7511):601-5. doi: 10.1038/nature13554. Epub 2014 Jul 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Human Immunology Section, Vaccine Research Center, National Institute of Allergy and Infectious Disease, National Institutes of Health, Bethesda, Maryland 20892, USA [2] Division of Infectious Diseases, Department of Internal Medicine, University of Texas Medical Branch at Galveston, Galveston, Texas 77555, USA. ; 1] Division of Microbiology and Immunology, Emory Vaccine Center, Yerkes National Primate Research Center, Atlanta, Georgia 30322, USA [2] Non-Human Primate Genomics Core, Yerkes National Primate Research Center, Robert W. Woodruff Health Sciences Center, Emory University, Atlanta, Georgia 30322, USA. ; AIDS and Cancer Virus Program, Leidos Biomedical Research, Inc., Frederick National Laboratory, Frederick, Maryland 21702, USA. ; Human Immunology Section, Vaccine Research Center, National Institute of Allergy and Infectious Disease, National Institutes of Health, Bethesda, Maryland 20892, USA. ; Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel. ; Laboratory of Animal Medicine, Vaccine Research Center, National Institute of Allergy and Infectious Disease, National Institutes of Health, Bethesda, Maryland 20892, USA. ; Division of Microbiology and Immunology, Emory Vaccine Center, Yerkes National Primate Research Center, Atlanta, Georgia 30322, USA. ; Biostatistics Research Branch, Division of Clinical Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA. ; Department of Genetics, Cell Biology and Anatomy, University of Nebraska Medical Center, Omaha, Nebraska 68198, USA. ; Department of Pharmacology, Rutgers - Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25043006" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antiviral Agents/pharmacology/therapeutic use ; CD4-Positive T-Lymphocytes/drug effects/immunology ; *Disease Progression ; Gene Expression Regulation/drug effects ; Immunity, Innate/drug effects ; Interferon-alpha/pharmacology/*therapeutic use ; Kaplan-Meier Estimate ; Macaca mulatta/*immunology ; Signal Transduction/drug effects ; *Simian Acquired Immunodeficiency Syndrome/drug therapy/immunology/prevention & ; control ; Simian Immunodeficiency Virus/*immunology
    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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  • 4
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    Enhanced neonatal Fc receptor function improves protection against primate SHIV infection (2014)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2014-08-15
    Description: To protect against human immunodeficiency virus (HIV-1) infection, broadly neutralizing antibodies (bnAbs) must be active at the portals of viral entry in the gastrointestinal or cervicovaginal tracts. The localization and persistence of antibodies at these sites is influenced by the neonatal Fc receptor (FcRn), whose role in protecting against infection in vivo has not been defined. Here, we show that a bnAb with enhanced FcRn binding has increased gut mucosal tissue localization, which improves protection against lentiviral infection in non-human primates. A bnAb directed to the CD4-binding site of the HIV-1 envelope (Env) protein (denoted VRC01) was modified by site-directed mutagenesis to increase its binding affinity for FcRn. This enhanced FcRn-binding mutant bnAb, denoted VRC01-LS, displayed increased transcytosis across human FcRn-expressing cellular monolayers in vitro while retaining FcgammaRIIIa binding and function, including antibody-dependent cell-mediated cytotoxicity (ADCC) activity, at levels similar to VRC01 (the wild type). VRC01-LS had a threefold longer serum half-life than VRC01 in non-human primates and persisted in the rectal mucosa even when it was no longer detectable in the serum. Notably, VRC01-LS mediated protection superior to that afforded by VRC01 against intrarectal infection with simian-human immunodeficiency virus (SHIV). These findings suggest that modification of FcRn binding provides a mechanism not only to increase serum half-life but also to enhance mucosal localization that confers immune protection. Mutations that enhance FcRn function could therefore increase the potency and durability of passive immunization strategies to prevent HIV-1 infection.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4433741/" 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/PMC4433741/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ko, Sung-Youl -- Pegu, Amarendra -- Rudicell, Rebecca S -- Yang, Zhi-yong -- Joyce, M Gordon -- Chen, Xuejun -- Wang, Keyun -- Bao, Saran -- Kraemer, Thomas D -- Rath, Timo -- Zeng, Ming -- Schmidt, Stephen D -- Todd, John-Paul -- Penzak, Scott R -- Saunders, Kevin O -- Nason, Martha C -- Haase, Ashley T -- Rao, Srinivas S -- Blumberg, Richard S -- Mascola, John R -- Nabel, Gary J -- DK0034854/DK/NIDDK NIH HHS/ -- DK044319/DK/NIDDK NIH HHS/ -- DK051362/DK/NIDDK NIH HHS/ -- DK053056/DK/NIDDK NIH HHS/ -- DK088199/DK/NIDDK NIH HHS/ -- R01 DK053056/DK/NIDDK NIH HHS/ -- Intramural NIH HHS/ -- England -- Nature. 2014 Oct 30;514(7524):642-5. doi: 10.1038/nature13612. Epub 2014 Aug 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Building 40, Room 4502, MSC-3005, 40 Convent Drive, Bethesda, Maryland 20892-3005, USA. ; 1] Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Building 40, Room 4502, MSC-3005, 40 Convent Drive, Bethesda, Maryland 20892-3005, USA [2] Sanofi, 640 Memorial Drive, Cambridge, Massachusetts 02139, USA (R.S.R., Z.-Y.Y. and G.J.N.); Center for Genetics of Host Defense, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235-8505, USA (M.Z.); University of North Texas System College of Pharmacy, 3500 Camp Bowie Boulevard, RES-340J, Fort Worth, Texas 76107, USA (S.R.P.). ; Division of Gastroenterology, Department of Medicine, Brigham &Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, Massachusetts 02115, USA. ; 1] Department of Microbiology, Medical School, University of Minnesota, 420 Delaware Street South East, Minneapolis, Minnesota 55455, USA [2] Sanofi, 640 Memorial Drive, Cambridge, Massachusetts 02139, USA (R.S.R., Z.-Y.Y. and G.J.N.); Center for Genetics of Host Defense, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235-8505, USA (M.Z.); University of North Texas System College of Pharmacy, 3500 Camp Bowie Boulevard, RES-340J, Fort Worth, Texas 76107, USA (S.R.P.). ; 1] Clinical Pharmacokinetics Laboratory, Pharmacy Department, Clinical Center, National Institutes of Health, Building 10, 10 Center Drive, Bethesda, Maryland 20814, USA [2] Sanofi, 640 Memorial Drive, Cambridge, Massachusetts 02139, USA (R.S.R., Z.-Y.Y. and G.J.N.); Center for Genetics of Host Defense, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235-8505, USA (M.Z.); University of North Texas System College of Pharmacy, 3500 Camp Bowie Boulevard, RES-340J, Fort Worth, Texas 76107, USA (S.R.P.). ; Biostatistics Research Branch, Division of Clinical Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 6700A Rockledge Drive, Room 5235, Bethesda, Maryland 20892, USA. ; Department of Microbiology, Medical School, University of Minnesota, 420 Delaware Street South East, Minneapolis, Minnesota 55455, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25119033" target="_blank"〉PubMed〈/a〉
    Keywords: Administration, Rectal ; Animals ; Antibodies, Neutralizing/analysis/blood/genetics/*immunology ; Antibodies, Viral/analysis/blood/genetics/*immunology ; Antibody Affinity/genetics/immunology ; Antibody-Dependent Cell Cytotoxicity/immunology ; Antigens, CD4/metabolism ; Binding Sites/genetics ; Female ; HIV/chemistry/immunology ; HIV Antibodies/analysis/blood/genetics/immunology ; HIV Envelope Protein gp160/chemistry/immunology ; HIV Infections/*immunology/*prevention & control ; Half-Life ; Histocompatibility Antigens Class I/*immunology ; Immunity, Mucosal/immunology ; Immunization, Passive ; Intestinal Mucosa/immunology ; Macaca mulatta ; Male ; Mice ; Mutagenesis, Site-Directed ; Receptors, Fc/*immunology ; Receptors, IgG/immunology/metabolism ; Rectum/immunology ; Simian Acquired Immunodeficiency Syndrome/*immunology/*prevention & control ; Simian Immunodeficiency Virus/immunology ; Transcytosis
    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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  • 5
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    Immunological and virological mechanisms of vaccine-mediated protection against SIV and HIV (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-12-20
    Description: A major challenge for the development of a highly effective AIDS vaccine is the identification of mechanisms of protective immunity. To address this question, we used a nonhuman primate challenge model with simian immunodeficiency virus (SIV). We show that antibodies to the SIV envelope are necessary and sufficient to prevent infection. Moreover, sequencing of viruses from breakthrough infections revealed selective pressure against neutralization-sensitive viruses; we identified a two-amino-acid signature that alters antigenicity and confers neutralization resistance. A similar signature confers resistance of human immunodeficiency virus (HIV)-1 to neutralization by monoclonal antibodies against variable regions 1 and 2 (V1V2), suggesting that SIV and HIV share a fundamental mechanism of immune escape from vaccine-elicited or naturally elicited antibodies. These analyses provide insight into the limited efficacy seen in HIV vaccine trials.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3946913/" 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/PMC3946913/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roederer, Mario -- Keele, Brandon F -- Schmidt, Stephen D -- Mason, Rosemarie D -- Welles, Hugh C -- Fischer, Will -- Labranche, Celia -- Foulds, Kathryn E -- Louder, Mark K -- Yang, Zhi-Yong -- Todd, John-Paul M -- Buzby, Adam P -- Mach, Linh V -- Shen, Ling -- Seaton, Kelly E -- Ward, Brandy M -- Bailer, Robert T -- Gottardo, Raphael -- Gu, Wenjuan -- Ferrari, Guido -- Alam, S Munir -- Denny, Thomas N -- Montefiori, David C -- Tomaras, Georgia D -- Korber, Bette T -- Nason, Martha C -- Seder, Robert A -- Koup, Richard A -- Letvin, Norman L -- Rao, Srinivas S -- Nabel, Gary J -- Mascola, John R -- AI100645/AI/NIAID NIH HHS/ -- HHSN261200800001E/PHS HHS/ -- HHSN27201100016C/PHS HHS/ -- UM1 AI100645/AI/NIAID NIH HHS/ -- Z99 AI999999/Intramural NIH HHS/ -- ZIA AI005019-12/Intramural NIH HHS/ -- England -- Nature. 2014 Jan 23;505(7484):502-8. doi: 10.1038/nature12893. Epub 2013 Dec 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, NIAID, NIH, Bethesda, Maryland 20892, USA. ; SAIC-Frederick, Frederick National Laboratory, NIH, Frederick, Maryland 21702, USA. ; 1] Vaccine Research Center, NIAID, NIH, Bethesda, Maryland 20892, USA [2] George Washington University, Washington DC 20052, USA. ; Los Alamos National Laboratories, Los Alamos, New Mexico 87545, USA. ; Department of Surgery, Duke University, Durham, North Carolina 27710, USA. ; 1] Vaccine Research Center, NIAID, NIH, Bethesda, Maryland 20892, USA [2] Sanofi-Pasteur, Cambridge, Massachusetts 02139, USA. ; Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02115, USA. ; Human Vaccine Institute, Duke University, Durham, North Carolina 27710, USA. ; Fred Hutchison Cancer Research Center, Seattle, Washington 98109, USA. ; Biostatistics Research Branch, NIAID, NIH, Bethesda, Maryland 20892, USA. ; 1] Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02115, USA [2].〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24352234" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/*immunology ; Amino Acid Sequence ; Animals ; Antibodies, Neutralizing/immunology ; Disease Susceptibility/immunology ; Female ; Founder Effect ; HIV Antibodies/immunology ; HIV Infections/immunology/*prevention & control/*virology ; HIV-1/chemistry/*immunology ; Humans ; Immune Evasion/immunology ; Macaca mulatta ; Male ; Molecular Sequence Data ; Phylogeny ; Risk ; SAIDS Vaccines/*immunology ; Simian Acquired Immunodeficiency Syndrome/immunology/prevention & ; control/virology ; Simian Immunodeficiency Virus/chemistry/genetics/*immunology/physiology ; 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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  • 6
    Electronic Resource
    Electronic Resource
    Extraction of Nucleic Acid-free Lipopolysaccharides from Gram-negative Bacteria (1961)
    [s.l.] : Nature Publishing Group
    Nature 190 (1961), S. 344-345 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] It is known that when the, trichloracetic acid method of Boivin is used to extract the somatic antigen, a considerable amount of the antigen may remain in the residue2. Working with a Pseudomonas species, we have found that the residue left after the dried cells have been treated with ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/190344b0
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  • 7
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    Trispecific broadly neutralizing HIV antibodies mediate potent SHIV protection in macaques (2017)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2017-10-06
    Description: The development of an effective AIDS vaccine has been challenging because of viral genetic diversity and the difficulty of generating broadly neutralizing antibodies (bnAbs). We engineered trispecific antibodies (Abs) that allow a single molecule to interact with three independent HIV-1 envelope determinants: the CD4 binding site, the membrane-proximal external region (MPER), and the V1V2 glycan site. Trispecific Abs exhibited higher potency and breadth than any previously described single bnAb, showed pharmacokinetics similar to those of human bnAbs, and conferred complete immunity against a mixture of simian-human immunodeficiency viruses (SHIVs) in nonhuman primates, in contrast to single bnAbs. Trispecific Abs thus constitute a platform to engage multiple therapeutic targets through a single protein, and they may be applicable for treatment of diverse diseases, including infections, cancer, and autoimmunity.
    Keywords: Immunology, Medicine, Diseases, Virology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Correction: Corrigendum: Protection against malaria at 1 year and immune correlates following PfSPZ vaccination (2016)
    Springer Nature
    Details
    Publication Date: 2016-06-01
    Print ISSN: 1078-8956
    Electronic ISSN: 1546-170X
    Topics: Biology , Medicine
    Published by Springer Nature
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  • 9
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    Protection against malaria at 1 year and immune correlates following PfSPZ vaccination (2016)
    Springer Nature
    Details
    Publication Date: 2016-05-09
    Print ISSN: 1078-8956
    Electronic ISSN: 1546-170X
    Topics: Biology , Medicine
    Published by Springer Nature
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  • 10
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    LATE MIOCENE SEASONAL TO SUBDECADAL CLIMATE VARIABILITY IN THE INDO-WEST PACIFIC (EAST KALIMANTAN, INDONESIA) PRESERVED IN GIANT CLAMS (2015)
    Society for Sedimentary Geology (SEPM)
    In: PALAIOS
    Details
    Publication Date: 2015-02-27
    Description: Two late Miocene Tridacna (giant clam) shells from East Kalimantan (Indonesia) were investigated in order to evaluate their potential as subannually resolved paleoenvironmental archives. Via a combination of X-ray diffraction (XRD), laser ablation–inductively coupled plasma–mass spectrometry (LA-ICPMS) trace element analysis, scanning electron microscopy (SEM) and cathodoluminescence (CL) imaging, pristine versus diagenetically altered domains within the shells were identified. LA-ICPMS transects targeting altered aragonite and calcite zones reveal distinct compositional differences in elemental ratios (B/Ca, Mg/Ca, Sr/Ca/ Ba/Ca, Mn/Ca, Al/Ca, La/Ca, Ce/Ca) relative to primary shell aragonite. Pristine shell domains are characterized by an intact banding pattern of alternating dark and light growth bands, with which spatially resolved LA-ICPMS element/Ca and micromilled 18 O records were aligned. Light 18 O values correspond to dark growth bands, indicating growth during warm seasons. The Mg/Ca and/or Sr/Ca ratios covary with oscillating stable oxygen isotope profiles. Progressive increase in Mg/Ca with age demonstrates that besides temperature, growth kinetics exert control over Mg incorporation. If interpreted as temperature controlled only, 18 O from both shells represents average seasonal sea-surface temperature (SST) variability of 2.7 ± 2.1 and 4.6 ± 1.7 °C, respectively. Using published temperature equations and assuming 18 O sw = –0.88, corresponding mean annual paleo–sea-surface temperatures of 27.8 ± 0.2 and 28.5 ± 0.2 °C are estimated. Although the fossil Tridacna shells were noticeably affected by alteration on their external surfaces, their internal aragonitic structure is, to a large extent, well preserved. These corresponding paleoproxy records provide detailed insight into tropical SST variability of the Indo-Pacific region during the late Miocene.
    Print ISSN: 0883-1351
    Electronic ISSN: 0883-1351
    Topics: Geosciences
    Published by Society for Sedimentary Geology (SEPM)
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