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  • 1
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    Functional and evolutionary insight from the crystal structure of rubella virus protein E1 (2013)
    Nature Publishing Group (NPG)
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    Publication Date: 2013-01-08
    Description: Little is known about the three-dimensional organization of rubella virus, which causes a relatively mild measles-like disease in children but leads to serious congenital health problems when contracted in utero. Although rubella virus belongs to the same family as the mosquito-borne alphaviruses, in many respects it is more similar to other aerosol-transmitted human viruses such as the agents of measles and mumps. Although the use of the triple MMR (measles, mumps and rubella) live vaccine has limited its incidence in western countries, congenital rubella syndrome remains an important health problem in the developing world. Here we report the 1.8 A resolution crystal structure of envelope glycoprotein E1, the main antigen and sole target of neutralizing antibodies against rubella virus. E1 is the main player during entry into target cells owing to its receptor-binding and membrane-fusion functions. The structure reveals the epitope and the neutralization mechanism of an important category of protecting antibodies against rubella infection. It also shows that rubella virus E1 is a class II fusion protein, which had hitherto only been structurally characterized for the arthropod-borne alphaviruses and flaviviruses. In addition, rubella virus E1 has an extensive membrane-fusion surface that includes a metal site, reminiscent of the T-cell immunoglobulin and mucin family of cellular proteins that bind phosphatidylserine lipids at the plasma membrane of cells undergoing apoptosis. Such features have not been seen in any fusion protein crystallized so far. Structural comparisons show that the class II fusion proteins from alphaviruses and flaviviruses, despite belonging to different virus families, are closer to each other than they are to rubella virus E1. This suggests that the constraints on arboviruses imposed by alternating cycles between vertebrates and arthropods resulted in more conservative evolution. By contrast, in the absence of this constraint, the strictly human rubella virus seems to have drifted considerably into a unique niche as sole member of the Rubivirus genus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DuBois, Rebecca M -- Vaney, Marie-Christine -- Tortorici, M Alejandra -- Kurdi, Rana Al -- Barba-Spaeth, Giovanna -- Krey, Thomas -- Rey, Felix A -- England -- Nature. 2013 Jan 24;493(7433):552-6. doi: 10.1038/nature11741. Epub 2013 Jan 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Pasteur, Departement de Virologie, Unite de Virologie Structurale and CNRS URA 3015, F-75724 Paris Cedex 15, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23292515" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; *Biological Evolution ; Cell Line ; Crystallography, X-Ray ; Drosophila melanogaster ; Evolution, Molecular ; Hydrogen-Ion Concentration ; Liposomes/chemistry/metabolism ; Membrane Fusion ; Metals/metabolism ; Models, Molecular ; Protein Multimerization ; Rubella Syndrome, Congenital/virology ; Rubella virus/*chemistry/physiology ; Viral Envelope Proteins/*chemistry/genetics/*metabolism/ultrastructure
    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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    Recognition determinants of broadly neutralizing human antibodies against dengue viruses (2015)
    Nature Publishing Group (NPG)
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    Publication Date: 2015-01-13
    Description: Dengue disease is caused by four different flavivirus serotypes, which infect 390 million people yearly with 25% symptomatic cases and for which no licensed vaccine is available. Recent phase III vaccine trials showed partial protection, and in particular no protection for dengue virus serotype 2 (refs 3, 4). Structural studies so far have characterized only epitopes recognized by serotype-specific human antibodies. We recently isolated human antibodies potently neutralizing all four dengue virus serotypes. Here we describe the X-ray structures of four of these broadly neutralizing antibodies in complex with the envelope glycoprotein E from dengue virus serotype 2, revealing that the recognition determinants are at a serotype-invariant site at the E-dimer interface, including the exposed main chain of the E fusion loop and the two conserved glycan chains. This 'E-dimer-dependent epitope' is also the binding site for the viral glycoprotein prM during virus maturation in the secretory pathway of the infected cell, explaining its conservation across serotypes and highlighting an Achilles' heel of the virus with respect to antibody neutralization. These findings will be instrumental for devising novel immunogens to protect simultaneously against all four serotypes of dengue virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rouvinski, Alexander -- Guardado-Calvo, Pablo -- Barba-Spaeth, Giovanna -- Duquerroy, Stephane -- Vaney, Marie-Christine -- Kikuti, Carlos M -- Navarro Sanchez, M Erika -- Dejnirattisai, Wanwisa -- Wongwiwat, Wiyada -- Haouz, Ahmed -- Girard-Blanc, Christine -- Petres, Stephane -- Shepard, William E -- Despres, Philippe -- Arenzana-Seisdedos, Fernando -- Dussart, Philippe -- Mongkolsapaya, Juthathip -- Screaton, Gavin R -- Rey, Felix A -- 095541/Wellcome Trust/United Kingdom -- Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- England -- Nature. 2015 Apr 2;520(7545):109-13. doi: 10.1038/nature14130. Epub 2015 Jan 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Institut Pasteur, Departement de Virologie, Unite de Virologie Structurale, 75724 Paris Cedex 15, France [2] CNRS UMR 3569 Virologie, 75724 Paris Cedex 15, France. ; 1] Institut Pasteur, Departement de Virologie, Unite de Virologie Structurale, 75724 Paris Cedex 15, France [2] CNRS UMR 3569 Virologie, 75724 Paris Cedex 15, France [3] Universite Paris-Sud, Faculte des Sciences, 91405 Orsay, France. ; Division of Immunology and Inflammation, Department of Medicine, Hammersmith Hospital Campus, Imperial College London, London W12 0NN, UK. ; Institut Pasteur, Proteopole, CNRS UMR 3528, 75724 Paris Cedex 15, France. ; Synchrotron SOLEIL, L'Orme des Merisiers, Saint Aubin, BP48, 91192 Gif-sur-Yvette, France. ; Institut Pasteur, Departement de Virologie, Unite des Interactions Moleculaires Flavivirus-Hotes, 75724 Paris Cedex 15, France. ; Institut Pasteur, Departement de Virologie, Unite de Pathogenie Virale, INSERM U1108, 75724 Paris Cedex 15, France. ; Institut Pasteur de Guyane, BP 6010, 97306 Cayenne, French Guiana. ; 1] Division of Immunology and Inflammation, Department of Medicine, Hammersmith Hospital Campus, Imperial College London, London W12 0NN, UK [2] Dengue Hemorrhagic Fever Research Unit, Office for Research and Development, Faculty of Medicine, Siriraj Hospital, Mahidol University, Bangkok 10700, Thailand. ; 1] Institut Pasteur, Departement de Virologie, Unite de Virologie Structurale, 75724 Paris Cedex 15, France [2] CNRS UMR 3569 Virologie, 75724 Paris Cedex 15, France [3] Institut Pasteur, Proteopole, CNRS UMR 3528, 75724 Paris Cedex 15, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25581790" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Neutralizing/*chemistry/genetics/*immunology ; Antibodies, Viral/*chemistry/genetics/*immunology ; Cross Reactions/immunology ; Crystallography, X-Ray ; Dengue Virus/*chemistry/classification/*immunology ; Epitopes/chemistry/immunology ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutation/genetics ; Protein Conformation ; Protein Multimerization ; Solubility ; Species Specificity ; Viral Envelope Proteins/chemistry/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)
    Location Call Number Expected Availability
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    PAPER CURRENT
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