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Multifunctional Pan-ebolavirus Antibody Recognizes a Site of Broad Vulnerability on the Ebolavirus Glycoprotein.
Gilchuk, Pavlo; Kuzmina, Natalia; Ilinykh, Philipp A; Huang, Kai; Gunn, Bronwyn M; Bryan, Aubrey; Davidson, Edgar; Doranz, Benjamin J; Turner, Hannah L; Fusco, Marnie L; Bramble, Matthew S; Hoff, Nicole A; Binshtein, Elad; Kose, Nurgun; Flyak, Andrew I; Flinko, Robin; Orlandi, Chiara; Carnahan, Robert; Parrish, Erica H; Sevy, Alexander M; Bombardi, Robin G; Singh, Prashant K; Mukadi, Patrick; Muyembe-Tamfum, Jean Jacques; Ohi, Melanie D; Saphire, Erica Ollmann; Lewis, George K; Alter, Galit; Ward, Andrew B; Rimoin, Anne W; Bukreyev, Alexander; Crowe, James E.
Afiliação
  • Gilchuk P; Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
  • Kuzmina N; Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA; Galveston National Laboratory, Galveston, TX 77550, USA.
  • Ilinykh PA; Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA; Galveston National Laboratory, Galveston, TX 77550, USA.
  • Huang K; Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA; Galveston National Laboratory, Galveston, TX 77550, USA.
  • Gunn BM; Ragon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USA.
  • Bryan A; Integral Molecular, Inc., Philadelphia, PA 19104, USA.
  • Davidson E; Integral Molecular, Inc., Philadelphia, PA 19104, USA.
  • Doranz BJ; Integral Molecular, Inc., Philadelphia, PA 19104, USA.
  • Turner HL; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • Fusco ML; The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • Bramble MS; Department of Epidemiology, Jonathan and Karin Fielding School of Public Health, University of California, Los Angeles, Los Angeles, CA 90095, USA; Department of Genetic Medicine Research, Children's Research Institute, Children's National Medical Center, Washington, DC 20010, USA.
  • Hoff NA; Department of Epidemiology, Jonathan and Karin Fielding School of Public Health, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Binshtein E; Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232, USA.
  • Kose N; Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
  • Flyak AI; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
  • Flinko R; Division of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
  • Orlandi C; Division of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
  • Carnahan R; Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
  • Parrish EH; Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
  • Sevy AM; Chemical and Physical Biology Program, Vanderbilt University, Nashville, TN 37232, USA.
  • Bombardi RG; Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
  • Singh PK; Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232, USA.
  • Mukadi P; Institut Nationale de Recherche Biomédicale, Kinshasa, Democratic Republic of the Congo.
  • Muyembe-Tamfum JJ; Institut Nationale de Recherche Biomédicale, Kinshasa, Democratic Republic of the Congo.
  • Ohi MD; Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232, USA.
  • Saphire EO; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA; Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA; The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La J
  • Lewis GK; Division of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
  • Alter G; Ragon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USA.
  • Ward AB; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • Rimoin AW; Department of Epidemiology, Jonathan and Karin Fielding School of Public Health, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  • Bukreyev A; Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA; Galveston National Laboratory, Galveston, TX 77550, USA; Department of Microbiology & Immunology, University of Texas Medical Branch, Galveston, TX 77555, USA. Electronic address: alexander.bukreyev@utmb.edu.
  • Crowe JE; Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA; Chemical and Physical Biology Program, Vanderbilt University, Nashville, TN 37232, USA; De
Immunity ; 49(2): 363-374.e10, 2018 08 21.
Article em En | MEDLINE | ID: mdl-30029854
ABSTRACT
Ebolaviruses cause severe disease in humans, and identification of monoclonal antibodies (mAbs) that are effective against multiple ebolaviruses are important for therapeutics development. Here we describe a distinct class of broadly neutralizing human mAbs with protective capacity against three ebolaviruses infectious for humans Ebola (EBOV), Sudan (SUDV), and Bundibugyo (BDBV) viruses. We isolated mAbs from human survivors of ebolavirus disease and identified a potent mAb, EBOV-520, which bound to an epitope in the glycoprotein (GP) base region. EBOV-520 efficiently neutralized EBOV, BDBV, and SUDV and also showed protective capacity in relevant animal models of these infections. EBOV-520 mediated protection principally by direct virus neutralization and exhibited multifunctional properties. This study identified a potent naturally occurring mAb and defined key features of the human antibody response that may contribute to broad protection. This multifunctional mAb and related clones are promising candidates for development as broadly protective pan-ebolavirus therapeutic molecules.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Glicoproteínas / Doença pelo Vírus Ebola / Ebolavirus / Anticorpos Neutralizantes / Anticorpos Monoclonais / Anticorpos Antivirais Limite: Adult / Animals / Female / Humans / Male Idioma: En Ano de publicação: 2018 Tipo de documento: Article
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Glicoproteínas / Doença pelo Vírus Ebola / Ebolavirus / Anticorpos Neutralizantes / Anticorpos Monoclonais / Anticorpos Antivirais Limite: Adult / Animals / Female / Humans / Male Idioma: En Ano de publicação: 2018 Tipo de documento: Article