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Your search keyword '"FUSION-LOOP"' showing total 2 results
Start Over Descriptor "FUSION-LOOP" Topic antibodies, monoclonal
2 results on '"FUSION-LOOP"'

1. Structural basis of potent Zika-dengue virus antibody cross-neutralization

Author

Franz X. Heinz, Juthathip Mongkolsapaya, Ahmed Haouz, Arvind Sharma, Patrick England, Van-Mai Cao-Lormeau, Wanwisa Dejnirattisai, Félix A. Rey, Anavaj Sakuntabhai, Iris Medits, Etienne Simon-Loriere, Gavin R. Screaton, Karin Stiasny, Alexander Rouvinski, Giovanna Barba-Spaeth, Marie Christine Vaney, Virologie Structurale - Structural Virology, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Division of Immunology and Inflammation, Department of Medicine, Imperial College London-Hammersmith Hospital Campus, Medizinische Universität Wien = Medical University of Vienna, Génétique fonctionnelle des Maladies infectieuses - Functional Genetics of Infectious Diseases, Emerging Infectious Diseases, Institut Louis Malardé [Papeete] (ILM), Institut de Recherche pour le Développement (IRD)-Institut de Recherche pour le Développement (IRD), Cristallographie (Plateforme) - Crystallography (Platform), Biophysique des Macromolécules et de leurs Interactions, Siriraj Hospital, Mahidol University, Mahidol University [Bangkok], We acknowledge support from the European Commission FP7 Programme for the DENFREE project under Grant Agreement number 282 378FP7 (F.A.R., J.M., G.R.S. and A.Sa.), the 'Integrative Biology of Emerging Infectious Diseases' Labex (Laboratoire d’Excellence) grant number ANR-10-LABX-62-IBEID (French Government’s 'Investissements d’Avenir' program ) (F.A.R.), the transnational ANR/FWF grant FlaviStem/I1378 (F.A.R. and K.S.), the Medical Research Council, UK (J.M.), the National Institute for Health Research Biomedical Research Centre, Funding Scheme, UK (G.R.S.), and the NEUTRAVIR grant from Région ile-de-France (DIM-Maladies Infectieuses) (P.E., A.H. and F.A.R., ANR-13-ISV8-0002,flavistem,La protéine E des flavivirus : interactions et fusion membranaire(2013), ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010), European Project: 282378,EC:FP7:HEALTH,FP7-HEALTH-2011-single-stage,DENFREE(2012), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Medical Research Council (MRC), Wellcome Trust, and Commission of the European Communities

Subjects
DYNAMICS, 0301 basic medicine, Models, Molecular, viruses, [SDV]Life Sciences [q-bio], Antigen-Antibody Complex, Dengue virus, medicine.disease_cause, Crystallography, X-Ray, Epitope, Zika virus, Dengue fever, Dengue, Epitopes, 0302 clinical medicine, Viral Envelope Proteins, INFECTION, Virus maturation, IN-VIVO, FLAVIVIRUSES, Phylogeny, Multidisciplinary, Zika Virus Infection, Antibodies, Monoclonal, REACTIVE ANTIBODIES, FUSION-LOOP, 3. Good health, Multidisciplinary Sciences, Flavivirus, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Science & Technology - Other Topics, Brazil, General Science & Technology, Dengue Vaccines, Biology, Cross Reactions, MATURATION, Microbiology, 03 medical and health sciences, ENHANCEMENT, medicine, Humans, Antibody-dependent enhancement, Dengue vaccine, Science & Technology, RECEPTOR, RECOGNITION, Viral Vaccines, Zika Virus, Dengue Virus, biology.organism_classification, medicine.disease, Virology, Antibodies, Neutralizing, 030104 developmental biology, 030217 neurology & neurosurgery
Abstract

International audience; Zika virus is a member of the Flavivirus genus that had not been associated with severe disease in humans until the recent outbreaks, when it was linked to microcephaly in newborns in Brazil and to Guillain-Barré syndrome in adults in French Polynesia. Zika virus is related to dengue virus, and here we report that a subset of antibodies targeting a conformational epitope isolated from patients with dengue virus also potently neutralize Zika virus. The crystal structure of two of these antibodies in complex with the envelope protein of Zika virus reveals the details of a conserved epitope, which is also the site of interaction of the envelope protein dimer with the precursor membrane (prM) protein during virus maturation. Comparison of the Zika and dengue virus immunocomplexes provides a lead for rational, epitope-focused design of a universal vaccine capable of eliciting potent cross-neutralizing antibodies to protect simultaneously against both Zika and dengue virus infections.

Published
2016
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2. A new class of highly potent, broadly neutralizing antibodies isolated from viremic patients infected with dengue virus

Author

Xinghong Dai, Gavin R. Screaton, Wiyada Wongwiwat, Thaneeya Duangchinda, Jeremy Farrar, Z. Hong Zhou, Xiaokang Zhang, Carolyn Edwards, Cameron P. Simmons, Jonathan M. Grimes, Sunpetchuda Supasa, Chih Yun Lai, Wei-Kung Wang, Nguyen Than Ha Quyen, Wanwisa Dejnirattisai, Félix A. Rey, Prida Malasit, Juthathip Mongkolsapaya, Wen-Yang Tsai, Alexander Rouvinsky, Amonrat Jumnainsong, Wellcome Trust, Commission of the European Communities, and Medical Research Council (MRC)

Subjects
TICK-BORNE ENCEPHALITIS, Dengue virus, medicine.disease_cause, Epitope, Neutralization, Dengue fever, Dengue, Viral Envelope Proteins, Monoclonal, Immunology and Allergy, IMMUNE-RESPONSE, Neutralizing, Antibodies, Monoclonal, ENVELOPE GLYCOPROTEIN, FUSION-LOOP, Infectious Diseases, 1107 Immunology, Biological Assay, Antibody, Infection, Life Sciences & Biomedicine, Biotechnology, medicine.drug_class, Immunology, Immunoblotting, Enzyme-Linked Immunosorbent Assay, Biology, MEMBRANE-FUSION, Monoclonal antibody, Virus, Antibodies, Article, MATURATION, Cell Line, Vaccine Related, Rare Diseases, Immunity, Biodefense, medicine, Animals, Humans, Science & Technology, Prevention, HUMAN MONOCLONAL-ANTIBODIES, Dengue Virus, medicine.disease, Virology, Antibodies, Neutralizing, Vector-Borne Diseases, Emerging Infectious Diseases, Good Health and Well Being, HEMORRHAGIC-FEVER, biology.protein, T-CELLS, Immunization, STRUCTURAL-CHANGES
Abstract

Dengue is a rapidly emerging, mosquito-borne viral infection, with an estimated 400 million infections occurring annually. To gain insight into dengue immunity, we characterized 145 human monoclonal antibodies (mAbs) and identified a previously unknown epitope, the envelope dimer epitope (EDE), that bridges two envelope protein subunits that make up the 90 repeating dimers on the mature virion. The mAbs to EDE were broadly reactive across the dengue serocomplex and fully neutralized virus produced in either insect cells or primary human cells, with 50% neutralization in the low picomolar range. Our results provide a path to a subunit vaccine against dengue virus and have implications for the design and monitoring of future vaccine trials in which the induction of antibody to the EDE should be prioritized.

Published
2014

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