6 results on '"Moscona, Anne"'
Search Results
2. Rapid Screening for Entry Inhibitors of Highly Pathogenic Viruses under Low-Level Biocontainment
- Author
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Talekar, Aparna, primary, Pessi, Antonello, additional, Glickman, Fraser, additional, Sengupta, Uttara, additional, Briese, Thomas, additional, Whitt, Michael A., additional, Mathieu, Cyrille, additional, Horvat, Branka, additional, Moscona, Anne, additional, and Porotto, Matteo, additional
- Published
- 2012
- Full Text
- View/download PDF
3. Synthetic Protocells Interact with Viral Nanomachinery and Inactivate Pathogenic Human Virus
- Author
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Porotto, Matteo, primary, Yi, Feng, additional, Moscona, Anne, additional, and LaVan, David A., additional
- Published
- 2011
- Full Text
- View/download PDF
4. Rapid Screening for Entry Inhibitors of Highly Pathogenic Viruses under Low-Level Biocontainment
- Author
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Branka Horvat, Cyrille Mathieu, Aparna Talekar, Uttara Sengupta, Anne Moscona, Michael A. Whitt, Fraser Glickman, Antonello Pessi, Thomas Briese, Matteo Porotto, Talekar, Aparna, Pessi, Antonello, Glickman, Fraser, Sengupta, Uttara, Briese, Thoma, Whitt, Michael A., Mathieu, Cyrille, Horvat, Branka, Moscona, Anne, Porotto, Matteo, Immunobiologie des infections virales – Immunobiology of Viral Infections (IbIV), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre International de Recherche en Infectiologie (CIRI), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
Viral Diseases ,viruses ,Drug Evaluation, Preclinical ,lcsh:Medicine ,Cercopithecus aethiop ,Virus Replication ,HEK293 Cell ,Chlorocebus aethiops ,lcsh:Science ,ComputingMilieux_MISCELLANEOUS ,Lujo virus ,0303 health sciences ,Multidisciplinary ,biology ,Transmission (medicine) ,Medicine (all) ,Zoonosis ,virus diseases ,Infectious Diseases ,[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology ,Medicine ,Immunotherapy ,Research Article ,Neglected Tropical Diseases ,Henipavirus ,Human ,DNA, Complementary ,Immunology ,Microbiology ,Antiviral Agents ,Hendra Virus ,03 medical and health sciences ,Virology ,medicine ,Animals ,Humans ,Technology, Pharmaceutical ,Hendra Viru ,Biology ,Vero Cells ,030304 developmental biology ,Antiviral Agent ,Biochemistry, Genetics and Molecular Biology (all) ,030306 microbiology ,Animal ,lcsh:R ,Nipah Virus ,Computational Biology ,biology.organism_classification ,medicine.disease ,Biocontainment ,Antibodies, Neutralizing ,Rats ,HEK293 Cells ,Nipah Viru ,Viral replication ,Agricultural and Biological Sciences (all) ,Junin virus ,Vero Cell ,Rat ,Clinical Immunology ,lcsh:Q - Abstract
Emerging viruses including Nipah, Hendra, Lujo, and Junin viruses have enormous potential to spread rapidly. Nipah virus, after emerging as a zoonosis, has also evolved the capacity for human-to-human transmission. Most of the diseases caused by these pathogens are untreatable and require high biocontainment conditions. Universal methods for rapidly identifying and screening candidate antivirals are urgently needed. We have developed a modular antiviral platform strategy that relies on simple bioinformatic and genetic information about each pathogen. Central to this platform is the use of envelope glycoprotein cDNAs to establish multi-cycle replication systems under BSL2 conditions for viral pathogens that normally require BSL3 and BSL4 facilities. We generated monoclonal antibodies against Nipah G by cDNA immunization in rats, and we showed that these antibodies neutralize both Nipah and Hendra live viruses. We then used these effective Henipavirus inhibitors to validate our screening strategy. Our proposed strategy should contribute to the response capability for emerging infectious diseases, providing a way to initiate antiviral development immediately upon identifying novel viruses. © 2012 Talekar et al.
- Published
- 2012
- Full Text
- View/download PDF
5. A general strategy to endow natural fusion-protein-derived peptides with potent antiviral activity
- Author
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Branka Horvat, Annunziata Langella, Antonello Pessi, Riccardo Cortese, Thomas J. Ketas, Guido Poli, Cyrille Mathieu, Matteo Porotto, Elisa Vicenzi, Silvia Ghezzi, Elena Capito, Anne Moscona, Pessi, A, Langella, A, Capito, E, Ghezzi, S, Vicenzi, E, Poli, Guido, Ketas, T, Mathieu, C, Cortese, R, Horvat, B, Moscona, A, Porotto, M., CEINGE, Okairos, Virologie humaine, École normale supérieure - Lyon (ENS Lyon)-IFR128-Institut National de la Santé et de la Recherche Médicale (INSERM), École normale supérieure de Lyon (ENS de Lyon)-IFR128-Institut National de la Santé et de la Recherche Médicale (INSERM), Pessi, Antonello, Langella, Annunziata, Capitã², Elena, Ghezzi, Silvia, Vicenzi, Elisa, Ketas, Thoma, Mathieu, Cyrille, Cortese, Riccardo, Horvat, Branka, Moscona, Anne, and Porotto, Matteo
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[SDV]Life Sciences [q-bio] ,viruses ,lcsh:Medicine ,MESH: Cricetinae ,MESH: Amino Acid Sequence ,MESH: Drug Design ,HeLa Cell ,Virus Replication ,MESH: Protein Structure, Tertiary ,MESH: Cholesterol ,Peptide Fragment ,Infectious Diseases of the Nervous System ,Cricetinae ,Zoonoses ,MESH: Animals ,lcsh:Science ,MESH: Peptide Fragments ,Viral Fusion Protein ,Peptide sequence ,0303 health sciences ,Multidisciplinary ,Cell fusion ,MESH: Protein Multimerization ,030302 biochemistry & molecular biology ,Applied Chemistry ,Chemical Engineering ,3. Good health ,AIDS ,Chemistry ,Cholesterol ,Veterinary Diseases ,MESH: Viral Fusion Proteins ,Biological Product ,Medicine ,Infectious diseases ,MESH: RNA Viruses ,Human ,Research Article ,MESH: Antiviral Agents ,MESH: Biological Products ,Molecular Sequence Data ,HIV prevention ,Sexually Transmitted Diseases ,Viral diseases ,Biology ,Antiviral Agents ,Virus ,Hendra Virus ,03 medical and health sciences ,Viral envelope ,Viral entry ,Chemical Biology ,Animals ,Humans ,RNA Viruses ,Amino Acid Sequence ,Henipavirus ,030304 developmental biology ,Antiviral Agent ,RNA Viruse ,Biological Products ,Biochemistry, Genetics and Molecular Biology (all) ,MESH: Humans ,MESH: Molecular Sequence Data ,Animal ,lcsh:R ,MESH: Virus Replication ,Lipid bilayer fusion ,HIV ,Veterinary Virology ,Fusion protein ,Virology ,Peptide Fragments ,Protein Structure, Tertiary ,Agricultural and Biological Sciences (all) ,Viral replication ,Drug Design ,MESH: HeLa Cells ,lcsh:Q ,Veterinary Science ,Protein Multimerization ,Human Parainfluenza Virus Infection ,Viral Fusion Proteins ,HeLa Cells - Abstract
International audience; Fusion between the viral and target cell membranes is an obligatory step for the infectivity of all enveloped virus, and blocking this process is a clinically validated therapeutic strategy.Viral fusion is driven by specialized proteins which, although specific to each virus, act through a common mechanism, the formation of a complex between two heptad repeat (HR) regions. The HR regions are initially separated in an intermediate termed "prehairpin", which bridges the viral and cell membranes, and then fold onto each other to form a 6-helical bundle (6HB), driving the two membranes to fuse. HR-derived peptides can inhibit viral infectivity by binding to the prehairpin intermediate and preventing its transition to the 6HB.The antiviral activity of HR-derived peptides differs considerably among enveloped viruses. For weak inhibitors, potency can be increased by peptide engineering strategies, but sequence-specific optimization is time-consuming. In seeking ways to increase potency without changing the native sequence, we previously reported that attachment to the HR peptide of a cholesterol group ("cholesterol-tagging") dramatically increases its antiviral potency, and simultaneously increases its half-life in vivo. We show here that antiviral potency may be increased by combining cholesterol-tagging with dimerization of the HR-derived sequence, using as examples human parainfluenza virus, Nipah virus, and HIV-1. Together, cholesterol-tagging and dimerization may represent strategies to boost HR peptide potency to levels that in some cases may be compatible with in vivo use, possibly contributing to emergency responses to outbreaks of existing or novel viruses.
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- 2011
6. Synthetic protocells interact with viral nanomachinery and inactivate pathogenic human virus
- Author
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Feng Yi, Matteo Porotto, David A. LaVan, Anne Moscona, Porotto, Matteo, Yi, Feng, Moscona, Anne, and Lavan, David A.
- Subjects
viruses ,lcsh:Medicine ,02 engineering and technology ,Nanoparticle ,Engineering ,Biomimetics ,Emerging Viral Diseases ,Receptors, Viru ,Biological Systems Engineering ,Nanotechnology ,lcsh:Science ,Membrane Protein ,0303 health sciences ,Multidisciplinary ,biology ,Medicine (all) ,Systems Biology ,Temperature ,021001 nanoscience & nanotechnology ,Antivirals ,3. Good health ,Vesicular stomatitis virus ,Receptors, Virus ,Synthetic Biology ,0210 nano-technology ,Human ,Henipavirus ,Research Article ,Protein Binding ,Protocell ,Materials Science ,Bioengineering ,Microbiology ,Virus ,Hendra Virus ,03 medical and health sciences ,Viral Proteins ,Viral envelope ,Virology ,Viral Protein ,Humans ,Hendra Viru ,Biology ,030304 developmental biology ,Biochemistry, Genetics and Molecular Biology (all) ,Cell Membrane ,lcsh:R ,Nipah Virus ,Lipid bilayer fusion ,Membrane Proteins ,biology.organism_classification ,Nipah Viru ,Agricultural and Biological Sciences (all) ,Solubility ,Bionanotechnology ,Nanoparticles ,Virus Inactivation ,Artificial Cells ,lcsh:Q ,Human Virus ,Artificial Cell - Abstract
We present a new antiviral strategy and research tool that could be applied to a wide range of enveloped viruses that infect human beings via membrane fusion. We test this strategy on two emerging zoonotic henipaviruses that cause fatal encephalitis in humans, Nipah (NiV) and Hendra (HeV) viruses. In the new approach, artificial cell-like particles (protocells) presenting membrane receptors in a biomimetic manner were developed and found to attract and inactivate henipavirus envelope glycoprotein pseudovirus particles, preventing infection. The protocells do not accumulate virus during the inactivation process. The use of protocells that interact with, but do not accumulate, viruses may provide significant advantages over current antiviral drugs, and this general approach may have wide potential for antiviral development.
- Published
- 2011
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