Potent peptidic fusion inhibitors of influenza virus
Autor: | Bart Stoops, Rob J. Vreeken, Chan Tang, Wim Bert Griet Schepens, Rameshwar U. Kadam, Jaap Goudsmit, Bart Rudolf Romanie Kesteleyn, Maria J. P. van Dongen, Wouter Goutier, Jan Vermond, Ronald Vogels, Boerries Brandenburg, Ian A. Wilson, Jarek Juraszek, Christophe Buyck, Robert H. E. Friesen |
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Rok vydání: | 2017 |
Předmět: |
Male
0301 basic medicine Protein Conformation Viral protein Hemagglutinin (influenza) Complementarity determining region Crystallography X-Ray medicine.disease_cause Antiviral Agents Peptides Cyclic Virus Epitope Mice 03 medical and health sciences Influenza A Virus H1N1 Subtype 0302 clinical medicine Influenza A virus medicine Animals Humans Mice Inbred BALB C Multidisciplinary Influenza A Virus H5N1 Subtype biology Lipid bilayer fusion Virus Internalization Antibodies Neutralizing Complementarity Determining Regions Virology Influenza A virus subtype H5N1 030104 developmental biology Drug Design biology.protein 030217 neurology & neurosurgery |
Zdroj: | Science. 358:496-502 |
ISSN: | 1095-9203 0036-8075 |
Popis: | Broadly reactive drugs for flu Drugs for influenza are limited. For those available, viral resistance is rife. Part of the problem is that the virus is constantly mutating. Kadam et al. tested the cell entry stage of the virus life cycle as a drug target (see the Perspective by Whitehead). Cell entry is mediated by the major surface glycoprotein hemagglutinin (HA). This stage can be blocked by broadly neutralizing antibodies binding to HA. The authors generated small cyclic peptides that bind to the same sites on HA as the antibodies and mimic their activity. The peptides are cheap and easy to synthesize, are nontoxic to mice, and prevented infection of cells by many types of influenza virus. Science , this issue p. 496 ; see also p. 450 |
Databáze: | OpenAIRE |
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