Novel insights into proteolytic cleavage of influenza virus hemagglutinin
Identifieur interne : 002760 ( Main/Exploration ); précédent : 002759; suivant : 002761Novel insights into proteolytic cleavage of influenza virus hemagglutinin
Auteurs : Stephanie Bertram [Allemagne] ; Ilona Glowacka [Allemagne] ; Imke Steffen [Allemagne] ; Annika Kühl [Allemagne] ; Stefan Pöhlmann [Allemagne]Source :
- Reviews in Medical Virology [ 1052-9276 ] ; 2010-09.
English descriptors
- Teeft :
- Acad, Activation, Airway, Antiviral, Arginine, Attractive targets, Avian, Avian viruses, Bertram, Biol, Biol chem, Cell surface, Cellular proteases, Cleavage, Cleavage site, Copyright, Epithelial, Epithelial cells, Epithelium, Extracellular, Extracellular space, Furin, Fusion peptide, Glycoprotein, Hemagglutinin, Host cell proteases, Hpaiv, Human airway protease, Human viruses, Inhibitor, John wiley sons, Kawaoka, Klenk, Linker sequence, Lpaiv, Lung epithelial cells, Mdck cells, Membrane, Membrane fusion, Monobasic, Monobasic cleavage site, Multibasic, Multibasic cleavage site, Natl, Neuraminidase, Pandemic, Pathogenic, Pathogenicity, Peptide, Plasma membrane, Plasminogen, Plasminogen recruitment, Proc, Proc natl acad, Protease, Protease domain, Protease inhibitors, Proteolytic, Proteolytic activation, Proteolytic cleavage, Receptor, Secretory pathway, Serine, Sialic acids, Soluble proteases, Subtypes, Target cell membrane, Target cell vesicles, Target cells, Therapeutic intervention, Tmprss2, Tmprss4, Transmembrane, Transmembrane domain, Transmembrane serine proteases, Trypsin, Ttsp, Ttsp family, Ttsps, Viral, Viral spread, Viral tropism, Virol, Virology, Virus, Virus entry, Virus hemagglutinin, Virus infection, Virus pathogenicity, Virus spread.
Abstract
The influenza virus hemagglutinin (HA) mediates the first essential step in the viral life cycle, virus entry into target cells. Influenza virus HA is synthesised as a precursor protein in infected cells and requires cleavage by host cell proteases to transit into an active form. Cleavage is essential for influenza virus infectivity and the HA‐processing proteases are attractive targets for therapeutic intervention. It is well established that cleavage by ubiquitously expressed subtilisin‐like proteases is a hallmark of highly pathogenic avian influenza viruses (HPAIV). In contrast, the nature of the proteases responsible for cleavage of HA of human influenza viruses and low pathogenic avian influenza viruses (LPAIV) is not well understood. Recent studies suggest that cleavage of HA of human influenza viruses might be a cell‐associated event and might be facilitated by the type II transmembrane serine proteases (TTSPs) TMPRSS2, TMPRSS4 and human airway trypsin‐like protease (HAT). Here, we will introduce the different concepts established for proteolytic activation of influenza virus HA, with a particular focus on the role of TTSPs, and we will discuss their implications for viral tropism, pathogenicity and antiviral intervention. Copyright © 2010 John Wiley & Sons, Ltd.
Url:
DOI: 10.1002/rmv.657
Affiliations:
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from="298">298</biblScope><biblScope unit="page" to="310">310</biblScope><biblScope unit="page-count">13</biblScope><publisher>John Wiley & Sons, Ltd.</publisher><pubPlace>Chichester, UK</pubPlace><date type="published" when="2010-09">2010-09</date></imprint><idno type="ISSN">1052-9276</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1052-9276</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Activation</term><term>Airway</term><term>Antiviral</term><term>Arginine</term><term>Attractive targets</term><term>Avian</term><term>Avian viruses</term><term>Bertram</term><term>Biol</term><term>Biol chem</term><term>Cell surface</term><term>Cellular proteases</term><term>Cleavage</term><term>Cleavage site</term><term>Copyright</term><term>Epithelial</term><term>Epithelial cells</term><term>Epithelium</term><term>Extracellular</term><term>Extracellular space</term><term>Furin</term><term>Fusion 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cleavage</term><term>Receptor</term><term>Secretory pathway</term><term>Serine</term><term>Sialic acids</term><term>Soluble proteases</term><term>Subtypes</term><term>Target cell membrane</term><term>Target cell vesicles</term><term>Target cells</term><term>Therapeutic intervention</term><term>Tmprss2</term><term>Tmprss4</term><term>Transmembrane</term><term>Transmembrane domain</term><term>Transmembrane serine proteases</term><term>Trypsin</term><term>Ttsp</term><term>Ttsp family</term><term>Ttsps</term><term>Viral</term><term>Viral spread</term><term>Viral tropism</term><term>Virol</term><term>Virology</term><term>Virus</term><term>Virus entry</term><term>Virus hemagglutinin</term><term>Virus infection</term><term>Virus pathogenicity</term><term>Virus spread</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The influenza virus hemagglutinin (HA) mediates the first essential step in the viral life cycle, virus entry into target cells. Influenza virus HA is synthesised as a precursor protein in infected cells and requires cleavage by host cell proteases to transit into an active form. Cleavage is essential for influenza virus infectivity and the HA‐processing proteases are attractive targets for therapeutic intervention. It is well established that cleavage by ubiquitously expressed subtilisin‐like proteases is a hallmark of highly pathogenic avian influenza viruses (HPAIV). In contrast, the nature of the proteases responsible for cleavage of HA of human influenza viruses and low pathogenic avian influenza viruses (LPAIV) is not well understood. Recent studies suggest that cleavage of HA of human influenza viruses might be a cell‐associated event and might be facilitated by the type II transmembrane serine proteases (TTSPs) TMPRSS2, TMPRSS4 and human airway trypsin‐like protease (HAT). Here, we will introduce the different concepts established for proteolytic activation of influenza virus HA, with a particular focus on the role of TTSPs, and we will discuss their implications for viral tropism, pathogenicity and antiviral intervention. Copyright © 2010 John Wiley & Sons, Ltd.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country><region><li>Basse-Saxe</li></region><settlement><li>Hanovre</li></settlement></list><tree><country name="Allemagne"><region name="Basse-Saxe"><name sortKey="Bertram, Stephanie" sort="Bertram, Stephanie" uniqKey="Bertram S" first="Stephanie" last="Bertram">Stephanie Bertram</name></region><name sortKey="Glowacka, Ilona" sort="Glowacka, Ilona" uniqKey="Glowacka I" first="Ilona" last="Glowacka">Ilona Glowacka</name><name sortKey="Kuhl, Annika" sort="Kuhl, Annika" uniqKey="Kuhl A" first="Annika" last="Kühl">Annika Kühl</name><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name><name sortKey="Steffen, Imke" sort="Steffen, Imke" uniqKey="Steffen I" first="Imke" last="Steffen">Imke Steffen</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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