Type II transmembrane serine proteases as potential target for anti-influenza drug discovery.
Identifieur interne : 000D45 ( Main/Exploration ); précédent : 000D44; suivant : 000D46Type II transmembrane serine proteases as potential target for anti-influenza drug discovery.
Auteurs : Woo-Jin Shin [États-Unis] ; Baik Lin Seong [Corée du Sud]Source :
- Expert opinion on drug discovery [ 1746-045X ] ; 2017.
Descripteurs français
- KwdFr :
- Animaux, Antiviraux (pharmacologie), Conception de médicament, Découverte de médicament (), Grippe humaine (traitement médicamenteux), Grippe humaine (virologie), Humains, Orthomyxoviridae (), Orthomyxoviridae (isolement et purification), Réplication virale (), Résistance virale aux médicaments, Serine endopeptidases (métabolisme).
- MESH :
- isolement et purification : Orthomyxoviridae.
- métabolisme : Serine endopeptidases.
- pharmacologie : Antiviraux.
- traitement médicamenteux : Grippe humaine.
- virologie : Grippe humaine.
- Animaux, Conception de médicament, Découverte de médicament, Humains, Orthomyxoviridae, Réplication virale, Résistance virale aux médicaments.
English descriptors
- KwdEn :
- Animals, Antiviral Agents (pharmacology), Drug Design, Drug Discovery (methods), Drug Resistance, Viral, Humans, Influenza, Human (drug therapy), Influenza, Human (virology), Orthomyxoviridae (drug effects), Orthomyxoviridae (isolation & purification), Serine Endopeptidases (metabolism), Virus Replication (drug effects).
- MESH :
- chemical , metabolism : Serine Endopeptidases.
- chemical , pharmacology : Antiviral Agents.
- drug effects : Orthomyxoviridae, Virus Replication.
- drug therapy : Influenza, Human.
- isolation & purification : Orthomyxoviridae.
- methods : Drug Discovery.
- virology : Influenza, Human.
- Animals, Drug Design, Drug Resistance, Viral, Humans.
Abstract
The outbreak of an influenza pandemic as well as the continued circulation of seasonal influenza highlights the need for effective antiviral therapies. The emergence of drug-resistant strains further necessitates the development of novel antivirals that target the host factors crucial for viral replication. Area covered: This review summarizes the current understanding of the structural and functional properties of type II transmembrane serine proteases (TTSPs) as a proteolytic activator of influenza virus infection and discusses their potential as antiviral targets. It also explores the experimental evidence accumulated for inhibitors of TTSPs as novel, broad-spectrum antivirals against various influenza virus subtypes. The review also provides an overview of the properties of small molecules, proteins, and peptides that efficiently inhibit the proteolytic activation of the influenza virus. Expert opinion: TTSPs activate a wide range of influenza virus subtypes including avian influenza viruses, both in vitro and in vivo, via proteolytic cleavage of influenza hemagglutinin (HA) into infection-competent fusogenic conformation. Other viruses such as SARS-, MERS-coronaviruses and human metapneumoviruses may use the same host cell proteases for activation, implying that TTSP inhibition might be a novel strategy for developing broad-spectrum antiviral agents for respiratory viral infections.
DOI: 10.1080/17460441.2017.1372417
PubMed: 28870104
Affiliations:
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Biotechnology, College of Life Science and Biotechnology , Yonsei University , Seoul , South Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>b Department of Biotechnology, College of Life Science and Biotechnology , Yonsei University , Seoul </wicri:regionArea><wicri:noRegion>Seoul </wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:28870104</idno><idno type="pmid">28870104</idno><idno type="doi">10.1080/17460441.2017.1372417</idno><idno type="wicri:Area/PubMed/Corpus">000A82</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000A82</idno><idno type="wicri:Area/PubMed/Curation">000A82</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000A82</idno><idno type="wicri:Area/PubMed/Checkpoint">000A46</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" 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xml:lang="en"><term>Animals</term><term>Antiviral Agents (pharmacology)</term><term>Drug Design</term><term>Drug Discovery (methods)</term><term>Drug Resistance, Viral</term><term>Humans</term><term>Influenza, Human (drug therapy)</term><term>Influenza, Human (virology)</term><term>Orthomyxoviridae (drug effects)</term><term>Orthomyxoviridae (isolation & purification)</term><term>Serine Endopeptidases (metabolism)</term><term>Virus Replication (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antiviraux (pharmacologie)</term><term>Conception de médicament</term><term>Découverte de médicament ()</term><term>Grippe humaine (traitement médicamenteux)</term><term>Grippe humaine (virologie)</term><term>Humains</term><term>Orthomyxoviridae ()</term><term>Orthomyxoviridae (isolement et purification)</term><term>Réplication virale ()</term><term>Résistance virale aux médicaments</term><term>Serine endopeptidases (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Serine Endopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Orthomyxoviridae</term><term>Virus Replication</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="isolation & purification" xml:lang="en"><term>Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Drug Discovery</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Serine endopeptidases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antiviraux</term></keywords><keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Grippe humaine</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Grippe humaine</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Influenza, Human</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Drug Design</term><term>Drug Resistance, Viral</term><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Conception de médicament</term><term>Découverte de médicament</term><term>Humains</term><term>Orthomyxoviridae</term><term>Réplication virale</term><term>Résistance virale aux médicaments</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The outbreak of an influenza pandemic as well as the continued circulation of seasonal influenza highlights the need for effective antiviral therapies. The emergence of drug-resistant strains further necessitates the development of novel antivirals that target the host factors crucial for viral replication. Area covered: This review summarizes the current understanding of the structural and functional properties of type II transmembrane serine proteases (TTSPs) as a proteolytic activator of influenza virus infection and discusses their potential as antiviral targets. It also explores the experimental evidence accumulated for inhibitors of TTSPs as novel, broad-spectrum antivirals against various influenza virus subtypes. The review also provides an overview of the properties of small molecules, proteins, and peptides that efficiently inhibit the proteolytic activation of the influenza virus. Expert opinion: TTSPs activate a wide range of influenza virus subtypes including avian influenza viruses, both in vitro and in vivo, via proteolytic cleavage of influenza hemagglutinin (HA) into infection-competent fusogenic conformation. Other viruses such as SARS-, MERS-coronaviruses and human metapneumoviruses may use the same host cell proteases for activation, implying that TTSP inhibition might be a novel strategy for developing broad-spectrum antiviral agents for respiratory viral infections.</div></front></TEI><affiliations><list><country><li>Corée du Sud</li><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><country name="États-Unis"><region name="Californie"><name sortKey="Shin, Woo Jin" sort="Shin, Woo Jin" uniqKey="Shin W" first="Woo-Jin" last="Shin">Woo-Jin Shin</name></region></country><country name="Corée du Sud"><noRegion><name sortKey="Seong, Baik Lin" sort="Seong, Baik Lin" uniqKey="Seong B" first="Baik Lin" last="Seong">Baik Lin Seong</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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