Type II transmembrane serine proteases as potential target for anti-influenza drug discovery.
Identifieur interne : 000B71 ( PubMed/Corpus ); précédent : 000B70; suivant : 000B72Type II transmembrane serine proteases as potential target for anti-influenza drug discovery.
Auteurs : Woo-Jin Shin ; Baik Lin SeongSource :
- Expert opinion on drug discovery [ 1746-045X ] ; 2017.
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
Links to Exploration step
pubmed:28870104Le document en format XML
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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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28870104</PMID><DateCompleted><Year>2017</Year><Month>10</Month><Day>23</Day></DateCompleted><DateRevised><Year>2018</Year><Month>02</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1746-045X</ISSN><JournalIssue CitedMedium="Internet"><Volume>12</Volume><Issue>11</Issue><PubDate><Year>2017</Year><Month>11</Month></PubDate></JournalIssue><Title>Expert opinion on drug discovery</Title><ISOAbbreviation>Expert Opin Drug Discov</ISOAbbreviation></Journal><ArticleTitle>Type II transmembrane serine proteases as potential target for anti-influenza drug discovery.</ArticleTitle><Pagination><MedlinePgn>1139-1152</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1080/17460441.2017.1372417</ELocationID><Abstract><AbstractText Label="INTRODUCTION">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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shin</LastName><ForeName>Woo-Jin</ForeName><Initials>WJ</Initials><AffiliationInfo><Affiliation>a Department of Molecular Microbiology and Immunology, Keck School of Medicine , University of Southern California , Los Angeles , CA , USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Seong</LastName><ForeName>Baik Lin</ForeName><Initials>BL</Initials><AffiliationInfo><Affiliation>b Department of Biotechnology, College of Life Science and Biotechnology , Yonsei University , Seoul , South Korea.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>c Vaccine Translational Research Center , Yonsei University , Seoul , South Korea.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>09</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Expert Opin Drug Discov</MedlineTA><NlmUniqueID>101295755</NlmUniqueID><ISSNLinking>1746-0441</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="D012697">Serine Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="C421305">TMPRSS2 protein, human</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015195" MajorTopicYN="N">Drug Design</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055808" MajorTopicYN="N">Drug Discovery</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D024882" MajorTopicYN="N">Drug Resistance, Viral</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007251" MajorTopicYN="N">Influenza, Human</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="Y">drug therapy</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009975" MajorTopicYN="N">Orthomyxoviridae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012697" MajorTopicYN="N">Serine Endopeptidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014779" MajorTopicYN="N">Virus Replication</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Influenza virus</Keyword><Keyword MajorTopicYN="Y">antiviral</Keyword><Keyword MajorTopicYN="Y">drug discovery</Keyword><Keyword MajorTopicYN="Y">novel antiviral target</Keyword><Keyword MajorTopicYN="Y">type II transmembrane serine protease</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>9</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>10</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>9</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28870104</ArticleId><ArticleId IdType="doi">10.1080/17460441.2017.1372417</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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