SPINT2 inhibits proteases involved in activation of both influenza viruses and metapneumoviruses
Identifieur interne : 001046 ( Ncbi/Merge ); précédent : 001045; suivant : 001047SPINT2 inhibits proteases involved in activation of both influenza viruses and metapneumoviruses
Auteurs : Marco R. Straus [États-Unis] ; Jonathan T. Kinder [États-Unis] ; Michal Segall [États-Unis] ; Rebecca Ellis Dutch [États-Unis] ; Gary R. Whittaker [États-Unis]Source :
- Virology [ 0042-6822 ] ; 2020.
Abstract
Viruses possessing class I fusion proteins require proteolytic activation by host cell proteases to mediate fusion with the host cell membrane. The mammalian SPINT2 gene encodes a protease inhibitor that targets trypsin-like serine proteases. Here we show the protease inhibitor, SPINT2, restricts cleavage-activation efficiently for a range of influenza viruses and for human metapneumovirus (HMPV). SPINT2 treatment resulted in the cleavage and fusion inhibition of full-length influenza A/CA/04/09 (H1N1) HA, A/Aichi/68 (H3N2) HA, A/Shanghai/2/2013 (H7N9) HA and HMPV F when activated by trypsin, recombinant matriptase or KLK5. We also demonstrate that SPINT2 was able to reduce viral growth of influenza A/CA/04/09 H1N1 and A/X31 H3N2 in cell culture by inhibiting matriptase or TMPRSS2. Moreover, inhibition efficacy did not differ whether SPINT2 was added at the time of infection or 24 h post-infection. Our data suggest that the SPINT2 inhibitor has a strong potential to serve as a novel broad-spectrum antiviral.
Url:
DOI: 10.1016/j.virol.2020.01.004
PubMed: 32056846
PubMed Central: 7112099
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<front><div type="abstract" xml:lang="en"><p>Viruses possessing class I fusion proteins require proteolytic activation by host cell proteases to mediate fusion with the host cell membrane. The mammalian SPINT2 gene encodes a protease inhibitor that targets trypsin-like serine proteases. Here we show the protease inhibitor, SPINT2, restricts cleavage-activation efficiently for a range of influenza viruses and for human metapneumovirus (HMPV). SPINT2 treatment resulted in the cleavage and fusion inhibition of full-length influenza A/CA/04/09 (H1N1) HA, A/Aichi/68 (H3N2) HA, A/Shanghai/2/2013 (H7N9) HA and HMPV F when activated by trypsin, recombinant matriptase or KLK5. We also demonstrate that SPINT2 was able to reduce viral growth of influenza A/CA/04/09 H1N1 and A/X31 H3N2 in cell culture by inhibiting matriptase or TMPRSS2. Moreover, inhibition efficacy did not differ whether SPINT2 was added at the time of infection or 24 h post-infection. Our data suggest that the SPINT2 inhibitor has a strong potential to serve as a novel broad-spectrum antiviral.</p>
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<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Virology</journal-id>
<journal-id journal-id-type="iso-abbrev">Virology</journal-id>
<journal-title-group><journal-title>Virology</journal-title>
</journal-title-group>
<issn pub-type="ppub">0042-6822</issn>
<issn pub-type="epub">1096-0341</issn>
<publisher><publisher-name>Elsevier Inc.</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">32056846</article-id>
<article-id pub-id-type="pmc">7112099</article-id>
<article-id pub-id-type="publisher-id">S0042-6822(20)30004-0</article-id>
<article-id pub-id-type="doi">10.1016/j.virol.2020.01.004</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>SPINT2 inhibits proteases involved in activation of both influenza viruses and metapneumoviruses</article-title>
</title-group>
<contrib-group><contrib contrib-type="author" id="au1"><name><surname>Straus</surname>
<given-names>Marco R.</given-names>
</name>
<email>mrs393@cornell.edu</email>
<xref rid="aff1" ref-type="aff">a</xref>
<xref rid="fn1" ref-type="fn">1</xref>
</contrib>
<contrib contrib-type="author" id="au2"><name><surname>Kinder</surname>
<given-names>Jonathan T.</given-names>
</name>
<xref rid="aff2" ref-type="aff">b</xref>
<xref rid="fn1" ref-type="fn">1</xref>
</contrib>
<contrib contrib-type="author" id="au3"><name><surname>Segall</surname>
<given-names>Michal</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author" id="au4"><name><surname>Dutch</surname>
<given-names>Rebecca Ellis</given-names>
</name>
<email>rebecca.dutch@uky.edu</email>
<xref rid="aff2" ref-type="aff">b</xref>
<xref rid="cor1" ref-type="corresp">∗</xref>
</contrib>
<contrib contrib-type="author" id="au5"><name><surname>Whittaker</surname>
<given-names>Gary R.</given-names>
</name>
<email>gary.whittaker@cornell.edu</email>
<xref rid="aff1" ref-type="aff">a</xref>
<xref rid="cor2" ref-type="corresp">∗∗</xref>
</contrib>
</contrib-group>
<aff id="aff1"><label>a</label>
Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY, United States</aff>
<aff id="aff2"><label>b</label>
Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY, United States</aff>
<author-notes><corresp id="cor1"><label>∗</label>
Corresponding author. <email>rebecca.dutch@uky.edu</email>
</corresp>
<corresp id="cor2"><label>∗∗</label>
Corresponding author. <email>gary.whittaker@cornell.edu</email>
</corresp>
<fn id="fn1"><label>1</label>
<p id="ntpara0010">M.R.S and J.T.K contributed equally to this work.</p>
</fn>
</author-notes>
<pub-date pub-type="pmc-release"><day>7</day>
<month>1</month>
<year>2020</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><month>4</month>
<year>2020</year>
</pub-date>
<pub-date pub-type="epub"><day>7</day>
<month>1</month>
<year>2020</year>
</pub-date>
<volume>543</volume>
<fpage>43</fpage>
<lpage>53</lpage>
<history><date date-type="received"><day>9</day>
<month>10</month>
<year>2019</year>
</date>
<date date-type="rev-recd"><day>25</day>
<month>12</month>
<year>2019</year>
</date>
<date date-type="accepted"><day>4</day>
<month>1</month>
<year>2020</year>
</date>
</history>
<permissions><copyright-statement>© 2020 Elsevier Inc. All rights reserved.</copyright-statement>
<copyright-year>2020</copyright-year>
<copyright-holder>Elsevier Inc.</copyright-holder>
<license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p>
</license>
</permissions>
<abstract id="abs0010"><p>Viruses possessing class I fusion proteins require proteolytic activation by host cell proteases to mediate fusion with the host cell membrane. The mammalian SPINT2 gene encodes a protease inhibitor that targets trypsin-like serine proteases. Here we show the protease inhibitor, SPINT2, restricts cleavage-activation efficiently for a range of influenza viruses and for human metapneumovirus (HMPV). SPINT2 treatment resulted in the cleavage and fusion inhibition of full-length influenza A/CA/04/09 (H1N1) HA, A/Aichi/68 (H3N2) HA, A/Shanghai/2/2013 (H7N9) HA and HMPV F when activated by trypsin, recombinant matriptase or KLK5. We also demonstrate that SPINT2 was able to reduce viral growth of influenza A/CA/04/09 H1N1 and A/X31 H3N2 in cell culture by inhibiting matriptase or TMPRSS2. Moreover, inhibition efficacy did not differ whether SPINT2 was added at the time of infection or 24 h post-infection. Our data suggest that the SPINT2 inhibitor has a strong potential to serve as a novel broad-spectrum antiviral.</p>
</abstract>
<kwd-group id="kwrds0010"><title>Keywords</title>
<kwd>Influenza</kwd>
<kwd>HMPV</kwd>
<kwd>Hemagglutinin</kwd>
<kwd>HMPV F</kwd>
<kwd>Proteases</kwd>
<kwd>Antiviral therapy</kwd>
<kwd>SPINT2</kwd>
<kwd>HAI-2</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Kentucky</li>
<li>État de New York</li>
</region>
<settlement><li>Ithaca (New York)</li>
</settlement>
<orgName><li>Université Cornell</li>
</orgName>
</list>
<tree><country name="États-Unis"><region name="État de New York"><name sortKey="Straus, Marco R" sort="Straus, Marco R" uniqKey="Straus M" first="Marco R." last="Straus">Marco R. Straus</name>
</region>
<name sortKey="Dutch, Rebecca Ellis" sort="Dutch, Rebecca Ellis" uniqKey="Dutch R" first="Rebecca Ellis" last="Dutch">Rebecca Ellis Dutch</name>
<name sortKey="Kinder, Jonathan T" sort="Kinder, Jonathan T" uniqKey="Kinder J" first="Jonathan T." last="Kinder">Jonathan T. Kinder</name>
<name sortKey="Segall, Michal" sort="Segall, Michal" uniqKey="Segall M" first="Michal" last="Segall">Michal Segall</name>
<name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R." last="Whittaker">Gary R. Whittaker</name>
</country>
</tree>
</affiliations>
</record>
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