Identification of a broad-spectrum antiviral small molecule against severe acute respiratory syndrome coronavirus and Ebola, Hendra, and Nipah viruses by using a novel high-throughput screening assay.
Identifieur interne : 001055 ( PubMed/Corpus ); précédent : 001054; suivant : 001056Identification of a broad-spectrum antiviral small molecule against severe acute respiratory syndrome coronavirus and Ebola, Hendra, and Nipah viruses by using a novel high-throughput screening assay.
Auteurs : Hatem A. Elshabrawy ; Jilao Fan ; Christine S. Haddad ; Kiira Ratia ; Christopher C. Broder ; Michael Caffrey ; Bellur S. PrabhakarSource :
- Journal of virology [ 1098-5514 ] ; 2014.
English descriptors
- KwdEn :
- Antiviral Agents (pharmacology), Cathepsin L (metabolism), Drug Evaluation, Preclinical (methods), Ebolavirus (drug effects), Ebolavirus (metabolism), Hendra Virus (drug effects), Hendra Virus (metabolism), High-Throughput Screening Assays (methods), Humans, Nipah Virus (drug effects), Nipah Virus (metabolism), SARS Virus (drug effects), SARS Virus (metabolism), Small Molecule Libraries (pharmacology), Viral Envelope Proteins (metabolism), Virus Diseases (enzymology), Virus Diseases (virology).
- MESH :
- chemical , metabolism : Cathepsin L, Viral Envelope Proteins.
- chemical , pharmacology : Antiviral Agents, Small Molecule Libraries.
- drug effects : Ebolavirus, Hendra Virus, Nipah Virus, SARS Virus.
- enzymology : Virus Diseases.
- metabolism : Ebolavirus, Hendra Virus, Nipah Virus, SARS Virus.
- methods : Drug Evaluation, Preclinical, High-Throughput Screening Assays.
- virology : Virus Diseases.
- Humans.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) and Ebola, Hendra, and Nipah viruses are members of different viral families and are known causative agents of fatal viral diseases. These viruses depend on cathepsin L for entry into their target cells. The viral glycoproteins need to be primed by protease cleavage, rendering them active for fusion with the host cell membrane. In this study, we developed a novel high-throughput screening assay based on peptides, derived from the glycoproteins of the aforementioned viruses, which contain the cathepsin L cleavage site. We screened a library of 5,000 small molecules and discovered a small molecule that can inhibit the cathepsin L cleavage of all viral peptides with minimal inhibition of cleavage of a host protein-derived peptide (pro-neuropeptide Y). The small molecule inhibited the entry of all pseudotyped viruses in vitro and the cleavage of SARS-CoV spike glycoprotein in an in vitro cleavage assay. In addition, the Hendra and Nipah virus fusion glycoproteins were not cleaved in the presence of the small molecule in a cell-based cleavage assay. Furthermore, we demonstrate that the small molecule is a mixed inhibitor of cathepsin L. Our broad-spectrum antiviral small molecule appears to be an ideal candidate for future optimization and development into a potent antiviral against SARS-CoV and Ebola, Hendra, and Nipah viruses.
DOI: 10.1128/JVI.03050-13
PubMed: 24501399
Links to Exploration step
pubmed:24501399Le document en format XML
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Haddad</name></author><author><name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</name></author><author><name sortKey="Broder, Christopher C" sort="Broder, Christopher C" uniqKey="Broder C" first="Christopher C" last="Broder">Christopher C. Broder</name></author><author><name sortKey="Caffrey, Michael" sort="Caffrey, Michael" uniqKey="Caffrey M" first="Michael" last="Caffrey">Michael Caffrey</name></author><author><name sortKey="Prabhakar, Bellur S" sort="Prabhakar, Bellur S" uniqKey="Prabhakar B" first="Bellur S" last="Prabhakar">Bellur S. 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Elshabrawy</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Fan, Jilao" sort="Fan, Jilao" uniqKey="Fan J" first="Jilao" last="Fan">Jilao Fan</name></author><author><name sortKey="Haddad, Christine S" sort="Haddad, Christine S" uniqKey="Haddad C" first="Christine S" last="Haddad">Christine S. Haddad</name></author><author><name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</name></author><author><name sortKey="Broder, Christopher C" sort="Broder, Christopher C" uniqKey="Broder C" first="Christopher C" last="Broder">Christopher C. Broder</name></author><author><name sortKey="Caffrey, Michael" sort="Caffrey, Michael" uniqKey="Caffrey M" first="Michael" last="Caffrey">Michael Caffrey</name></author><author><name sortKey="Prabhakar, Bellur S" sort="Prabhakar, Bellur S" uniqKey="Prabhakar B" first="Bellur S" last="Prabhakar">Bellur S. Prabhakar</name></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antiviral Agents (pharmacology)</term><term>Cathepsin L (metabolism)</term><term>Drug Evaluation, Preclinical (methods)</term><term>Ebolavirus (drug effects)</term><term>Ebolavirus (metabolism)</term><term>Hendra Virus (drug effects)</term><term>Hendra Virus (metabolism)</term><term>High-Throughput Screening Assays (methods)</term><term>Humans</term><term>Nipah Virus (drug effects)</term><term>Nipah Virus (metabolism)</term><term>SARS Virus (drug effects)</term><term>SARS Virus (metabolism)</term><term>Small Molecule Libraries (pharmacology)</term><term>Viral Envelope Proteins (metabolism)</term><term>Virus Diseases (enzymology)</term><term>Virus Diseases (virology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cathepsin L</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Small Molecule Libraries</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Ebolavirus</term><term>Hendra Virus</term><term>Nipah Virus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Virus Diseases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Ebolavirus</term><term>Hendra Virus</term><term>Nipah Virus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Drug Evaluation, Preclinical</term><term>High-Throughput Screening Assays</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Virus Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) and Ebola, Hendra, and Nipah viruses are members of different viral families and are known causative agents of fatal viral diseases. These viruses depend on cathepsin L for entry into their target cells. The viral glycoproteins need to be primed by protease cleavage, rendering them active for fusion with the host cell membrane. In this study, we developed a novel high-throughput screening assay based on peptides, derived from the glycoproteins of the aforementioned viruses, which contain the cathepsin L cleavage site. We screened a library of 5,000 small molecules and discovered a small molecule that can inhibit the cathepsin L cleavage of all viral peptides with minimal inhibition of cleavage of a host protein-derived peptide (pro-neuropeptide Y). The small molecule inhibited the entry of all pseudotyped viruses in vitro and the cleavage of SARS-CoV spike glycoprotein in an in vitro cleavage assay. In addition, the Hendra and Nipah virus fusion glycoproteins were not cleaved in the presence of the small molecule in a cell-based cleavage assay. Furthermore, we demonstrate that the small molecule is a mixed inhibitor of cathepsin L. Our broad-spectrum antiviral small molecule appears to be an ideal candidate for future optimization and development into a potent antiviral against SARS-CoV and Ebola, Hendra, and Nipah viruses.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24501399</PMID><DateCompleted><Year>2014</Year><Month>06</Month><Day>24</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>88</Volume><Issue>8</Issue><PubDate><Year>2014</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Identification of a broad-spectrum antiviral small molecule against severe acute respiratory syndrome coronavirus and Ebola, Hendra, and Nipah viruses by using a novel high-throughput screening assay.</ArticleTitle><Pagination><MedlinePgn>4353-65</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.03050-13</ELocationID><Abstract><AbstractText Label="UNLABELLED">Severe acute respiratory syndrome coronavirus (SARS-CoV) and Ebola, Hendra, and Nipah viruses are members of different viral families and are known causative agents of fatal viral diseases. These viruses depend on cathepsin L for entry into their target cells. The viral glycoproteins need to be primed by protease cleavage, rendering them active for fusion with the host cell membrane. In this study, we developed a novel high-throughput screening assay based on peptides, derived from the glycoproteins of the aforementioned viruses, which contain the cathepsin L cleavage site. We screened a library of 5,000 small molecules and discovered a small molecule that can inhibit the cathepsin L cleavage of all viral peptides with minimal inhibition of cleavage of a host protein-derived peptide (pro-neuropeptide Y). The small molecule inhibited the entry of all pseudotyped viruses in vitro and the cleavage of SARS-CoV spike glycoprotein in an in vitro cleavage assay. In addition, the Hendra and Nipah virus fusion glycoproteins were not cleaved in the presence of the small molecule in a cell-based cleavage assay. Furthermore, we demonstrate that the small molecule is a mixed inhibitor of cathepsin L. Our broad-spectrum antiviral small molecule appears to be an ideal candidate for future optimization and development into a potent antiviral against SARS-CoV and Ebola, Hendra, and Nipah viruses.</AbstractText><AbstractText Label="IMPORTANCE" NlmCategory="OBJECTIVE">We developed a novel high-throughput screening assay to identify small molecules that can prevent cathepsin L cleavage of viral glycoproteins derived from SARS-CoV and Ebola, Hendra, and Nipah viruses that are required for their entry into the host cell. We identified a novel broad-spectrum small molecule that could block cathepsin L-mediated cleavage and thus inhibit the entry of pseudotypes bearing the glycoprotein derived from SARS-CoV or Ebola, Hendra, or Nipah virus. The small molecule can be further optimized and developed into a potent broad-spectrum antiviral drug.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Elshabrawy</LastName><ForeName>Hatem A</ForeName><Initials>HA</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fan</LastName><ForeName>Jilao</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Haddad</LastName><ForeName>Christine S</ForeName><Initials>CS</Initials></Author><Author ValidYN="Y"><LastName>Ratia</LastName><ForeName>Kiira</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Broder</LastName><ForeName>Christopher C</ForeName><Initials>CC</Initials></Author><Author ValidYN="Y"><LastName>Caffrey</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Prabhakar</LastName><ForeName>Bellur S</ForeName><Initials>BS</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>1U01AI082296</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D023362">Evaluation Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>02</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054852">Small Molecule Libraries</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.15</RegistryNumber><NameOfSubstance UI="D056668">Cathepsin L</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D056668" MajorTopicYN="N">Cathepsin L</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004353" MajorTopicYN="N">Drug Evaluation, Preclinical</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029043" MajorTopicYN="N">Ebolavirus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045404" MajorTopicYN="N">Hendra Virus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057166" MajorTopicYN="N">High-Throughput Screening Assays</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045405" MajorTopicYN="N">Nipah Virus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054852" MajorTopicYN="N">Small Molecule Libraries</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014777" MajorTopicYN="N">Virus Diseases</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000821" 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| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |