SrasV1, PubMed, Checkpoint, bibRecord, 000D75

Protease inhibitors targeting coronavirus and filovirus entry.

Identifieur interne : 000D75 ( PubMed/Checkpoint ); précédent : 000D74; suivant : 000D76

Protease inhibitors targeting coronavirus and filovirus entry.

Auteurs : Yanchen Zhou [États-Unis] ; Punitha Vedantham [États-Unis] ; Kai Lu [États-Unis] ; Juliet Agudelo [États-Unis] ; Ricardo Carrion [États-Unis] ; Jerritt W. Nunneley [États-Unis] ; Dale Barnard [États-Unis] ; Stefan Pöhlmann [Allemagne] ; James H. Mckerrow [États-Unis] ; Adam R. Renslo [États-Unis] ; Graham Simmons [États-Unis]

Source :

Antiviral research [ 1872-9096 ] ; 2015.

RBID : pubmed:25666761

Descripteurs français

KwdFr :
- Animaux, Antiviraux (pharmacologie), Cathepsines (métabolisme), Composés vinyliques (pharmacologie), Coronavirus (), Coronavirus (physiologie), Dipeptides (pharmacologie), Ebolavirus (), Ebolavirus (physiologie), Filoviridae (), Filoviridae (physiologie), Gabexate (analogues et dérivés), Gabexate (pharmacologie), Humains, Infections à coronavirus (traitement médicamenteux), Inhibiteurs de la sérine protéinase (pharmacologie), Inhibiteurs de protéases (pharmacologie), Lignée cellulaire tumorale, Pénétration virale (), Serine endopeptidases (métabolisme), Souris, Souris de lignée BALB C, Virus du SRAS (), Virus du SRAS (physiologie).
MESH :
- analogues et dérivés : Gabexate.
- métabolisme : Cathepsines, Serine endopeptidases.
- pharmacologie : Antiviraux, Composés vinyliques, Dipeptides, Gabexate, Inhibiteurs de la sérine protéinase, Inhibiteurs de protéases.
- physiologie : Coronavirus, Ebolavirus, Filoviridae, Virus du SRAS.
- traitement médicamenteux : Infections à coronavirus.
- Animaux, Coronavirus, Ebolavirus, Filoviridae, Humains, Lignée cellulaire tumorale, Pénétration virale, Souris, Souris de lignée BALB C, Virus du SRAS.

English descriptors

KwdEn :
- Animals, Antiviral Agents (pharmacology), Cathepsins (metabolism), Cell Line, Tumor, Coronavirus (drug effects), Coronavirus (physiology), Coronavirus Infections (drug therapy), Dipeptides (pharmacology), Ebolavirus (drug effects), Ebolavirus (physiology), Filoviridae (drug effects), Filoviridae (physiology), Gabexate (analogs & derivatives), Gabexate (pharmacology), Humans, Mice, Mice, Inbred BALB C, Protease Inhibitors (pharmacology), SARS Virus (drug effects), SARS Virus (physiology), Serine Endopeptidases (metabolism), Serine Proteinase Inhibitors (pharmacology), Vinyl Compounds (pharmacology), Virus Internalization (drug effects).
MESH :
- chemical , analogs & derivatives : Gabexate.
- chemical , metabolism : Cathepsins, Serine Endopeptidases.
- chemical , pharmacology : Antiviral Agents, Dipeptides, Gabexate, Protease Inhibitors, Serine Proteinase Inhibitors, Vinyl Compounds.
- drug effects : Coronavirus, Ebolavirus, Filoviridae, SARS Virus, Virus Internalization.
- drug therapy : Coronavirus Infections.
- physiology : Coronavirus, Ebolavirus, Filoviridae, SARS Virus.
- Animals, Cell Line, Tumor, Humans, Mice, Mice, Inbred BALB C.

Abstract

In order to gain entry into cells, diverse viruses, including Ebola virus, SARS-coronavirus and the emerging MERS-coronavirus, depend on activation of their envelope glycoproteins by host cell proteases. The respective enzymes are thus excellent targets for antiviral intervention. In cell culture, activation of Ebola virus, as well as SARS- and MERS-coronavirus can be accomplished by the endosomal cysteine proteases, cathepsin L (CTSL) and cathepsin B (CTSB). In addition, SARS- and MERS-coronavirus can use serine proteases localized at the cell surface, for their activation. However, it is currently unclear which protease(s) facilitate viral spread in the infected host. We report here that the cysteine protease inhibitor K11777, ((2S)-N-[(1E,3S)-1-(benzenesulfonyl)-5-phenylpent-1-en-3-yl]-2-{[(E)-4-methylpiperazine-1-carbonyl]amino}-3-phenylpropanamide) and closely-related vinylsulfones act as broad-spectrum antivirals by targeting cathepsin-mediated cell entry. K11777 is already in advanced stages of development for a number of parasitic diseases, such as Chagas disease, and has proven to be safe and effective in a range of animal models. K11777 inhibition of SARS-CoV and Ebola virus entry was observed in the sub-nanomolar range. In order to assess whether cysteine or serine proteases promote viral spread in the host, we compared the antiviral activity of an optimized K11777-derivative with that of camostat, an inhibitor of TMPRSS2 and related serine proteases. Employing a pathogenic animal model of SARS-CoV infection, we demonstrated that viral spread and pathogenesis of SARS-CoV is driven by serine rather than cysteine proteases and can be effectively prevented by camostat. Camostat has been clinically used to treat chronic pancreatitis, and thus represents an exciting potential therapeutic for respiratory coronavirus infections. Our results indicate that camostat, or similar serine protease inhibitors, might be an effective option for treatment of SARS and potentially MERS, while vinyl sulfone-based inhibitors are excellent lead candidates for Ebola virus therapeutics.

DOI: 10.1016/j.antiviral.2015.01.011
PubMed: 25666761

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">In order to gain entry into cells, diverse viruses, including Ebola virus, SARS-coronavirus and the emerging MERS-coronavirus, depend on activation of their envelope glycoproteins by host cell proteases. The respective enzymes are thus excellent targets for antiviral intervention. In cell culture, activation of Ebola virus, as well as SARS- and MERS-coronavirus can be accomplished by the endosomal cysteine proteases, cathepsin L (CTSL) and cathepsin B (CTSB). In addition, SARS- and MERS-coronavirus can use serine proteases localized at the cell surface, for their activation. However, it is currently unclear which protease(s) facilitate viral spread in the infected host. We report here that the cysteine protease inhibitor K11777, ((2S)-N-[(1E,3S)-1-(benzenesulfonyl)-5-phenylpent-1-en-3-yl]-2-{[(E)-4-methylpiperazine-1-carbonyl]amino}-3-phenylpropanamide) and closely-related vinylsulfones act as broad-spectrum antivirals by targeting cathepsin-mediated cell entry. K11777 is already in advanced stages of development for a number of parasitic diseases, such as Chagas disease, and has proven to be safe and effective in a range of animal models. K11777 inhibition of SARS-CoV and Ebola virus entry was observed in the sub-nanomolar range. In order to assess whether cysteine or serine proteases promote viral spread in the host, we compared the antiviral activity of an optimized K11777-derivative with that of camostat, an inhibitor of TMPRSS2 and related serine proteases. Employing a pathogenic animal model of SARS-CoV infection, we demonstrated that viral spread and pathogenesis of SARS-CoV is driven by serine rather than cysteine proteases and can be effectively prevented by camostat. Camostat has been clinically used to treat chronic pancreatitis, and thus represents an exciting potential therapeutic for respiratory coronavirus infections. Our results indicate that camostat, or similar serine protease inhibitors, might be an effective option for treatment of SARS and potentially MERS, while vinyl sulfone-based inhibitors are excellent lead candidates for Ebola virus therapeutics. </div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25666761</PMID>
<DateCompleted><Year>2015</Year>
<Month>12</Month>
<Day>15</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>04</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-9096</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>116</Volume>
<PubDate><Year>2015</Year>
<Month>Apr</Month>
</PubDate>
</JournalIssue>
<Title>Antiviral research</Title>
<ISOAbbreviation>Antiviral Res.</ISOAbbreviation>
</Journal>
<ArticleTitle>Protease inhibitors targeting coronavirus and filovirus entry.</ArticleTitle>
<Pagination><MedlinePgn>76-84</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.antiviral.2015.01.011</ELocationID>
<ELocationID EIdType="pii" ValidYN="Y">S0166-3542(15)00024-8</ELocationID>
<Abstract><AbstractText>In order to gain entry into cells, diverse viruses, including Ebola virus, SARS-coronavirus and the emerging MERS-coronavirus, depend on activation of their envelope glycoproteins by host cell proteases. The respective enzymes are thus excellent targets for antiviral intervention. In cell culture, activation of Ebola virus, as well as SARS- and MERS-coronavirus can be accomplished by the endosomal cysteine proteases, cathepsin L (CTSL) and cathepsin B (CTSB). In addition, SARS- and MERS-coronavirus can use serine proteases localized at the cell surface, for their activation. However, it is currently unclear which protease(s) facilitate viral spread in the infected host. We report here that the cysteine protease inhibitor K11777, ((2S)-N-[(1E,3S)-1-(benzenesulfonyl)-5-phenylpent-1-en-3-yl]-2-{[(E)-4-methylpiperazine-1-carbonyl]amino}-3-phenylpropanamide) and closely-related vinylsulfones act as broad-spectrum antivirals by targeting cathepsin-mediated cell entry. K11777 is already in advanced stages of development for a number of parasitic diseases, such as Chagas disease, and has proven to be safe and effective in a range of animal models. K11777 inhibition of SARS-CoV and Ebola virus entry was observed in the sub-nanomolar range. In order to assess whether cysteine or serine proteases promote viral spread in the host, we compared the antiviral activity of an optimized K11777-derivative with that of camostat, an inhibitor of TMPRSS2 and related serine proteases. Employing a pathogenic animal model of SARS-CoV infection, we demonstrated that viral spread and pathogenesis of SARS-CoV is driven by serine rather than cysteine proteases and can be effectively prevented by camostat. Camostat has been clinically used to treat chronic pancreatitis, and thus represents an exciting potential therapeutic for respiratory coronavirus infections. Our results indicate that camostat, or similar serine protease inhibitors, might be an effective option for treatment of SARS and potentially MERS, while vinyl sulfone-based inhibitors are excellent lead candidates for Ebola virus therapeutics. </AbstractText>
<CopyrightInformation>Copyright © 2015. Published by Elsevier B.V.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhou</LastName>
<ForeName>Yanchen</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Blood Systems Research Institute, San Francisco, CA 94118, USA; Department of Laboratory Medicine, University of California, San Francisco, San Francisco, CA 94118, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Vedantham</LastName>
<ForeName>Punitha</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Small Molecule Discovery Center and Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94158, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lu</LastName>
<ForeName>Kai</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Blood Systems Research Institute, San Francisco, CA 94118, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Agudelo</LastName>
<ForeName>Juliet</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Blood Systems Research Institute, San Francisco, CA 94118, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Carrion</LastName>
<ForeName>Ricardo</ForeName>
<Initials>R</Initials>
<Suffix>Jr</Suffix>
<AffiliationInfo><Affiliation>Texas Biomedical Research Institute, San Antonio, TX 78227, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Nunneley</LastName>
<ForeName>Jerritt W</ForeName>
<Initials>JW</Initials>
<AffiliationInfo><Affiliation>Texas Biomedical Research Institute, San Antonio, TX 78227, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Barnard</LastName>
<ForeName>Dale</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>Institute for Antiviral Research, Department of Animal, Dairy and Veterinary Science, Utah State University, Logan, UT 84322, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pöhlmann</LastName>
<ForeName>Stefan</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Infection Biology Unit, German Primate Center, 37077 Göttingen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>McKerrow</LastName>
<ForeName>James H</ForeName>
<Initials>JH</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Center for Discovery and Innovation in Parasitic Diseases, University of California, San Francisco, San Francisco, CA 94158, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Renslo</LastName>
<ForeName>Adam R</ForeName>
<Initials>AR</Initials>
<AffiliationInfo><Affiliation>Small Molecule Discovery Center and Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94158, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Simmons</LastName>
<ForeName>Graham</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>Blood Systems Research Institute, San Francisco, CA 94118, USA; Department of Laboratory Medicine, University of California, San Francisco, San Francisco, CA 94118, USA. Electronic address: gsimmons@bloodsystems.org.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R21 AI107165</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>HHSN272201000039C</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R21AI107165</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>HHSN272201000039I</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>HHSN272201000039I</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 AI074986</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01AI074986</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2015</Year>
<Month>02</Month>
<Day>07</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Netherlands</Country>
<MedlineTA>Antiviral Res</MedlineTA>
<NlmUniqueID>8109699</NlmUniqueID>
<ISSNLinking>0166-3542</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D004151">Dipeptides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C487484">N-pip-phenylalanine-homophenylalanine-vinyl sulfone phenyl</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance>
</Chemical>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014753">Vinyl Compounds</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0FD207WKDU</RegistryNumber>
<NameOfSubstance UI="C034532">camostat</NameOfSubstance>
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<Chemical><RegistryNumber>4V7M9137X9</RegistryNumber>
<NameOfSubstance UI="D016670">Gabexate</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.-</RegistryNumber>
<NameOfSubstance UI="D002403">Cathepsins</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>
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<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="D002403" MajorTopicYN="N">Cathepsins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017934" MajorTopicYN="N">Coronavirus</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018352" MajorTopicYN="N">Coronavirus Infections</DescriptorName>
<QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004151" MajorTopicYN="N">Dipeptides</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029043" MajorTopicYN="N">Ebolavirus</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016563" MajorTopicYN="N">Filoviridae</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016670" MajorTopicYN="N">Gabexate</DescriptorName>
<QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008807" MajorTopicYN="N">Mice, Inbred BALB C</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012697" MajorTopicYN="N">Serine Endopeptidases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015842" MajorTopicYN="N">Serine Proteinase Inhibitors</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014753" MajorTopicYN="N">Vinyl Compounds</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053586" MajorTopicYN="N">Virus Internalization</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Cathepsin</Keyword>
<Keyword MajorTopicYN="N">Coronavirus</Keyword>
<Keyword MajorTopicYN="N">Filovirus</Keyword>
<Keyword MajorTopicYN="N">Vinylsulfones</Keyword>
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</ReferenceList>
<ReferenceList><Reference><Citation>Bioorg Med Chem Lett. 2010 Dec 15;20(24):7444-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21041084</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2012 Apr;86(7):3736-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22278224</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
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<affiliations><list><country><li>Allemagne</li>
<li>États-Unis</li>
</country>
<region><li>Basse-Saxe</li>
<li>Californie</li>
<li>Texas</li>
<li>Utah</li>
</region>
<settlement><li>Göttingen</li>
</settlement>
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<tree><country name="États-Unis"><region name="Californie"><name sortKey="Zhou, Yanchen" sort="Zhou, Yanchen" uniqKey="Zhou Y" first="Yanchen" last="Zhou">Yanchen Zhou</name>
</region>
<name sortKey="Agudelo, Juliet" sort="Agudelo, Juliet" uniqKey="Agudelo J" first="Juliet" last="Agudelo">Juliet Agudelo</name>
<name sortKey="Barnard, Dale" sort="Barnard, Dale" uniqKey="Barnard D" first="Dale" last="Barnard">Dale Barnard</name>
<name sortKey="Carrion, Ricardo" sort="Carrion, Ricardo" uniqKey="Carrion R" first="Ricardo" last="Carrion">Ricardo Carrion</name>
<name sortKey="Lu, Kai" sort="Lu, Kai" uniqKey="Lu K" first="Kai" last="Lu">Kai Lu</name>
<name sortKey="Mckerrow, James H" sort="Mckerrow, James H" uniqKey="Mckerrow J" first="James H" last="Mckerrow">James H. Mckerrow</name>
<name sortKey="Nunneley, Jerritt W" sort="Nunneley, Jerritt W" uniqKey="Nunneley J" first="Jerritt W" last="Nunneley">Jerritt W. Nunneley</name>
<name sortKey="Renslo, Adam R" sort="Renslo, Adam R" uniqKey="Renslo A" first="Adam R" last="Renslo">Adam R. Renslo</name>
<name sortKey="Simmons, Graham" sort="Simmons, Graham" uniqKey="Simmons G" first="Graham" last="Simmons">Graham Simmons</name>
<name sortKey="Vedantham, Punitha" sort="Vedantham, Punitha" uniqKey="Vedantham P" first="Punitha" last="Vedantham">Punitha Vedantham</name>
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<country name="Allemagne"><region name="Basse-Saxe"><name sortKey="Pohlmann, Stefan" sort="Pohlmann, Stefan" uniqKey="Pohlmann S" first="Stefan" last="Pöhlmann">Stefan Pöhlmann</name>
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   |texte=   Protease inhibitors targeting coronavirus and filovirus entry.
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Protease inhibitors targeting coronavirus and filovirus entry.

Protease inhibitors targeting coronavirus and filovirus entry.

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