Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry.
Identifieur interne : 002606 ( PubMed/Corpus ); précédent : 002605; suivant : 002607Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry.
Auteurs : Graham Simmons ; Dhaval N. Gosalia ; Andrew J. Rennekamp ; Jacqueline D. Reeves ; Scott L. Diamond ; Paul BatesSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2005.
English descriptors
- KwdEn :
- Cathepsin L, Cathepsins (antagonists & inhibitors), Cathepsins (metabolism), Cell Line, Cell Membrane (chemistry), Cell Membrane (drug effects), Cell Membrane (metabolism), Cysteine Endopeptidases (metabolism), Humans, Membrane Fusion (drug effects), Membrane Fusion (physiology), Molecular Structure, Protease Inhibitors (pharmacology), SARS Virus (drug effects), SARS Virus (physiology), Severe Acute Respiratory Syndrome (enzymology), Severe Acute Respiratory Syndrome (prevention & control), Severe Acute Respiratory Syndrome (virology), Temperature.
- MESH :
- chemical , antagonists & inhibitors : Cathepsins.
- chemical , metabolism : Cathepsins, Cysteine Endopeptidases.
- chemical , pharmacology : Protease Inhibitors.
- chemical : Cathepsin L.
- chemistry : Cell Membrane.
- drug effects : Cell Membrane, Membrane Fusion, SARS Virus.
- enzymology : Severe Acute Respiratory Syndrome.
- metabolism : Cell Membrane.
- physiology : Membrane Fusion, SARS Virus.
- prevention & control : Severe Acute Respiratory Syndrome.
- virology : Severe Acute Respiratory Syndrome.
- Cell Line, Humans, Molecular Structure, Temperature.
Abstract
Severe acute respiratory syndrome (SARS) is caused by an emergent coronavirus (SARS-CoV), for which there is currently no effective treatment. SARS-CoV mediates receptor binding and entry by its spike (S) glycoprotein, and infection is sensitive to lysosomotropic agents that perturb endosomal pH. We demonstrate here that the lysosomotropic-agent-mediated block to SARS-CoV infection is overcome by protease treatment of target-cell-associated virus. In addition, SARS-CoV infection was blocked by specific inhibitors of the pH-sensitive endosomal protease cathepsin L. A cell-free membrane-fusion system demonstrates that engagement of receptor followed by proteolysis is required for SARS-CoV membrane fusion and indicates that cathepsin L is sufficient to activate membrane fusion by SARS-CoV S. These results suggest that SARS-CoV infection results from a unique, three-step process: receptor binding and induced conformational changes in S glycoprotein followed by cathepsin L proteolysis within endosomes. The requirement for cathepsin L proteolysis identifies a previously uncharacterized class of inhibitor for SARS-CoV infection.
DOI: 10.1073/pnas.0505577102
PubMed: 16081529
Links to Exploration step
pubmed:16081529Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry.</title><author><name sortKey="Simmons, Graham" sort="Simmons, Graham" uniqKey="Simmons G" first="Graham" last="Simmons">Graham Simmons</name><affiliation><nlm:affiliation>Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. gsimmons@mail.med.upenn.edu</nlm:affiliation></affiliation></author><author><name sortKey="Gosalia, Dhaval N" sort="Gosalia, Dhaval N" uniqKey="Gosalia D" first="Dhaval N" last="Gosalia">Dhaval N. Gosalia</name></author><author><name sortKey="Rennekamp, Andrew J" sort="Rennekamp, Andrew J" uniqKey="Rennekamp A" first="Andrew J" last="Rennekamp">Andrew J. Rennekamp</name></author><author><name sortKey="Reeves, Jacqueline D" sort="Reeves, Jacqueline D" uniqKey="Reeves J" first="Jacqueline D" last="Reeves">Jacqueline D. Reeves</name></author><author><name sortKey="Diamond, Scott L" sort="Diamond, Scott L" uniqKey="Diamond S" first="Scott L" last="Diamond">Scott L. Diamond</name></author><author><name sortKey="Bates, Paul" sort="Bates, Paul" uniqKey="Bates P" first="Paul" last="Bates">Paul Bates</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:16081529</idno><idno type="pmid">16081529</idno><idno type="doi">10.1073/pnas.0505577102</idno><idno type="wicri:Area/PubMed/Corpus">002606</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002606</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry.</title><author><name sortKey="Simmons, Graham" sort="Simmons, Graham" uniqKey="Simmons G" first="Graham" last="Simmons">Graham Simmons</name><affiliation><nlm:affiliation>Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. gsimmons@mail.med.upenn.edu</nlm:affiliation></affiliation></author><author><name sortKey="Gosalia, Dhaval N" sort="Gosalia, Dhaval N" uniqKey="Gosalia D" first="Dhaval N" last="Gosalia">Dhaval N. Gosalia</name></author><author><name sortKey="Rennekamp, Andrew J" sort="Rennekamp, Andrew J" uniqKey="Rennekamp A" first="Andrew J" last="Rennekamp">Andrew J. Rennekamp</name></author><author><name sortKey="Reeves, Jacqueline D" sort="Reeves, Jacqueline D" uniqKey="Reeves J" first="Jacqueline D" last="Reeves">Jacqueline D. Reeves</name></author><author><name sortKey="Diamond, Scott L" sort="Diamond, Scott L" uniqKey="Diamond S" first="Scott L" last="Diamond">Scott L. Diamond</name></author><author><name sortKey="Bates, Paul" sort="Bates, Paul" uniqKey="Bates P" first="Paul" last="Bates">Paul Bates</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cathepsin L</term><term>Cathepsins (antagonists & inhibitors)</term><term>Cathepsins (metabolism)</term><term>Cell Line</term><term>Cell Membrane (chemistry)</term><term>Cell Membrane (drug effects)</term><term>Cell Membrane (metabolism)</term><term>Cysteine Endopeptidases (metabolism)</term><term>Humans</term><term>Membrane Fusion (drug effects)</term><term>Membrane Fusion (physiology)</term><term>Molecular Structure</term><term>Protease Inhibitors (pharmacology)</term><term>SARS Virus (drug effects)</term><term>SARS Virus (physiology)</term><term>Severe Acute Respiratory Syndrome (enzymology)</term><term>Severe Acute Respiratory Syndrome (prevention & control)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Temperature</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Cathepsins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cathepsins</term><term>Cysteine Endopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cathepsin L</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Membrane</term><term>Membrane Fusion</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Membrane Fusion</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>Molecular Structure</term><term>Temperature</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is caused by an emergent coronavirus (SARS-CoV), for which there is currently no effective treatment. SARS-CoV mediates receptor binding and entry by its spike (S) glycoprotein, and infection is sensitive to lysosomotropic agents that perturb endosomal pH. We demonstrate here that the lysosomotropic-agent-mediated block to SARS-CoV infection is overcome by protease treatment of target-cell-associated virus. In addition, SARS-CoV infection was blocked by specific inhibitors of the pH-sensitive endosomal protease cathepsin L. A cell-free membrane-fusion system demonstrates that engagement of receptor followed by proteolysis is required for SARS-CoV membrane fusion and indicates that cathepsin L is sufficient to activate membrane fusion by SARS-CoV S. These results suggest that SARS-CoV infection results from a unique, three-step process: receptor binding and induced conformational changes in S glycoprotein followed by cathepsin L proteolysis within endosomes. The requirement for cathepsin L proteolysis identifies a previously uncharacterized class of inhibitor for SARS-CoV infection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16081529</PMID><DateCompleted><Year>2005</Year><Month>10</Month><Day>25</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>102</Volume><Issue>33</Issue><PubDate><Year>2005</Year><Month>Aug</Month><Day>16</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation></Journal><ArticleTitle>Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry.</ArticleTitle><Pagination><MedlinePgn>11876-81</MedlinePgn></Pagination><Abstract><AbstractText>Severe acute respiratory syndrome (SARS) is caused by an emergent coronavirus (SARS-CoV), for which there is currently no effective treatment. SARS-CoV mediates receptor binding and entry by its spike (S) glycoprotein, and infection is sensitive to lysosomotropic agents that perturb endosomal pH. We demonstrate here that the lysosomotropic-agent-mediated block to SARS-CoV infection is overcome by protease treatment of target-cell-associated virus. In addition, SARS-CoV infection was blocked by specific inhibitors of the pH-sensitive endosomal protease cathepsin L. A cell-free membrane-fusion system demonstrates that engagement of receptor followed by proteolysis is required for SARS-CoV membrane fusion and indicates that cathepsin L is sufficient to activate membrane fusion by SARS-CoV S. These results suggest that SARS-CoV infection results from a unique, three-step process: receptor binding and induced conformational changes in S glycoprotein followed by cathepsin L proteolysis within endosomes. The requirement for cathepsin L proteolysis identifies a previously uncharacterized class of inhibitor for SARS-CoV infection.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Simmons</LastName><ForeName>Graham</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. gsimmons@mail.med.upenn.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gosalia</LastName><ForeName>Dhaval N</ForeName><Initials>DN</Initials></Author><Author ValidYN="Y"><LastName>Rennekamp</LastName><ForeName>Andrew J</ForeName><Initials>AJ</Initials></Author><Author ValidYN="Y"><LastName>Reeves</LastName><ForeName>Jacqueline D</ForeName><Initials>JD</Initials></Author><Author ValidYN="Y"><LastName>Diamond</LastName><ForeName>Scott L</ForeName><Initials>SL</Initials></Author><Author ValidYN="Y"><LastName>Bates</LastName><ForeName>Paul</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI43455</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R21 AI058701</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI043455</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R21 AI 058701</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R21 AI059172</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U54 AI057168</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType 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IdType="pubmed">15163706</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60</Citation><ArticleIdList><ArticleId IdType="pubmed">15150417</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 1994 Sep;203(2):313-9</Citation><ArticleIdList><ArticleId IdType="pubmed">8053155</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 1994 Sep;68(9):5623-8</Citation><ArticleIdList><ArticleId IdType="pubmed">8057442</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 1995 Feb 1;206(2):935-44</Citation><ArticleIdList><ArticleId IdType="pubmed">7531918</ArticleId></ArticleIdList></Reference><Reference><Citation>Annu Rev Biochem. 2000;69:531-69</Citation><ArticleIdList><ArticleId IdType="pubmed">10966468</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Neurosci. 1999 Jul;11(7):2375-84</Citation><ArticleIdList><ArticleId IdType="pubmed">10383627</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2004 Dec;78(24):13430-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15564453</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2005 Jun 10;308(5728):1643-5</Citation><ArticleIdList><ArticleId IdType="pubmed">15831716</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2000 Jun 5;271(2):248-52</Citation><ArticleIdList><ArticleId IdType="pubmed">10860878</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 2000 Nov 10;103(4):679-89</Citation><ArticleIdList><ArticleId IdType="pubmed">11106737</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2001 Jul;75(13):5851-9</Citation><ArticleIdList><ArticleId IdType="pubmed">11390586</ArticleId></ArticleIdList></Reference><Reference><Citation>Bioorg Med Chem Lett. 2002 May 20;12(10):1335-8</Citation><ArticleIdList><ArticleId IdType="pubmed">11992771</ArticleId></ArticleIdList></Reference><Reference><Citation>Biol Chem. 2002 Jul-Aug;383(7-8):1305-8</Citation><ArticleIdList><ArticleId IdType="pubmed">12437121</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2003 Mar;77(5):3058-66</Citation><ArticleIdList><ArticleId IdType="pubmed">12584331</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2003 May 30;300(5624):1394-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12730500</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2003 Jul 22;100(15):8721-6</Citation><ArticleIdList><ArticleId IdType="pubmed">12851459</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2003 Oct 10;302(5643):276-8</Citation><ArticleIdList><ArticleId IdType="pubmed">12958366</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Immunol. 2003 Dec;33(12):3242-54</Citation><ArticleIdList><ArticleId IdType="pubmed">14635032</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2003 Nov 27;426(6965):450-4</Citation><ArticleIdList><ArticleId IdType="pubmed">14647384</ArticleId></ArticleIdList></Reference><Reference><Citation>Antivir Chem Chemother. 2004 Jan;15(1):15-22</Citation><ArticleIdList><ArticleId IdType="pubmed">15074711</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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