Middle East respiratory syndrome coronavirus infection is inhibited by griffithsin.
Identifieur interne : 001045 ( PubMed/Corpus ); précédent : 001044; suivant : 001046Middle East respiratory syndrome coronavirus infection is inhibited by griffithsin.
Auteurs : Jean K. Millet ; Karin Séron ; Rachael N. Labitt ; Adeline Danneels ; Kenneth E. Palmer ; Gary R. Whittaker ; Jean Dubuisson ; Sandrine BelouzardSource :
- Antiviral research [ 1872-9096 ] ; 2016.
English descriptors
- KwdEn :
- Animals, Antiviral Agents (pharmacology), Biological Products (pharmacology), Cell Line, Cell Survival (drug effects), Cells, Cultured, Coronavirus Infections (virology), Dose-Response Relationship, Drug, Humans, Middle East Respiratory Syndrome Coronavirus (drug effects), Middle East Respiratory Syndrome Coronavirus (physiology), Plant Lectins (pharmacology), Virus Internalization (drug effects), Virus Replication (drug effects).
- MESH :
- chemical , pharmacology : Antiviral Agents, Biological Products, Plant Lectins.
- drug effects : Cell Survival, Middle East Respiratory Syndrome Coronavirus, Virus Internalization, Virus Replication.
- physiology : Middle East Respiratory Syndrome Coronavirus.
- virology : Coronavirus Infections.
- Animals, Cell Line, Cells, Cultured, Dose-Response Relationship, Drug, Humans.
Abstract
Highly pathogenic human coronaviruses associated with a severe respiratory syndrome, including Middle East respiratory syndrome coronavirus (MERS-CoV), have recently emerged. The MERS-CoV epidemic started in 2012 and is still ongoing, with a mortality rate of approximately 35%. No vaccine is available against MERS-CoV and therapeutic options for MERS-CoV infections are limited to palliative and supportive care. A search for specific antiviral treatments is urgently needed. Coronaviruses are enveloped viruses, with the spike proteins present on their surface responsible for virus entry into the target cell. Lectins are attractive anti-coronavirus candidates because of the highly glycosylated nature of the spike protein. We tested the antiviral effect of griffithsin (GRFT), a lectin isolated from the red marine alga Griffithsia sp. against MERS-CoV infection. Our results demonstrate that while displaying no significant cytotoxicity, griffithsin is a potent inhibitor of MERS-CoV infection. Griffithsin also inhibits entry into host cells of particles pseudotyped with the MERS-CoV spike protein, suggesting that griffithsin inhibits spike protein function during entry. Spike proteins have a dual function during entry, they mediate binding to the host cell surface and also the fusion of the viral envelope with host cell membrane. Time course experiments show that griffithsin inhibits MERS-CoV infection at the binding step. In conclusion, we identify griffithsin as a potent inhibitor of MERS-CoV infection at the entry step.
DOI: 10.1016/j.antiviral.2016.07.011
PubMed: 27424494
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pubmed:27424494Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Middle East respiratory syndrome coronavirus infection is inhibited by griffithsin.</title><author><name sortKey="Millet, Jean K" sort="Millet, Jean K" uniqKey="Millet J" first="Jean K" last="Millet">Jean K. Millet</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Seron, Karin" sort="Seron, Karin" uniqKey="Seron K" first="Karin" last="Séron">Karin Séron</name><affiliation><nlm:affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Labitt, Rachael N" sort="Labitt, Rachael N" uniqKey="Labitt R" first="Rachael N" last="Labitt">Rachael N. Labitt</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Danneels, Adeline" sort="Danneels, Adeline" uniqKey="Danneels A" first="Adeline" last="Danneels">Adeline Danneels</name><affiliation><nlm:affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Palmer, Kenneth E" sort="Palmer, Kenneth E" uniqKey="Palmer K" first="Kenneth E" last="Palmer">Kenneth E. Palmer</name><affiliation><nlm:affiliation>Department of Pharmacology and Toxicology, James Graham Brown Cancer Center, University of Louisville School of Medicine, Louisville, KY, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R" last="Whittaker">Gary R. Whittaker</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Dubuisson, Jean" sort="Dubuisson, Jean" uniqKey="Dubuisson J" first="Jean" last="Dubuisson">Jean Dubuisson</name><affiliation><nlm:affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Belouzard, Sandrine" sort="Belouzard, Sandrine" uniqKey="Belouzard S" first="Sandrine" last="Belouzard">Sandrine Belouzard</name><affiliation><nlm:affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France. Electronic address: Sandrine.belouzard@ibl.cnrs.fr.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:27424494</idno><idno type="pmid">27424494</idno><idno type="doi">10.1016/j.antiviral.2016.07.011</idno><idno type="wicri:Area/PubMed/Corpus">001045</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001045</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Middle East respiratory syndrome coronavirus infection is inhibited by griffithsin.</title><author><name sortKey="Millet, Jean K" sort="Millet, Jean K" uniqKey="Millet J" first="Jean K" last="Millet">Jean K. Millet</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Seron, Karin" sort="Seron, Karin" uniqKey="Seron K" first="Karin" last="Séron">Karin Séron</name><affiliation><nlm:affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Labitt, Rachael N" sort="Labitt, Rachael N" uniqKey="Labitt R" first="Rachael N" last="Labitt">Rachael N. Labitt</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Danneels, Adeline" sort="Danneels, Adeline" uniqKey="Danneels A" first="Adeline" last="Danneels">Adeline Danneels</name><affiliation><nlm:affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Palmer, Kenneth E" sort="Palmer, Kenneth E" uniqKey="Palmer K" first="Kenneth E" last="Palmer">Kenneth E. Palmer</name><affiliation><nlm:affiliation>Department of Pharmacology and Toxicology, James Graham Brown Cancer Center, University of Louisville School of Medicine, Louisville, KY, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R" last="Whittaker">Gary R. Whittaker</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Dubuisson, Jean" sort="Dubuisson, Jean" uniqKey="Dubuisson J" first="Jean" last="Dubuisson">Jean Dubuisson</name><affiliation><nlm:affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Belouzard, Sandrine" sort="Belouzard, Sandrine" uniqKey="Belouzard S" first="Sandrine" last="Belouzard">Sandrine Belouzard</name><affiliation><nlm:affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France. Electronic address: Sandrine.belouzard@ibl.cnrs.fr.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Antiviral research</title><idno type="eISSN">1872-9096</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antiviral Agents (pharmacology)</term><term>Biological Products (pharmacology)</term><term>Cell Line</term><term>Cell Survival (drug effects)</term><term>Cells, Cultured</term><term>Coronavirus Infections (virology)</term><term>Dose-Response Relationship, Drug</term><term>Humans</term><term>Middle East Respiratory Syndrome Coronavirus (drug effects)</term><term>Middle East Respiratory Syndrome Coronavirus (physiology)</term><term>Plant Lectins (pharmacology)</term><term>Virus Internalization (drug effects)</term><term>Virus Replication (drug effects)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Biological Products</term><term>Plant Lectins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Survival</term><term>Middle East Respiratory Syndrome Coronavirus</term><term>Virus Internalization</term><term>Virus Replication</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Cells, Cultured</term><term>Dose-Response Relationship, Drug</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Highly pathogenic human coronaviruses associated with a severe respiratory syndrome, including Middle East respiratory syndrome coronavirus (MERS-CoV), have recently emerged. The MERS-CoV epidemic started in 2012 and is still ongoing, with a mortality rate of approximately 35%. No vaccine is available against MERS-CoV and therapeutic options for MERS-CoV infections are limited to palliative and supportive care. A search for specific antiviral treatments is urgently needed. Coronaviruses are enveloped viruses, with the spike proteins present on their surface responsible for virus entry into the target cell. Lectins are attractive anti-coronavirus candidates because of the highly glycosylated nature of the spike protein. We tested the antiviral effect of griffithsin (GRFT), a lectin isolated from the red marine alga Griffithsia sp. against MERS-CoV infection. Our results demonstrate that while displaying no significant cytotoxicity, griffithsin is a potent inhibitor of MERS-CoV infection. Griffithsin also inhibits entry into host cells of particles pseudotyped with the MERS-CoV spike protein, suggesting that griffithsin inhibits spike protein function during entry. Spike proteins have a dual function during entry, they mediate binding to the host cell surface and also the fusion of the viral envelope with host cell membrane. Time course experiments show that griffithsin inhibits MERS-CoV infection at the binding step. In conclusion, we identify griffithsin as a potent inhibitor of MERS-CoV infection at the entry step.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27424494</PMID><DateCompleted><Year>2017</Year><Month>11</Month><Day>16</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-9096</ISSN><JournalIssue CitedMedium="Internet"><Volume>133</Volume><PubDate><Year>2016</Year><Month>09</Month></PubDate></JournalIssue><Title>Antiviral research</Title><ISOAbbreviation>Antiviral Res.</ISOAbbreviation></Journal><ArticleTitle>Middle East respiratory syndrome coronavirus infection is inhibited by griffithsin.</ArticleTitle><Pagination><MedlinePgn>1-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.antiviral.2016.07.011</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0166-3542(16)30172-3</ELocationID><Abstract><AbstractText>Highly pathogenic human coronaviruses associated with a severe respiratory syndrome, including Middle East respiratory syndrome coronavirus (MERS-CoV), have recently emerged. The MERS-CoV epidemic started in 2012 and is still ongoing, with a mortality rate of approximately 35%. No vaccine is available against MERS-CoV and therapeutic options for MERS-CoV infections are limited to palliative and supportive care. A search for specific antiviral treatments is urgently needed. Coronaviruses are enveloped viruses, with the spike proteins present on their surface responsible for virus entry into the target cell. Lectins are attractive anti-coronavirus candidates because of the highly glycosylated nature of the spike protein. We tested the antiviral effect of griffithsin (GRFT), a lectin isolated from the red marine alga Griffithsia sp. against MERS-CoV infection. Our results demonstrate that while displaying no significant cytotoxicity, griffithsin is a potent inhibitor of MERS-CoV infection. Griffithsin also inhibits entry into host cells of particles pseudotyped with the MERS-CoV spike protein, suggesting that griffithsin inhibits spike protein function during entry. Spike proteins have a dual function during entry, they mediate binding to the host cell surface and also the fusion of the viral envelope with host cell membrane. Time course experiments show that griffithsin inhibits MERS-CoV infection at the binding step. In conclusion, we identify griffithsin as a potent inhibitor of MERS-CoV infection at the entry step.</AbstractText><CopyrightInformation>Copyright © 2016 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Millet</LastName><ForeName>Jean K</ForeName><Initials>JK</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Séron</LastName><ForeName>Karin</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Labitt</LastName><ForeName>Rachael N</ForeName><Initials>RN</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Danneels</LastName><ForeName>Adeline</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Palmer</LastName><ForeName>Kenneth E</ForeName><Initials>KE</Initials><AffiliationInfo><Affiliation>Department of Pharmacology and Toxicology, James Graham Brown Cancer Center, University of Louisville School of Medicine, Louisville, KY, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Whittaker</LastName><ForeName>Gary R</ForeName><Initials>GR</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dubuisson</LastName><ForeName>Jean</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Belouzard</LastName><ForeName>Sandrine</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Centre d'Infection et d'Immunité de Lille, F-59000, Lille, France. Electronic address: Sandrine.belouzard@ibl.cnrs.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R21 AI111085</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>2016</Year><Month>07</Month><Day>15</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="D001688">Biological Products</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037121">Plant Lectins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C499654">griffithsin protein, Griffithsia</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="D001688" MajorTopicYN="N">Biological Products</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002470" MajorTopicYN="N">Cell Survival</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018352" MajorTopicYN="N">Coronavirus Infections</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D065207" MajorTopicYN="N">Middle East Respiratory Syndrome Coronavirus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000502" 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