Targeted intracellular degradation of SARS-CoV-2 via computationally optimized peptide fusions.
Identifieur interne : 000062 ( Main/Exploration ); précédent : 000061; suivant : 000063Targeted intracellular degradation of SARS-CoV-2 via computationally optimized peptide fusions.
Auteurs : Pranam Chatterjee [États-Unis] ; Manvitha Ponnapati [États-Unis] ; Christian Kramme [États-Unis] ; Alexandru M. Plesa [États-Unis] ; George M. Church [États-Unis] ; Joseph M. Jacobson [États-Unis]Source :
- Communications biology [ 2399-3642 ] ; 2020.
Abstract
The COVID-19 pandemic, caused by the novel coronavirus SARS-CoV-2, has elicited a global health crisis of catastrophic proportions. With only a few vaccines approved for early or limited use, there is a critical need for effective antiviral strategies. In this study, we report a unique antiviral platform, through computational design of ACE2-derived peptides which both target the viral spike protein receptor binding domain (RBD) and recruit E3 ubiquitin ligases for subsequent intracellular degradation of SARS-CoV-2 in the proteasome. Our engineered peptide fusions demonstrate robust RBD degradation capabilities in human cells and are capable of inhibiting infection-competent viral production, thus prompting their further experimental characterization and therapeutic development.
DOI: 10.1038/s42003-020-01470-7
PubMed: 33230174
PubMed Central: PMC7683566
Affiliations:
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Jacobson</name><affiliation wicri:level="1"><nlm:affiliation>The MIT Center for Bits and Atoms, Cambridge, MA, 02139, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>The MIT Center for Bits and Atoms, Cambridge, MA, 02139</wicri:regionArea><wicri:noRegion>02139</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>MIT Media Lab, Massachusetts Institute of Technology (MIT), Cambridge, MA, 02139-4307, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>MIT Media Lab, Massachusetts Institute of Technology (MIT), Cambridge, MA, 02139-4307</wicri:regionArea><wicri:noRegion>02139-4307</wicri:noRegion></affiliation></author></analytic><series><title level="j">Communications biology</title><idno type="eISSN">2399-3642</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The COVID-19 pandemic, caused by the novel coronavirus SARS-CoV-2, has elicited a global health crisis of catastrophic proportions. With only a few vaccines approved for early or limited use, there is a critical need for effective antiviral strategies. In this study, we report a unique antiviral platform, through computational design of ACE2-derived peptides which both target the viral spike protein receptor binding domain (RBD) and recruit E3 ubiquitin ligases for subsequent intracellular degradation of SARS-CoV-2 in the proteasome. Our engineered peptide fusions demonstrate robust RBD degradation capabilities in human cells and are capable of inhibiting infection-competent viral production, thus prompting their further experimental characterization and therapeutic development.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">33230174</PMID><DateRevised><Year>2020</Year><Month>12</Month><Day>07</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2399-3642</ISSN><JournalIssue CitedMedium="Internet"><Volume>3</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>11</Month><Day>23</Day></PubDate></JournalIssue><Title>Communications biology</Title><ISOAbbreviation>Commun Biol</ISOAbbreviation></Journal><ArticleTitle>Targeted intracellular degradation of SARS-CoV-2 via computationally optimized peptide fusions.</ArticleTitle><Pagination><MedlinePgn>715</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s42003-020-01470-7</ELocationID><Abstract><AbstractText>The COVID-19 pandemic, caused by the novel coronavirus SARS-CoV-2, has elicited a global health crisis of catastrophic proportions. With only a few vaccines approved for early or limited use, there is a critical need for effective antiviral strategies. In this study, we report a unique antiviral platform, through computational design of ACE2-derived peptides which both target the viral spike protein receptor binding domain (RBD) and recruit E3 ubiquitin ligases for subsequent intracellular degradation of SARS-CoV-2 in the proteasome. Our engineered peptide fusions demonstrate robust RBD degradation capabilities in human cells and are capable of inhibiting infection-competent viral production, thus prompting their further experimental characterization and therapeutic development.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chatterjee</LastName><ForeName>Pranam</ForeName><Initials>P</Initials><Identifier Source="ORCID">0000-0003-3957-8478</Identifier><AffiliationInfo><Affiliation>The MIT Center for Bits and Atoms, Cambridge, MA, 02139, USA. pranam@mit.edu.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>MIT Media Lab, Massachusetts Institute of Technology (MIT), Cambridge, MA, 02139-4307, USA. pranam@mit.edu.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Genetics, Harvard Medical School, Boston, MA, 02115, USA. pranam@mit.edu.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Wyss Institute for Biologically Inspired Engineering, Harvard University, Center for Life Science Bldg., Boston, MA, 02115, USA. pranam@mit.edu.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ponnapati</LastName><ForeName>Manvitha</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>The MIT Center for Bits and Atoms, Cambridge, MA, 02139, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>MIT Media Lab, Massachusetts Institute of Technology (MIT), Cambridge, MA, 02139-4307, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kramme</LastName><ForeName>Christian</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Genetics, Harvard Medical School, Boston, MA, 02115, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Wyss Institute for Biologically Inspired Engineering, Harvard University, Center for Life Science Bldg., Boston, MA, 02115, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Plesa</LastName><ForeName>Alexandru M</ForeName><Initials>AM</Initials><Identifier Source="ORCID">0000-0002-0414-4285</Identifier><AffiliationInfo><Affiliation>Department of Genetics, Harvard Medical School, Boston, MA, 02115, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Wyss Institute for Biologically Inspired Engineering, Harvard University, Center for Life Science Bldg., Boston, MA, 02115, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Church</LastName><ForeName>George M</ForeName><Initials>GM</Initials><AffiliationInfo><Affiliation>Department of Genetics, Harvard Medical School, Boston, MA, 02115, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Wyss Institute for Biologically Inspired Engineering, Harvard University, Center for Life Science Bldg., Boston, MA, 02115, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jacobson</LastName><ForeName>Joseph 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Chatterjee</name></noRegion><name sortKey="Chatterjee, Pranam" sort="Chatterjee, Pranam" uniqKey="Chatterjee P" first="Pranam" last="Chatterjee">Pranam Chatterjee</name><name sortKey="Chatterjee, Pranam" sort="Chatterjee, Pranam" uniqKey="Chatterjee P" first="Pranam" last="Chatterjee">Pranam Chatterjee</name><name sortKey="Chatterjee, Pranam" sort="Chatterjee, Pranam" uniqKey="Chatterjee P" first="Pranam" last="Chatterjee">Pranam Chatterjee</name><name sortKey="Church, George M" sort="Church, George M" uniqKey="Church G" first="George M" last="Church">George M. Church</name><name sortKey="Church, George M" sort="Church, George M" uniqKey="Church G" first="George M" last="Church">George M. Church</name><name sortKey="Jacobson, Joseph M" sort="Jacobson, Joseph M" uniqKey="Jacobson J" first="Joseph M" last="Jacobson">Joseph M. Jacobson</name><name sortKey="Jacobson, Joseph M" sort="Jacobson, Joseph M" uniqKey="Jacobson J" first="Joseph M" last="Jacobson">Joseph M. Jacobson</name><name sortKey="Kramme, Christian" sort="Kramme, Christian" uniqKey="Kramme C" first="Christian" last="Kramme">Christian Kramme</name><name sortKey="Kramme, Christian" sort="Kramme, Christian" uniqKey="Kramme C" first="Christian" last="Kramme">Christian Kramme</name><name sortKey="Plesa, Alexandru M" sort="Plesa, Alexandru M" uniqKey="Plesa A" first="Alexandru M" last="Plesa">Alexandru M. Plesa</name><name sortKey="Plesa, Alexandru M" sort="Plesa, Alexandru M" uniqKey="Plesa A" first="Alexandru M" last="Plesa">Alexandru M. Plesa</name><name sortKey="Ponnapati, Manvitha" sort="Ponnapati, Manvitha" uniqKey="Ponnapati M" first="Manvitha" last="Ponnapati">Manvitha Ponnapati</name><name sortKey="Ponnapati, Manvitha" sort="Ponnapati, Manvitha" uniqKey="Ponnapati M" first="Manvitha" last="Ponnapati">Manvitha Ponnapati</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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