Umeå University's logo

umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets
Department of Medical Biochemistry and Microbiology, Uppsala University, Box 582, Husargatan 3, Uppsala, Sweden.
Department of Chemistry - BMC, Uppsala University, Box 576, Husargatan 3, Uppsala, Sweden.
Department of Chemistry - BMC, Uppsala University, Box 576, Husargatan 3, Uppsala, Sweden.
Umeå University, Faculty of Medicine, Department of Clinical Microbiology. Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).
Show others and affiliations
2023 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 14, no 1, article id 5636Article in journal (Refereed) Published
Abstract [en]

The virus life cycle depends on host-virus protein-protein interactions, which often involve a disordered protein region binding to a folded protein domain. Here, we used proteomic peptide phage display (ProP-PD) to identify peptides from the intrinsically disordered regions of the human proteome that bind to folded protein domains encoded by the SARS-CoV-2 genome. Eleven folded domains of SARS-CoV-2 proteins were found to bind 281 peptides from human proteins, and affinities of 31 interactions involving eight SARS-CoV-2 protein domains were determined (K D ∼ 7-300 μM). Key specificity residues of the peptides were established for six of the interactions. Two of the peptides, binding Nsp9 and Nsp16, respectively, inhibited viral replication. Our findings demonstrate how high-throughput peptide binding screens simultaneously identify potential host-virus interactions and peptides with antiviral properties. Furthermore, the high number of low-affinity interactions suggest that overexpression of viral proteins during infection may perturb multiple cellular pathways.

Place, publisher, year, edition, pages
Nature Publishing Group, 2023. Vol. 14, no 1, article id 5636
National Category
Infectious Medicine
Identifiers
URN: urn:nbn:se:umu:diva-214614DOI: 10.1038/s41467-023-41312-8PubMedID: 37704626Scopus ID: 2-s2.0-85171182010OAI: oai:DiVA.org:umu-214614DiVA, id: diva2:1800639
Funder
Swedish Foundation for Strategic Research, SB16-0039Swedish Research Council, 2020-03380Swedish Research Council, 2020-04395Swedish Research Council, 2018-05851Knut and Alice Wallenberg Foundation, KAW 2020.0241Knut and Alice Wallenberg Foundation, V-2020-0699Available from: 2023-09-27 Created: 2023-09-27 Last updated: 2023-09-27Bibliographically approved

Open Access in DiVA

fulltext(2681 kB)42 downloads
File information
File name FULLTEXT01.pdfFile size 2681 kBChecksum SHA-512
b0b1f037f3008ed016d5c68cab223dee0715e3f1be6c1527b7f07bff9b121a574e97f3b7681b0ee9c57d41be367ae40dbdddb3c2b9deacc7586c0b55fc4c6b2a
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMedScopus

Authority records

Lindquist, RichardÖverby, Anna K.

Search in DiVA

By author/editor
Lindquist, RichardÖverby, Anna K.
By organisation
Department of Clinical MicrobiologyMolecular Infection Medicine Sweden (MIMS)
In the same journal
Nature Communications
Infectious Medicine

Search outside of DiVA

GoogleGoogle Scholar
Total: 42 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 241 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf