A dimeric proteomimetic prevents SARS-CoV-2 infection by dimerizing the spike protein.


Journal

Nature chemical biology
ISSN: 1552-4469
Titre abrégé: Nat Chem Biol
Pays: United States
ID NLM: 101231976

Informations de publication

Date de publication:
10 2022
Historique:
received: 06 12 2021
accepted: 10 05 2022
pubmed: 3 6 2022
medline: 28 9 2022
entrez: 2 6 2022
Statut: ppublish

Résumé

Protein tertiary structure mimetics are valuable tools to target large protein-protein interaction interfaces. Here, we demonstrate a strategy for designing dimeric helix-hairpin motifs from a previously reported three-helix-bundle miniprotein that targets the receptor-binding domain (RBD) of severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2). Through truncation of the third helix and optimization of the interhelical loop residues of the miniprotein, we developed a thermostable dimeric helix-hairpin. The dimeric four-helix bundle competes with the human angiotensin-converting enzyme 2 (ACE2) in binding to RBD with 2:2 stoichiometry. Cryogenic-electron microscopy revealed the formation of dimeric spike ectodomain trimer by the four-helix bundle, where all the three RBDs from either spike protein are attached head-to-head in an open conformation, revealing a novel mechanism for virus neutralization. The proteomimetic protects hamsters from high dose viral challenge with replicative SARS-CoV-2 viruses, demonstrating the promise of this class of peptides that inhibit protein-protein interaction through target dimerization.

Identifiants

pubmed: 35654847
doi: 10.1038/s41589-022-01060-0
pii: 10.1038/s41589-022-01060-0
pmc: PMC9512702
doi:

Substances chimiques

Peptides 0
Spike Glycoprotein, Coronavirus 0
spike protein, SARS-CoV-2 0
Peptidyl-Dipeptidase A EC 3.4.15.1
Angiotensin-Converting Enzyme 2 EC 3.4.17.23

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1046-1055

Informations de copyright

© 2022. The Author(s), under exclusive licence to Springer Nature America, Inc.

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Auteurs

Bhavesh Khatri (B)

Molecular Biophysics Unit (MBU), Indian Institute of Science, Bangalore, India.

Ishika Pramanick (I)

Molecular Biophysics Unit (MBU), Indian Institute of Science, Bangalore, India.

Sameer Kumar Malladi (SK)

Molecular Biophysics Unit (MBU), Indian Institute of Science, Bangalore, India.

Raju S Rajmani (RS)

Molecular Biophysics Unit (MBU), Indian Institute of Science, Bangalore, India.

Sahil Kumar (S)

Virology Unit, Institute of Microbial Technology, Council of Scientific and Industrial Research (CSIR), Chandigarh, India.

Pritha Ghosh (P)

Molecular Biophysics Unit (MBU), Indian Institute of Science, Bangalore, India.

Nayanika Sengupta (N)

Molecular Biophysics Unit (MBU), Indian Institute of Science, Bangalore, India.

R Rahisuddin (R)

Institute of Microbial Technology, Council of Scientific and Industrial Research (CSIR), Chandigarh, India.

Narender Kumar (N)

Institute of Microbial Technology, Council of Scientific and Industrial Research (CSIR), Chandigarh, India.

S Kumaran (S)

Institute of Microbial Technology, Council of Scientific and Industrial Research (CSIR), Chandigarh, India.

Rajesh P Ringe (RP)

Virology Unit, Institute of Microbial Technology, Council of Scientific and Industrial Research (CSIR), Chandigarh, India.

Raghavan Varadarajan (R)

Molecular Biophysics Unit (MBU), Indian Institute of Science, Bangalore, India.

Somnath Dutta (S)

Molecular Biophysics Unit (MBU), Indian Institute of Science, Bangalore, India. somnath@iisc.ac.in.

Jayanta Chatterjee (J)

Molecular Biophysics Unit (MBU), Indian Institute of Science, Bangalore, India. jayanta@iisc.ac.in.

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Classifications MeSH