Peptides derived from the SARS-CoV-2 receptor binding motif bind to ACE2 but do not block ACE2-mediated host cell entry or pro-inflammatory cytokine induction.


Journal

PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081

Informations de publication

Date de publication:
2021
Historique:
received: 01 09 2021
accepted: 05 11 2021
entrez: 18 11 2021
pubmed: 19 11 2021
medline: 1 12 2021
Statut: epublish

Résumé

SARS-CoV-2 viral attachment and entry into host cells is mediated by a direct interaction between viral spike glycoproteins and membrane bound angiotensin-converting enzyme 2 (ACE2). The receptor binding motif (RBM), located within the S1 subunit of the spike protein, incorporates the majority of known ACE2 contact residues responsible for high affinity binding and associated virulence. Observation of existing crystal structures of the SARS-CoV-2 receptor binding domain (SRBD)-ACE2 interface, combined with peptide array screening, allowed us to define a series of linear native RBM-derived peptides that were selected as potential antiviral decoy sequences with the aim of directly binding ACE2 and attenuating viral cell entry. RBM1 (16mer): S443KVGGNYNYLYRLFRK458, RBM2A (25mer): E484GFNCYFPLQSYGFQPTNGVGYQPY508, RBM2B (20mer): F456NCYFPLQSYGFQPTNGVGY505 and RBM2A-Sc (25mer): NYGLQGSPFGYQETPYPFCNFVQYG. Data from fluorescence polarisation experiments suggested direct binding between RBM peptides and ACE2, with binding affinities ranging from the high nM to low μM range (Kd = 0.207-1.206 μM). However, the RBM peptides demonstrated only modest effects in preventing SRBD internalisation and showed no antiviral activity in a spike protein trimer neutralisation assay. The RBM peptides also failed to suppress S1-protein mediated inflammation in an endogenously expressing ACE2 human cell line. We conclude that linear native RBM-derived peptides are unable to outcompete viral spike protein for binding to ACE2 and therefore represent a suboptimal approach to inhibiting SARS-CoV-2 viral cell entry. These findings reinforce the notion that larger biologics (such as soluble ACE2, 'miniproteins', nanobodies and antibodies) are likely better suited as SARS-CoV-2 cell-entry inhibitors than short-sequence linear peptides.

Identifiants

pubmed: 34793553
doi: 10.1371/journal.pone.0260283
pii: PONE-D-21-28336
pmc: PMC8601423
doi:

Substances chimiques

Antiviral Agents 0
Peptides 0
Spike Glycoprotein, Coronavirus 0
spike protein, SARS-CoV-2 0
ACE2 protein, human EC 3.4.17.23
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

e0260283

Subventions

Organisme : Medical Research Council
ID : MC_PC_19026
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_UU_12014/7
Pays : United Kingdom

Déclaration de conflit d'intérêts

The authors declare no competing interests.

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Auteurs

Amit Mahindra (A)

School of Chemistry, University of Glasgow, Glasgow, United Kingdom.

Gonzalo Tejeda (G)

Institute of Molecular Cell & Systems Biology, School of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.

Mario Rossi (M)

Institute of Molecular Cell & Systems Biology, School of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
Department of Biotechnological and Applied Clinical Sciences, University of L'Aquila, L'Aquila, Italy.

Omar Janha (O)

Institute of Molecular Cell & Systems Biology, School of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.

Imogen Herbert (I)

MRC Centre for Virus Research, University of Glasgow, Glasgow, United Kingdom.

Caroline Morris (C)

School of Chemistry, University of Glasgow, Glasgow, United Kingdom.

Danielle C Morgan (DC)

School of Chemistry, University of Glasgow, Glasgow, United Kingdom.

Wendy Beattie (W)

Institute of Cardiovascular and Medical Sciences, Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.

Augusto C Montezano (AC)

Institute of Cardiovascular and Medical Sciences, Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.

Brian Hudson (B)

Institute of Molecular Cell & Systems Biology, School of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.

Andrew B Tobin (AB)

Institute of Molecular Cell & Systems Biology, School of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.

David Bhella (D)

MRC Centre for Virus Research, University of Glasgow, Glasgow, United Kingdom.

Rhian M Touyz (RM)

Institute of Cardiovascular and Medical Sciences, Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.

Andrew G Jamieson (AG)

School of Chemistry, University of Glasgow, Glasgow, United Kingdom.

George S Baillie (GS)

Institute of Cardiovascular and Medical Sciences, Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.

Connor M Blair (CM)

Institute of Cardiovascular and Medical Sciences, Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.

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Classifications MeSH