Picomolar inhibition of SARS-CoV-2 variants of concern by an engineered ACE2-IgG4-Fc fusion protein.


Journal

Antiviral research
ISSN: 1872-9096
Titre abrégé: Antiviral Res
Pays: Netherlands
ID NLM: 8109699

Informations de publication

Date de publication:
12 2021
Historique:
received: 12 07 2021
revised: 27 09 2021
accepted: 26 10 2021
pubmed: 15 11 2021
medline: 17 12 2021
entrez: 14 11 2021
Statut: ppublish

Résumé

SARS-CoV-2 enters host cells after binding through its spike glycoprotein to the angiotensin-converting enzyme 2 (ACE2) receptor. Soluble ACE2 ectodomains bind and neutralize the virus, yet their short in vivo half-live limits their therapeutic use. This limitation can be overcome by fusing the fragment crystallizable (Fc) part of human immunoglobulin G (IgG) to the ACE2 ectodomain, but this bears the risk of Fc-receptor activation and antibody-dependent cellular cytotoxicity. Here, we describe optimized ACE2-IgG4-Fc fusion constructs that avoid Fc-receptor activation, preserve the desired ACE2 enzymatic activity and show promising pharmaceutical properties. The engineered ACE2-IgG4-Fc fusion proteins neutralize the original SARS-CoV, pandemic SARS-CoV-2 as well as the rapidly spreading SARS-CoV-2 alpha, beta and delta variants of concern. Importantly, these variants of concern are inhibited at picomolar concentrations proving that ACE2-IgG4 maintains - in contrast to therapeutic antibodies - its full antiviral potential. Thus, ACE2-IgG4-Fc fusion proteins are promising candidate anti-antivirals to combat the current and future pandemics.

Identifiants

pubmed: 34774603
pii: S0166-3542(21)00187-X
doi: 10.1016/j.antiviral.2021.105197
pmc: PMC8579703
pii:
doi:

Substances chimiques

Antiviral Agents 0
Immunoglobulin G 0
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

105197

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier B.V. All rights reserved.

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Auteurs

Hristo L Svilenov (HL)

Department of Chemistry, Technical University of Munich, Garching, Germany.

Julia Sacherl (J)

Institute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany.

Alwin Reiter (A)

Formycon AG, Martinsried/Planegg, Germany.

Lisa S Wolff (LS)

Institute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany.

Cho-Chin Cheng (CC)

Institute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany; German Center for Infection Research, Munich Partner Site, Munich, Germany.

Marcel Stern (M)

Max von Pettenkofer Institute & Gene Center, Virology, LMU München, Munich, Germany; German Center for Infection Research, Munich Partner Site, Munich, Germany.

Vincent Grass (V)

Institute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany.

Martin Feuerherd (M)

Institute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany.

Frank-Peter Wachs (FP)

Formycon AG, Martinsried/Planegg, Germany.

Nicole Simonavicius (N)

Formycon AG, Martinsried/Planegg, Germany.

Susanne Pippig (S)

Formycon AG, Martinsried/Planegg, Germany.

Florian Wolschin (F)

Formycon AG, Martinsried/Planegg, Germany.

Oliver T Keppler (OT)

Max von Pettenkofer Institute & Gene Center, Virology, LMU München, Munich, Germany; German Center for Infection Research, Munich Partner Site, Munich, Germany.

Johannes Buchner (J)

Department of Chemistry, Technical University of Munich, Garching, Germany.

Carsten Brockmeyer (C)

Formycon AG, Martinsried/Planegg, Germany. Electronic address: carsten.brockmeyer@formycon.com.

Ulrike Protzer (U)

Institute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany; German Center for Infection Research, Munich Partner Site, Munich, Germany. Electronic address: protzer@tum.de.

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Classifications MeSH