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Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
Extrinsic stabilization of antiviral ACE2-Fc fusion proteins targeting SARS-CoV-2.
Comm. Biol. 6:386 (2023)
The angiotensin-converting enzyme 2 (ACE2) is a viral receptor used by sarbecoviruses to infect cells. Fusion proteins comprising extracellular ACE2 domains and the Fc part of immunoglobulins exhibit high virus neutralization efficiency, but the structure and stability of these molecules are poorly understood. We show that although the hinge between the ACE2 and the IgG4-Fc is highly flexible, the conformational dynamics of the two ACE2 domains is restricted by their association. Interestingly, the conformational stability of the ACE2 moiety is much lower than that of the Fc part. We found that chemical compounds binding to ACE2, such as DX600 and MLN4760, can be used to strongly increase the thermal stability of the ACE2 by different mechanisms. Together, our findings reveal a general concept for stabilizing the labile receptor segments of therapeutic antiviral fusion proteins by chemical compounds.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Angiotensin-converting Enzyme; Binding; Spike
ISSN (print) / ISBN
2399-3642
e-ISSN
2399-3642
Journal
Communications Biology
Quellenangaben
Volume: 6,
Issue: 1,
Article Number: 386
Publisher
Springer
Publishing Place
London
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
Grants
DFG
Peter und Traudl Engelhorn Stiftung
Deutsche Forschungsgemeinschaft
Peter und Traudl Engelhorn Stiftung
Deutsche Forschungsgemeinschaft