Permission is not required) please go to the Copyright If you want to reproduce the wholeĪrticle in a third-party commercial publication (excluding your thesis/dissertation for which If you are the author of this article, you do not need to request permission to reproduce figuresĪnd diagrams provided correct acknowledgement is given. Provided correct acknowledgement is given. If you are an author contributing to an RSC publication, you do not need to request permission Please go to the Copyright Clearance Center request page. To request permission to reproduce material from this article in a commercial publication, Provided that the correct acknowledgement is given and it is not used for commercial purposes. This article in other publications, without requesting further permission from the RSC, Kasson,Ĭreative Commons Attribution-NonCommercial 3.0 Unported Licence. The ACE2 receptor accelerates but is not biochemically required for SARS-CoV-2 membrane fusion Since ACE2 serves as the high-affinity attachment factor on human cells, the possibility to replace it with other factors implies a flatter fitness landscape for host adaptation by SARS-CoV-2 and future related coronaviruses. Kinetic analysis suggests at least two rate-limiting steps for SARS-CoV-2 membrane fusion, one of which is ACE2 dependent and one of which is not. On a per-spike level, ACE2 appears to promote activation for fusion and then subsequent inactivation if an appropriate protease is not present. However, addition of soluble ACE2 speeds the fusion reaction. Thus, ACE2 is not biochemically required for SARS-CoV-2 membrane fusion. We find that SARS-CoV-2 pseudovirus and virus-like particles are capable of membrane fusion without ACE2 if activated with an appropriate protease. Here, we test that hypothesis directly, using DNA-lipid tethering as a synthetic attachment factor in place of ACE2. Structural evidence suggests that ACE2 may not just serve as an attachment factor but also conformationally activate the SARS-CoV-2 spike protein for membrane fusion. The SARS-CoV-2 coronavirus infects human cells via the ACE2 receptor.
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