{"entity": "researcher", "timestamp": "2026-08-25T13:32:54.148Z", "family": "Morbioli", "given": "Giorgio G", "initials": "GG", "orcid": "0000-0003-2665-9009", "affiliations": ["Departments of Molecular Physiology and Biomedical Engineering, University of Virginia Charlottesville VA 22908 USA kassonlab@gmail.com."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/384848feb1b646e5877956e9e0c951b9.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/384848feb1b646e5877956e9e0c951b9"}}, "publications": [{"entity": "publication", "iuid": "37146d4edea24c6b8be04499771a7a36", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/37146d4edea24c6b8be04499771a7a36.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/37146d4edea24c6b8be04499771a7a36"}}, "title": "The ACE2 receptor accelerates but is not biochemically required for SARS-CoV-2 membrane fusion.", "authors": [{"family": "Cervantes", "given": "Marcos", "initials": "M"}, {"family": "Hess", "given": "Tobin", "initials": "T"}, {"family": "Morbioli", "given": "Giorgio G", "initials": "GG", "orcid": "0000-0003-2665-9009", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/384848feb1b646e5877956e9e0c951b9.json"}}, {"family": "Sengar", "given": "Anjali", "initials": "A"}, {"family": "Kasson", "given": "Peter M", "initials": "PM", "orcid": "0000-0002-3111-8103", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/8c30532fab22425ab83ea04a65e33f72.json"}}], "type": "journal article", "published": "2023-06-28", "journal": {"title": "Chem Sci", "issn": "2041-6520", "volume": "14", "issue": "25", "pages": "6997-7004", "issn-l": null}, "abstract": "The SARS-CoV-2 coronavirus infects human cells via the ACE2 receptor. 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. Here, we test that hypothesis directly, using DNA-lipid tethering as a synthetic attachment factor in place of ACE2. We find that SARS-CoV-2 pseudovirus and virus-like particles are capable of membrane fusion without ACE2 if activated with an appropriate protease. Thus, ACE2 is not biochemically required for SARS-CoV-2 membrane fusion. However, addition of soluble ACE2 speeds up the fusion reaction. On a per-spike level, ACE2 appears to promote activation for fusion and then subsequent inactivation if an appropriate protease is not present. 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. Since ACE2 serves as a 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.", "doi": "10.1039/d2sc06967a", "pmid": "37389252", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC10306070"}, {"db": "pii", "key": "d2sc06967a"}], "notes": [], "created": "2026-08-21T11:58:08.790Z", "modified": "2026-08-21T11:58:08.926Z"}]}