{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,5]],"date-time":"2026-05-05T22:40:40Z","timestamp":1778020840654,"version":"3.51.4"},"reference-count":48,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2023,10,16]],"date-time":"2023-10-16T00:00:00Z","timestamp":1697414400000},"content-version":"vor","delay-in-days":15,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000030","name":"Centers for Disease Control and Prevention","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000030","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Medical Virology"],"published-print":{"date-parts":[[2023,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Severe Acute Respiratory Syndrome Coronavirus 2 (SARS\u2010CoV\u20102) enters the host cell by binding to angiotensin\u2010converting enzyme 2 (ACE2). While evolutionarily conserved, ACE2 receptors differ across various species and differential interactions with Spike (S) glycoproteins of SARS\u2010CoV\u20102 viruses impact species specificity. Reverse zoonoses led to SARS\u2010CoV\u20102 outbreaks on multiple American mink (<jats:italic>Mustela vison<\/jats:italic>) farms during the pandemic and gave rise to mink\u2010associated S substitutions known for transmissibility between mink and zoonotic transmission to humans. In this study, we used bio\u2010layer interferometry (BLI) to discern the differences in binding affinity between multiple human and mink\u2010derived S glycoproteins of SARS\u2010CoV\u20102 and their respective ACE2 receptors. Further, we conducted a structural analysis of a mink variant S glycoprotein and American mink ACE2 (mvACE2) using cryo\u2010electron microscopy (cryo\u2010EM), revealing four distinct conformations. We discovered a novel intermediary conformation where the mvACE2 receptor is bound to the receptor\u2010binding domain (RBD) of the S glycoprotein in a \u201cdown\u201d position, approximately 34\u00b0 lower than previously reported \u201cup\u201d RBD. Finally, we compared residue interactions in the S\u2010ACE2 complex interface of S glycoprotein conformations with varying RBD orientations. These findings provide valuable insights into the molecular mechanisms of SARS\u2010CoV\u20102 entry.<\/jats:p>","DOI":"10.1002\/jmv.29163","type":"journal-article","created":{"date-parts":[[2023,10,16]],"date-time":"2023-10-16T09:19:35Z","timestamp":1697447975000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Structural basis of the American mink ACE2 binding by Y453F trimeric spike glycoproteins of SARS\u2010CoV\u20102"],"prefix":"10.1002","volume":"95","author":[{"given":"Hyunjun","family":"Ahn","sequence":"first","affiliation":[{"name":"Department of Biochemistry Emory University School of Medicine  Atlanta Georgia USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Brenda M.","family":"Calderon","sequence":"additional","affiliation":[{"name":"COVID\u201019 Emergency Response Centers for Disease Control and Prevention  Atlanta Georgia USA"},{"name":"Influenza Division, National Center for 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