{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T09:34:00Z","timestamp":1768469640907,"version":"3.49.0"},"reference-count":72,"publisher":"MDPI AG","issue":"19","license":[{"start":{"date-parts":[[2021,10,7]],"date-time":"2021-10-07T00:00:00Z","timestamp":1633564800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Coronavirus disease 19, or COVID-19, is an infection associated with an unprecedented worldwide pandemic caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), which has led to more than 215 million infected people and more than 4.5 million deaths worldwide. SARS-CoV-2 cell infection is initiated by a densely glycosylated spike (S) protein, a fusion protein, binding human angiotensin converting enzyme 2 (hACE2), that acts as the functional receptor through the receptor binding domain (RBD). In this article, the interaction of hACE2 with the RBD and how fusion is initiated after recognition are explored, as well as how mutations influence infectivity and immune response. Thus, we focused on all structures available in the Protein Data Bank for the interaction between SARS-CoV-2 S protein and hACE2. Specifically, the Delta variant carries particular mutations associated with increased viral fitness through decreased antibody binding, increased RBD affinity and altered protein dynamics. Combining both existing mutations and mutagenesis studies, new potential SARS-CoV-2 variants, harboring advantageous S protein mutations, may be predicted. These include mutations S13I and W152C, decreasing antibody binding, N460K, increasing RDB affinity, or Q498R, positively affecting both properties.<\/jats:p>","DOI":"10.3390\/ijms221910836","type":"journal-article","created":{"date-parts":[[2021,10,8]],"date-time":"2021-10-08T21:23:55Z","timestamp":1633728235000},"page":"10836","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":32,"title":["SARS-CoV-2 Virus\u2212Host Interaction: Currently Available Structures and Implications of Variant Emergence on Infectivity and Immune Response"],"prefix":"10.3390","volume":"22","author":[{"given":"Lu\u00eds","family":"Queir\u00f3s-Reis","sequence":"first","affiliation":[{"name":"Abel Salazar Institute of Biomedical Sciences (ICBAS), University of Porto, 4050-313 Porto, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8384-0640","authenticated-orcid":false,"given":"Priscilla","family":"Gomes da Silva","sequence":"additional","affiliation":[{"name":"Abel Salazar Institute of Biomedical Sciences (ICBAS), University of Porto, 4050-313 Porto, Portugal"},{"name":"Epidemiology Research Unit (EPIunit), Institute of Public Health, University of Porto, 4050-091 Porto, Portugal"},{"name":"LEPABE\u2014Laboratory for Process Engineering, Environment, Biotechnology and Energy, Faculty of Engineering, University of Porto, 4200-465 Porto, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2191-527X","authenticated-orcid":false,"given":"Jos\u00e9","family":"Gon\u00e7alves","sequence":"additional","affiliation":[{"name":"Institute of Sustainable Processes, University of Valladolid, 47011 Valladolid, Spain"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9728-3419","authenticated-orcid":false,"given":"Andrea","family":"Brancale","sequence":"additional","affiliation":[{"name":"Cardiff School of Pharmacy and Pharmaceutical Sciences, Cardiff University, Cardiff CF10 3NB, UK"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2491-5868","authenticated-orcid":false,"given":"Marcella","family":"Bassetto","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Science and Engineering, Swansea University, \r\n\t\t Swansea SA2 8PP, UK"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8769-8103","authenticated-orcid":false,"given":"Jo\u00e3o R.","family":"Mesquita","sequence":"additional","affiliation":[{"name":"Abel Salazar Institute of Biomedical Sciences (ICBAS), University of Porto, 4050-313 Porto, Portugal"},{"name":"Epidemiology Research Unit (EPIunit), Institute of Public Health, University of Porto, 4050-091 Porto, Portugal"}]}],"member":"1968","published-online":{"date-parts":[[2021,10,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"587269","DOI":"10.3389\/fcimb.2020.587269","article-title":"SARS-CoV-2: Structure, Biology, and Structure-Based Therapeutics Development","volume":"10","author":"Wang","year":"2020","journal-title":"Front Cell Infect. 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