{"id":{"repo_id":"cornell","oai_identifier":"oai:ecommons.cornell.edu:1813/117600"},"canonical_url":"https://search.dev.ndltd.org/etd/cornell/oai:ecommons.cornell.edu:1813/117600","repository":{"repo_id":"cornell","name":"Cornell University","base_url":"https://ecommons.cornell.edu/server/oai/request"},"display":{"title":"CHASING VARIANTS: MAKING THE MATCH BETWEEN THE SARS-COV-2 S1/S2 CLEAVAGE SITE AND HOST CELL PROTEASES","abstract":"SARS-CoV-2 has spread rapidly throughout the human population since its discovery, and as it has spread it has acquired a variety of mutations. While many of these mutations have a role in immune evasion, some have impacted the role of the S protein in fusion and host cell entry. Among these are those mutations around the S1/S2 site, which is thought to be mainly cleaved by furin during virion formation. The 681st amino acid S position in particular has been the site nonynomymous substitutions several times, and interestingly has toggled between arginine (R) and histidine (H) ever since leaving the original proline (P) behind. In this work we investigate the impact of these mutations on the cleavability and function of the spike protein and also investigate the epidemiological context in which these mutations occurred and rapidly reached population dominance.","abstract_html":"SARS-CoV-2 has spread rapidly throughout the human population since its discovery, and as it has spread it has acquired a variety of mutations. While many of these mutations have a role in immune evasion, some have impacted the role of the S protein in fusion and host cell entry. Among these are those mutations around the S1/S2 site, which is thought to be mainly cleaved by furin during virion formation. The 681st amino acid S position in particular has been the site nonynomymous substitutions several times, and interestingly has toggled between arginine (R) and histidine (H) ever since leaving the original proline (P) behind. In this work we investigate the impact of these mutations on the cleavability and function of the spike protein and also investigate the epidemiological context in which these mutations occurred and rapidly reached population dominance.","abstract_has_math":false,"creators":["Lubinski, Bailey"],"institution":"Cornell University","degree_name":"Ph. 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While many of these mutations have a role in immune evasion, some have impacted the role of the S protein in fusion and host cell entry. Among these are those mutations around the S1/S2 site, which is thought to be mainly cleaved by furin during virion formation. The 681st amino acid S position in particular has been the site nonynomymous substitutions several times, and interestingly has toggled between arginine (R) and histidine (H) ever since leaving the original proline (P) behind. In this work we investigate the impact of these mutations on the cleavability and function of the spike protein and also investigate the epidemiological context in which these mutations occurred and rapidly reached population dominance."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["CHASING VARIANTS: MAKING THE MATCH BETWEEN THE SARS-COV-2 S1/S2 CLEAVAGE SITE AND HOST CELL PROTEASES"]}]}],"canonical_facts":{"dc:contributor.committeemember":["Parrish, Colin","Diel, Diego","Leifer, Cynthia"],"dc:creator":["Lubinski, Bailey"],"dc:date.accessioned":["2025-08-21T14:13:56Z"],"dc:date.issued":["2025-05"],"dc:description":["196 pages"],"dc:description.abstract":["SARS-CoV-2 has spread rapidly throughout the human population since its discovery, and as it has spread it has acquired a variety of mutations. 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