2026-09-20T21:55:12Zhttps://ecommons.cornell.edu/server/oai/requestoai:ecommons.cornell.edu:1813/1176002026-05-15T17:54:17Zcom_1813_35col_1813_47
Lubinski, Bailey
Whittaker, Gary
Parrish, Colin
Diel, Diego
Leifer, Cynthia
2025-08-21T14:13:56Z
2025-05
ProQuest Submission ID: 14984
ProQuest Publication ID: 32001095
https://hdl.handle.net/1813/117600
https://doi.org/10.7298/9c4p-9768
16938298
196 pages
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.
2027-06-18
en
Coronavirus
Furin
S1/S2 mutations
SARS-CoV-2
Spike
CHASING VARIANTS: MAKING THE MATCH BETWEEN THE SARS-COV-2 S1/S2 CLEAVAGE SITE AND HOST CELL PROTEASES
dissertation or thesis
https://newcatalog.library.cornell.edu/catalog/16938298
application/pdf
Biomedical and Biological Sciences
Cornell University
Doctor of Philosophy
Ph. D., Biomedical and Biological Sciences
https://hdl.handle.net/1813/59810.2
Publication
Cornell Theses and Dissertations
Lubinski, Bailey
5893a6ea-7af3-41d7-abc6-04bcd26ab5df
embargo
embargo
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<Keyword>Coronavirus</Keyword>
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<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>
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