Progressive membrane-binding mechanism of SARS-CoV-2 variant spike proteins
Summary: Membrane recognition by viral spike proteins is critical for infection. Here we show the host cell membrane-binding surfaces of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike variants Alpha, Beta, Gamma, Delta, Epsilon, Kappa, and Omicron as well as SARS-CoV-1 and pangol...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2022-08-01
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| Series: | iScience |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2589004222009944 |
| _version_ | 1811294172589588480 |
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| author | Michael Overduin Troy A. Kervin Anh Tran |
| author_facet | Michael Overduin Troy A. Kervin Anh Tran |
| author_sort | Michael Overduin |
| collection | DOAJ |
| description | Summary: Membrane recognition by viral spike proteins is critical for infection. Here we show the host cell membrane-binding surfaces of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike variants Alpha, Beta, Gamma, Delta, Epsilon, Kappa, and Omicron as well as SARS-CoV-1 and pangolin and bat relatives. They show increases in membrane binding propensities over time, with all spike head mutations in variants, and particularly BA.1, impacting the protein’s affinity to cell membranes. Comparison of hundreds of structures yields a progressive model of membrane docking in which spike protein trimers shift from initial perpendicular stances to increasingly tilted positions that draw viral particles alongside host cell membranes before optionally engaging angiotensin-converting enzyme 2 (ACE2) receptors. This culminates in the assembly of the symmetric fusion apparatus, with enhanced membrane interactions of variants explaining their unique cell fusion capacities and COVID-19 disease transmission rates. |
| first_indexed | 2024-04-13T05:12:33Z |
| format | Article |
| id | doaj.art-145aab6d8a8d4d62a405b1a5bf7640f6 |
| institution | Directory Open Access Journal |
| issn | 2589-0042 |
| language | English |
| last_indexed | 2024-04-13T05:12:33Z |
| publishDate | 2022-08-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj.art-145aab6d8a8d4d62a405b1a5bf7640f62022-12-22T03:00:59ZengElsevieriScience2589-00422022-08-01258104722Progressive membrane-binding mechanism of SARS-CoV-2 variant spike proteinsMichael Overduin0Troy A. Kervin1Anh Tran2Department of Biochemistry, University of Alberta, Edmonton, AB, Canada; Corresponding authorDepartment of Biochemistry, University of Alberta, Edmonton, AB, CanadaDepartment of Biochemistry, University of Alberta, Edmonton, AB, CanadaSummary: Membrane recognition by viral spike proteins is critical for infection. Here we show the host cell membrane-binding surfaces of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike variants Alpha, Beta, Gamma, Delta, Epsilon, Kappa, and Omicron as well as SARS-CoV-1 and pangolin and bat relatives. They show increases in membrane binding propensities over time, with all spike head mutations in variants, and particularly BA.1, impacting the protein’s affinity to cell membranes. Comparison of hundreds of structures yields a progressive model of membrane docking in which spike protein trimers shift from initial perpendicular stances to increasingly tilted positions that draw viral particles alongside host cell membranes before optionally engaging angiotensin-converting enzyme 2 (ACE2) receptors. This culminates in the assembly of the symmetric fusion apparatus, with enhanced membrane interactions of variants explaining their unique cell fusion capacities and COVID-19 disease transmission rates.http://www.sciencedirect.com/science/article/pii/S2589004222009944VirologyStructural biologyProtein structure aspects |
| spellingShingle | Michael Overduin Troy A. Kervin Anh Tran Progressive membrane-binding mechanism of SARS-CoV-2 variant spike proteins iScience Virology Structural biology Protein structure aspects |
| title | Progressive membrane-binding mechanism of SARS-CoV-2 variant spike proteins |
| title_full | Progressive membrane-binding mechanism of SARS-CoV-2 variant spike proteins |
| title_fullStr | Progressive membrane-binding mechanism of SARS-CoV-2 variant spike proteins |
| title_full_unstemmed | Progressive membrane-binding mechanism of SARS-CoV-2 variant spike proteins |
| title_short | Progressive membrane-binding mechanism of SARS-CoV-2 variant spike proteins |
| title_sort | progressive membrane binding mechanism of sars cov 2 variant spike proteins |
| topic | Virology Structural biology Protein structure aspects |
| url | http://www.sciencedirect.com/science/article/pii/S2589004222009944 |
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