dc.creator | Fernandez, Ariel | |
dc.date.accessioned | 2020-12-21T14:46:41Z | |
dc.date.accessioned | 2022-10-14T23:30:12Z | |
dc.date.available | 2020-12-21T14:46:41Z | |
dc.date.available | 2022-10-14T23:30:12Z | |
dc.date.created | 2020-12-21T14:46:41Z | |
dc.date.issued | 2020-09 | |
dc.identifier | Fernandez, Ariel; Structural Impact of Mutation D614G in SARS-CoV-2 Spike Protein: Enhanced Infectivity and Therapeutic Opportunity; American Chemical Society; ACS Medicinal Chemistry Letters; 11; 9; 9-2020; 1667-1670 | |
dc.identifier | 1948-5875 | |
dc.identifier | http://hdl.handle.net/11336/120934 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4319589 | |
dc.description.abstract | With the COVID-19 pandemic, the evolutionary fate of SARS-CoV-2 becomes a matter of utmost concern. Mutation D614G in the spike (S) protein has become dominant, and recent evidence suggests it yields a more stable phenotype with higher transmission efficacy. We carry out a structural analysis that provides mechanistic clues on the enhanced infectivity. The D614G substitution creates a sticky packing defect in subunit S1, promoting its association with subunit S2 as a means to stabilize the structure of S1 within the S1/S2 complex. The results raise the therapeutic possibility of immunologically targeting the epitope involved in stabilizing the G614 phenotype as a means of reducing the infection efficacy of SARS-CoV-2. This therapeutic modality would not a-priori interfere directly with current efforts toward the immunological targeting of the RBD epitope; hence, it could be exploited as a complementary treatment. | |
dc.language | eng | |
dc.publisher | American Chemical Society | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/acsmedchemlett.0c00410 | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/acsmedchemlett.0c00410 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | COVID-19 | |
dc.subject | SARS-CoV-2 | |
dc.subject | Biophysics | |
dc.subject | Dehydron Physics | |
dc.title | Structural Impact of Mutation D614G in SARS-CoV-2 Spike Protein: Enhanced Infectivity and Therapeutic Opportunity | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |