The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective
ABSTRACT: Specific S477N, N501Y, K417N, K417T, E484K mutations in the receptor binding domain (RBD) of the spike protein in the wild type SARS-COV-2 virus have resulted, among others, in the following variants: B.1.160 (20A or EU2, first reported in continental Europe), B1.1.7 (α or 20I501Y.V1, firs...
- Autores:
-
Agudelo Gómez, Santiago
Rojas Valencia, Natalia Andrea
Restrepo Cossio, Albeiro Alonso
Gómez, Sara
Cappelli, Chiara
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2022
- Institución:
- Universidad de Antioquia
- Repositorio:
- Repositorio UdeA
- Idioma:
- eng
- OAI Identifier:
- oai:bibliotecadigital.udea.edu.co:10495/41664
- Acceso en línea:
- https://hdl.handle.net/10495/41664
- Palabra clave:
- COVID-19
Mutación
Mutation
Unión Proteica - genética
Protein Binding - genetics
SARS-CoV-2 - genética
SARS-CoV-2 - genetics
Glicoproteína de la Espiga del Coronavirus
Spike Glycoprotein, Coronavirus - chemistry - química
https://id.nlm.nih.gov/mesh/D000086382
https://id.nlm.nih.gov/mesh/D009154
https://id.nlm.nih.gov/mesh/D011485
https://id.nlm.nih.gov/mesh/D000086402
https://id.nlm.nih.gov/mesh/D064370
- Rights
- openAccess
- License
- https://creativecommons.org/licenses/by-nc-nd/4.0/
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| dc.title.spa.fl_str_mv |
The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective |
| title |
The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective |
| spellingShingle |
The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective COVID-19 Mutación Mutation Unión Proteica - genética Protein Binding - genetics SARS-CoV-2 - genética SARS-CoV-2 - genetics Glicoproteína de la Espiga del Coronavirus Spike Glycoprotein, Coronavirus - chemistry - química https://id.nlm.nih.gov/mesh/D000086382 https://id.nlm.nih.gov/mesh/D009154 https://id.nlm.nih.gov/mesh/D011485 https://id.nlm.nih.gov/mesh/D000086402 https://id.nlm.nih.gov/mesh/D064370 |
| title_short |
The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective |
| title_full |
The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective |
| title_fullStr |
The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective |
| title_full_unstemmed |
The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective |
| title_sort |
The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective |
| dc.creator.fl_str_mv |
Agudelo Gómez, Santiago Rojas Valencia, Natalia Andrea Restrepo Cossio, Albeiro Alonso Gómez, Sara Cappelli, Chiara |
| dc.contributor.author.none.fl_str_mv |
Agudelo Gómez, Santiago Rojas Valencia, Natalia Andrea Restrepo Cossio, Albeiro Alonso Gómez, Sara Cappelli, Chiara |
| dc.contributor.researchgroup.spa.fl_str_mv |
Grupo de Química-Física Teórica |
| dc.subject.decs.none.fl_str_mv |
COVID-19 Mutación Mutation Unión Proteica - genética Protein Binding - genetics SARS-CoV-2 - genética SARS-CoV-2 - genetics Glicoproteína de la Espiga del Coronavirus Spike Glycoprotein, Coronavirus - chemistry - química |
| topic |
COVID-19 Mutación Mutation Unión Proteica - genética Protein Binding - genetics SARS-CoV-2 - genética SARS-CoV-2 - genetics Glicoproteína de la Espiga del Coronavirus Spike Glycoprotein, Coronavirus - chemistry - química https://id.nlm.nih.gov/mesh/D000086382 https://id.nlm.nih.gov/mesh/D009154 https://id.nlm.nih.gov/mesh/D011485 https://id.nlm.nih.gov/mesh/D000086402 https://id.nlm.nih.gov/mesh/D064370 |
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https://id.nlm.nih.gov/mesh/D000086382 https://id.nlm.nih.gov/mesh/D009154 https://id.nlm.nih.gov/mesh/D011485 https://id.nlm.nih.gov/mesh/D000086402 https://id.nlm.nih.gov/mesh/D064370 |
| description |
ABSTRACT: Specific S477N, N501Y, K417N, K417T, E484K mutations in the receptor binding domain (RBD) of the spike protein in the wild type SARS-COV-2 virus have resulted, among others, in the following variants: B.1.160 (20A or EU2, first reported in continental Europe), B1.1.7 (α or 20I501Y.V1, first reported in the United Kingdom), B.1.351 (β or 20H/501Y.V2, first reported in South Africa), B.1.1.28.1 (γ or P.1 or 20J/501Y.V3, first reported in Brazil), and B.1.1.28.2 (ζ, or P.2 or 20B/S484K, also first reported in Brazil). From the analysis of a set of bonding descriptors firmly rooted in the formalism of quantum mechanics, including Natural Bond Orbitals (NBO), Quantum Theory of Atoms In Molecules (QTAIM) and highly correlated energies within the Domain Based Local Pair Natural Orbital Coupled Cluster Method (DLPNO-CCSD(T)), and from a set of compute electronic spectral patterns with environmental effects, we show that the new variants improve their ability to recognize available sites to either hydrogen bond or to form salt bridges with residues in the ACE2 receptor of the host cells. This results in significantly improved initial virus···cell molecular recognition and attachment at the microscopic level, which trigger the infectious cycle. |
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2022 |
| dc.date.issued.none.fl_str_mv |
2022 |
| dc.date.accessioned.none.fl_str_mv |
2024-09-02T11:59:57Z |
| dc.date.available.none.fl_str_mv |
2024-09-02T11:59:57Z |
| dc.type.spa.fl_str_mv |
Artículo de investigación |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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http://purl.org/coar/version/c_970fb48d4fbd8a85 |
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info:eu-repo/semantics/article |
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Gómez SA, Rojas-Valencia N, Gómez S, Cappelli C, Restrepo A. The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective. Chembiochem. 2022 Apr 5;23(7):e202100393. doi: 10.1002/cbic.202100393 |
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1439-4227 |
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https://hdl.handle.net/10495/41664 |
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10.1002/cbic.202100393 |
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1439-7633 |
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Gómez SA, Rojas-Valencia N, Gómez S, Cappelli C, Restrepo A. The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective. Chembiochem. 2022 Apr 5;23(7):e202100393. doi: 10.1002/cbic.202100393 1439-4227 10.1002/cbic.202100393 1439-7633 |
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https://hdl.handle.net/10495/41664 |
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eng |
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eng |
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ChemBioChem |
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10 |
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1 |
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23 |
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ChemBioChem |
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Agudelo Gómez, SantiagoRojas Valencia, Natalia AndreaRestrepo Cossio, Albeiro AlonsoGómez, SaraCappelli, ChiaraGrupo de Química-Física Teórica2024-09-02T11:59:57Z2024-09-02T11:59:57Z2022Gómez SA, Rojas-Valencia N, Gómez S, Cappelli C, Restrepo A. The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction Perspective. Chembiochem. 2022 Apr 5;23(7):e202100393. doi: 10.1002/cbic.2021003931439-4227https://hdl.handle.net/10495/4166410.1002/cbic.2021003931439-7633ABSTRACT: Specific S477N, N501Y, K417N, K417T, E484K mutations in the receptor binding domain (RBD) of the spike protein in the wild type SARS-COV-2 virus have resulted, among others, in the following variants: B.1.160 (20A or EU2, first reported in continental Europe), B1.1.7 (α or 20I501Y.V1, first reported in the United Kingdom), B.1.351 (β or 20H/501Y.V2, first reported in South Africa), B.1.1.28.1 (γ or P.1 or 20J/501Y.V3, first reported in Brazil), and B.1.1.28.2 (ζ, or P.2 or 20B/S484K, also first reported in Brazil). From the analysis of a set of bonding descriptors firmly rooted in the formalism of quantum mechanics, including Natural Bond Orbitals (NBO), Quantum Theory of Atoms In Molecules (QTAIM) and highly correlated energies within the Domain Based Local Pair Natural Orbital Coupled Cluster Method (DLPNO-CCSD(T)), and from a set of compute electronic spectral patterns with environmental effects, we show that the new variants improve their ability to recognize available sites to either hydrogen bond or to form salt bridges with residues in the ACE2 receptor of the host cells. This results in significantly improved initial virus···cell molecular recognition and attachment at the microscopic level, which trigger the infectious cycle.COL000439910 páginasapplication/pdfengWileyGesellschaft Deutscher Chemikerhttps://creativecommons.org/licenses/by-nc-nd/4.0/http://creativecommons.org/licenses/by-nc-nd/2.5/co/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2The Role of Spike Protein Mutations in the Infectious Power of SARS-COV-2 Variants: A Molecular Interaction PerspectiveArtículo de investigaciónhttp://purl.org/coar/resource_type/c_2df8fbb1https://purl.org/redcol/resource_type/ARThttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionCOVID-19MutaciónMutationUnión Proteica - genéticaProtein Binding - geneticsSARS-CoV-2 - genéticaSARS-CoV-2 - geneticsGlicoproteína de la Espiga del CoronavirusSpike Glycoprotein, Coronavirus - chemistry - químicahttps://id.nlm.nih.gov/mesh/D000086382https://id.nlm.nih.gov/mesh/D009154https://id.nlm.nih.gov/mesh/D011485https://id.nlm.nih.gov/mesh/D000086402https://id.nlm.nih.gov/mesh/D064370ChemBioChem107123ChemBioChemPublicationCC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; 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