Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India)
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
DOI: | 10.1016/j.jve.2021.100054 |
Texto Completo: | http://dx.doi.org/10.1016/j.jve.2021.100054 http://hdl.handle.net/11449/233558 |
Resumo: | New variants of SARS-CoV-2 Alpha (B.1.1.7); Beta (B.1.351) Gamma (P.1) and Delta (B.1.617.2) quickly spread in the UK, South Africa, Brazil and India, respectively. To address whether mutations in SARS-CoV-2 RBD spike protein could affect virus infectivity, peptides containing RBD amino acids mutations have been constructed and interacted with human ACE2 by computational methods. Our results suggest that mutations in RBD amino acids K417, E484, L452, T478 and N501 are expressively increasing the affinity of this protein with human angiotensin-converting enzyme 2 (ACE2), consequently, variants Alpha (B.1.1.7), Beta (B1.351), Gamma (P.1) and Delta (B.1.617.2) could be more infective in human cells compared with SARS-CoV-2 isolated in Wuhan-2019 and the Gamma and Delta variants could be the most infective among them. |
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Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India)Human ACE2New variantsReceptor binding domainSARS-CoV-2Spike proteinNew variants of SARS-CoV-2 Alpha (B.1.1.7); Beta (B.1.351) Gamma (P.1) and Delta (B.1.617.2) quickly spread in the UK, South Africa, Brazil and India, respectively. To address whether mutations in SARS-CoV-2 RBD spike protein could affect virus infectivity, peptides containing RBD amino acids mutations have been constructed and interacted with human ACE2 by computational methods. Our results suggest that mutations in RBD amino acids K417, E484, L452, T478 and N501 are expressively increasing the affinity of this protein with human angiotensin-converting enzyme 2 (ACE2), consequently, variants Alpha (B.1.1.7), Beta (B1.351), Gamma (P.1) and Delta (B.1.617.2) could be more infective in human cells compared with SARS-CoV-2 isolated in Wuhan-2019 and the Gamma and Delta variants could be the most infective among them.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Institute of Chemistry UNESP - São Paulo State UniversityInstitute of Biomedical Sciences Department of Pharmacology University of São PauloDepartment of Morphology School of Medicine Federal University of CearáInstitute of Bioscience Language and Exact Science UNESP - São Paulo State University São José Do Rio PretoInstitute of Chemistry UNESP - São Paulo State UniversityInstitute of Bioscience Language and Exact Science UNESP - São Paulo State University São José Do Rio PretoFAPESP: FAPESP 20/05761–3FAPESP: FAPESP 20/12519–4Universidade Estadual Paulista (UNESP)Universidade de São Paulo (USP)Federal University of CearáSanches, Paulo R.S. [UNESP]Charlie-Silva, IvesBraz, Helyson L.B.Bittar, Cíntia [UNESP]Freitas Calmon, Marilia [UNESP]Rahal, Paula [UNESP]Cilli, Eduardo M. [UNESP]2022-05-01T09:30:34Z2022-05-01T09:30:34Z2021-09-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.jve.2021.100054Journal of Virus Eradication, v. 7, n. 3, 2021.2055-66592055-6640http://hdl.handle.net/11449/23355810.1016/j.jve.2021.1000542-s2.0-85115260703Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Virus Eradicationinfo:eu-repo/semantics/openAccess2022-05-01T09:30:34Zoai:repositorio.unesp.br:11449/233558Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T16:28:32.831604Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India) |
title |
Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India) |
spellingShingle |
Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India) Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India) Sanches, Paulo R.S. [UNESP] Human ACE2 New variants Receptor binding domain SARS-CoV-2 Spike protein Sanches, Paulo R.S. [UNESP] Human ACE2 New variants Receptor binding domain SARS-CoV-2 Spike protein |
title_short |
Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India) |
title_full |
Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India) |
title_fullStr |
Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India) Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India) |
title_full_unstemmed |
Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India) Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India) |
title_sort |
Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India) |
author |
Sanches, Paulo R.S. [UNESP] |
author_facet |
Sanches, Paulo R.S. [UNESP] Sanches, Paulo R.S. [UNESP] Charlie-Silva, Ives Braz, Helyson L.B. Bittar, Cíntia [UNESP] Freitas Calmon, Marilia [UNESP] Rahal, Paula [UNESP] Cilli, Eduardo M. [UNESP] Charlie-Silva, Ives Braz, Helyson L.B. Bittar, Cíntia [UNESP] Freitas Calmon, Marilia [UNESP] Rahal, Paula [UNESP] Cilli, Eduardo M. [UNESP] |
author_role |
author |
author2 |
Charlie-Silva, Ives Braz, Helyson L.B. Bittar, Cíntia [UNESP] Freitas Calmon, Marilia [UNESP] Rahal, Paula [UNESP] Cilli, Eduardo M. [UNESP] |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (UNESP) Universidade de São Paulo (USP) Federal University of Ceará |
dc.contributor.author.fl_str_mv |
Sanches, Paulo R.S. [UNESP] Charlie-Silva, Ives Braz, Helyson L.B. Bittar, Cíntia [UNESP] Freitas Calmon, Marilia [UNESP] Rahal, Paula [UNESP] Cilli, Eduardo M. [UNESP] |
dc.subject.por.fl_str_mv |
Human ACE2 New variants Receptor binding domain SARS-CoV-2 Spike protein |
topic |
Human ACE2 New variants Receptor binding domain SARS-CoV-2 Spike protein |
description |
New variants of SARS-CoV-2 Alpha (B.1.1.7); Beta (B.1.351) Gamma (P.1) and Delta (B.1.617.2) quickly spread in the UK, South Africa, Brazil and India, respectively. To address whether mutations in SARS-CoV-2 RBD spike protein could affect virus infectivity, peptides containing RBD amino acids mutations have been constructed and interacted with human ACE2 by computational methods. Our results suggest that mutations in RBD amino acids K417, E484, L452, T478 and N501 are expressively increasing the affinity of this protein with human angiotensin-converting enzyme 2 (ACE2), consequently, variants Alpha (B.1.1.7), Beta (B1.351), Gamma (P.1) and Delta (B.1.617.2) could be more infective in human cells compared with SARS-CoV-2 isolated in Wuhan-2019 and the Gamma and Delta variants could be the most infective among them. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-09-01 2022-05-01T09:30:34Z 2022-05-01T09:30:34Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.jve.2021.100054 Journal of Virus Eradication, v. 7, n. 3, 2021. 2055-6659 2055-6640 http://hdl.handle.net/11449/233558 10.1016/j.jve.2021.100054 2-s2.0-85115260703 |
url |
http://dx.doi.org/10.1016/j.jve.2021.100054 http://hdl.handle.net/11449/233558 |
identifier_str_mv |
Journal of Virus Eradication, v. 7, n. 3, 2021. 2055-6659 2055-6640 10.1016/j.jve.2021.100054 2-s2.0-85115260703 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of Virus Eradication |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1822182508609929216 |
dc.identifier.doi.none.fl_str_mv |
10.1016/j.jve.2021.100054 |