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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)

dc.contributor.authorSanches, Paulo R.S. [UNESP]
dc.contributor.authorCharlie-Silva, Ives
dc.contributor.authorBraz, Helyson L.B.
dc.contributor.authorBittar, Cíntia [UNESP]
dc.contributor.authorFreitas Calmon, Marilia [UNESP]
dc.contributor.authorRahal, Paula [UNESP]
dc.contributor.authorCilli, Eduardo M. [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionFederal University of Ceará
dc.date.accessioned2022-05-01T09:30:34Z
dc.date.available2022-05-01T09:30:34Z
dc.date.issued2021-09-01
dc.description.abstractNew 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.en
dc.description.affiliationInstitute of Chemistry UNESP - São Paulo State University
dc.description.affiliationInstitute of Biomedical Sciences Department of Pharmacology University of São Paulo
dc.description.affiliationDepartment of Morphology School of Medicine Federal University of Ceará
dc.description.affiliationInstitute of Bioscience Language and Exact Science UNESP - São Paulo State University São José Do Rio Preto
dc.description.affiliationUnespInstitute of Chemistry UNESP - São Paulo State University
dc.description.affiliationUnespInstitute of Bioscience Language and Exact Science UNESP - São Paulo State University São José Do Rio Preto
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdFAPESP: FAPESP 20/05761–3
dc.description.sponsorshipIdFAPESP: FAPESP 20/12519–4
dc.identifierhttp://dx.doi.org/10.1016/j.jve.2021.100054
dc.identifier.citationJournal of Virus Eradication, v. 7, n. 3, 2021.
dc.identifier.doi10.1016/j.jve.2021.100054
dc.identifier.issn2055-6659
dc.identifier.issn2055-6640
dc.identifier.scopus2-s2.0-85115260703
dc.identifier.urihttp://hdl.handle.net/11449/233558
dc.language.isoeng
dc.relation.ispartofJournal of Virus Eradication
dc.sourceScopus
dc.subjectHuman ACE2
dc.subjectNew variants
dc.subjectReceptor binding domain
dc.subjectSARS-CoV-2
dc.subjectSpike protein
dc.titleRecent 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)en
dc.typeArtigopt
dspace.entity.typePublication
relation.isOrgUnitOfPublicationbc74a1ce-4c4c-4dad-8378-83962d76c4fd
relation.isOrgUnitOfPublication.latestForDiscoverybc74a1ce-4c4c-4dad-8378-83962d76c4fd
unesp.author.orcid0000-0003-1996-8831[3]
unesp.author.orcid0000-0001-5203-0103[5]
unesp.author.orcid0000-0002-4767-0904[7]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Química, Araraquarapt
unesp.departmentBiologia - IBILCEpt
unesp.departmentBioquímica e Tecnologia - IQpt

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