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)

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.contributorFederal University of Ceará-
Autor(es): dc.creatorSanches, Paulo R.S.-
Autor(es): dc.creatorCharlie-Silva, Ives-
Autor(es): dc.creatorBraz, Helyson L.B.-
Autor(es): dc.creatorBittar, Cíntia-
Autor(es): dc.creatorFreitas Calmon, Marilia-
Autor(es): dc.creatorRahal, Paula-
Autor(es): dc.creatorCilli, Eduardo M.-
Data de aceite: dc.date.accessioned2025-08-21T17:14:29Z-
Data de disponibilização: dc.date.available2025-08-21T17:14:29Z-
Data de envio: dc.date.issued2022-05-01-
Data de envio: dc.date.issued2022-05-01-
Data de envio: dc.date.issued2021-09-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.jve.2021.100054-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/233558-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/233558-
Descrição: dc.descriptionNew 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.-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionInstitute of Chemistry UNESP - São Paulo State University-
Descrição: dc.descriptionInstitute of Biomedical Sciences Department of Pharmacology University of São Paulo-
Descrição: dc.descriptionDepartment of Morphology School of Medicine Federal University of Ceará-
Descrição: dc.descriptionInstitute of Bioscience Language and Exact Science UNESP - São Paulo State University São José Do Rio Preto-
Descrição: dc.descriptionInstitute of Chemistry UNESP - São Paulo State University-
Descrição: dc.descriptionInstitute of Bioscience Language and Exact Science UNESP - São Paulo State University São José Do Rio Preto-
Descrição: dc.descriptionFAPESP: FAPESP 20/05761–3-
Descrição: dc.descriptionFAPESP: FAPESP 20/12519–4-
Idioma: dc.languageen-
Relação: dc.relationJournal of Virus Eradication-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectHuman ACE2-
Palavras-chave: dc.subjectNew variants-
Palavras-chave: dc.subjectReceptor binding domain-
Palavras-chave: dc.subjectSARS-CoV-2-
Palavras-chave: dc.subjectSpike protein-
Título: 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)-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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