Author(s): 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]
Date: 2022
Persistent ID: http://hdl.handle.net/11449/233558
Origin: Oasisbr
Subject(s): Human ACE2; New variants; Receptor binding domain; SARS-CoV-2; Spike protein
Made available in DSpace on 2022-05-01T09:30:34Z (GMT). No. of bitstreams: 0 Previous issue date: 2021-09-01
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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.
Institute of Chemistry UNESP - São Paulo State University
Institute of Biomedical Sciences Department of Pharmacology University of São Paulo
Department of Morphology School of Medicine Federal University of Ceará
Institute of Bioscience Language and Exact Science UNESP - São Paulo State University São José Do Rio Preto
Institute of Chemistry UNESP - São Paulo State University
Institute of Bioscience Language and Exact Science UNESP - São Paulo State University São José Do Rio Preto
FAPESP: FAPESP 20/05761–3
FAPESP: FAPESP 20/12519–4
