Articolo in rivista, 2021, ENG, 10.3390/biomedicines9081038
Deborah Giordano, Luigi De Masi, Maria Antonia Argenio, and Angelo Facchiano
National Research Council (CNR), Institute of Food Sciences (ISA), via Roma 64, 83100 Avellino, Italy National Research Council (CNR), Institute of Biosciences and BioResources (IBBR), via Università 133, 80055 Portici, Italy
An outbreak by a new severe acute respiratory syndrome betacoronavirus (SARS-CoV-2) has spread CoronaVirus Disease 2019 (COVID-19) all over the world. Immediately, following studies have confirmed the human Angiotensin-Converting Enzyme 2 (ACE2) as a cellular receptor of viral Spike-Protein (Sp) that mediates the CoV-2 invasion into the pulmonary host cells. Here, we compared the molecular interactions of the viral Sp from previous SARS-CoV-1 of 2002 and SARS-CoV-2 with the host ACE2 protein by in silico analysis of the available experimental structures of Sp-ACE2 complexes. The K417 amino acid residue, located in the region of Sp Receptor-Binding Domain (RBD) of the new coronavirus SARS-CoV-2, showed to have a key role for the binding to the ACE2 N-terminal region. The R426 residue of SARS-CoV-1 Sp-RBD also plays a key role, although by interacting with the central region of the ACE2 sequence. Therefore, our study evidenced peculiarities in the interactions of the two Sp-ACE2 complexes. Our outcomes were consistent with previously reported mutagenesis studies on SARS-CoV-1 and support the idea that a new and different RBD was acquired by SARS-CoV-2. These results have interesting implications and suggest further investigations
Biomedicines 9 (8)
SARS-CoV-1, SARS-CoV-2, COVID-19, human ACE2, viral spike-protein, Receptor-Binding Domain (RBD), binding interface
Giordano Deborah, Facchiano Angelo, De Masi Luigi
IBBR – Istituto di Bioscienze e Biorisorse, ISA – Istituto di Scienze dell'Alimentazione
ID: 456202
Year: 2021
Type: Articolo in rivista
Creation: 2021-08-31 09:34:07.000
Last update: 2021-09-06 16:54:35.000
External IDs
CNR OAI-PMH: oai:it.cnr:prodotti:456202
DOI: 10.3390/biomedicines9081038
Scopus: 2-s2.0-85113721336
ISI Web of Science (WOS): 000688779600001
PubMed: 34440241