Featuring ACE2 binding SARS-CoV and SARS-CoV-2 through a conserved evolutionary pattern of amino acid residues

Author(s)

Carvalho, Patricia P. D. ^[1] ; Alves, Nelson A. ^[1]

Affiliation

^[1] Univ Sao Paulo, Dept Fis, FFCLRP, Ribeirao Preto, SP - Brazil

• Document type: Journal article
• Source: JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS; AUG 2021.
• Web of Science Citations: 0

Abstract

Spike (S) glycoproteins mediate the coronavirus entry into the host cell. The S1 subunit of S-proteins contains the receptor-binding domain (RBD) that is able to recognize different host receptors, highlighting its remarkable capacity to adapt to their hosts along the viral evolution. While RBD in spike proteins is determinant for the virus-receptor interaction, the active residues lie at the receptor-binding motif (RBM), a region located in RBD that plays a fundamental role binding the outer surface of their receptors. Here, we address the hypothesis that SARS-CoV and SARS-CoV-2 strains able to use angiotensin-converting enzyme 2 (ACE2) proteins have adapted their RBM along the viral evolution to explore specific conformational topology driven by the residues YGF to infect host cells. We also speculate that this YGF-based mechanism can act as a protein signature located at the RBM to distinguish coronaviruses able to use ACE2 as a cell entry receptor. Communicated by Ramaswamy H. Sarma (AU)

• FAPESP's process: 15/16116-3 - Molecular mechanisms of electrostatic origin responsible for protein complexation
• Grantee: Fernando Luis Barroso da Silva
• Support Opportunities: Regular Research Grants