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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Virus+Res
2020 ; 285
(ä): 198021
Nephropedia Template TP
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English Wikipedia
On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2
spike proteins with monoclonal antibodies and the receptor ACE2
#MMPMID32416259
Corrêa Giron C
; Laaksonen A
; Barroso da Silva FL
Virus Res
2020[Aug]; 285
(ä): 198021
PMID32416259
show ga
A new betacoronavirus named SARS-CoV-2 has emerged as a new threat to global
health and economy. A promising target for both diagnosis and therapeutics
treatments of the new disease named COVID-19 is the coronavirus (CoV) spike (S)
glycoprotein. By constant-pH Monte Carlo simulations and the PROCEEDpKa method,
we have mapped the electrostatic epitopes for four monoclonal antibodies and the
angiotensin-converting enzyme 2 (ACE2) on both SARS-CoV-1 and the new SARS-CoV-2
S receptor binding domain (RBD) proteins. We also calculated free energy of
interactions and shown that the S RBD proteins from both SARS viruses binds to
ACE2 with similar affinities. However, the affinity between the S RBD protein
from the new SARS-CoV-2 and ACE2 is higher than for any studied antibody
previously found complexed with SARS-CoV-1. Based on physical chemical analysis
and free energies estimates, we can shed some light on the involved molecular
recognition processes, their clinical aspects, the implications for drug
developments, and suggest structural modifications on the CR3022 antibody that
would improve its binding affinities for SARS-CoV-2 and contribute to address the
ongoing international health crisis.