By Dr. Priyom Bose, Ph.D.Sep 30 2022Reviewed by Aimee Molineux The ongoing coronavirus disease 2019 pandemic, caused by the severe acute respiratory syndrome coronavirus 2 , has claimed more than 6.5 million lives worldwide. Due to genomic mutations, several SARS-CoV-2 variants have emerged, categorized as variants of concern and variants of interest . The B.1.1.529 variant, along with its subvariants , have become the dominantly circulating strain worldwide.
Monoclonal antibodies are used for treating children with the respiratory syncytial virus. Additionally, animal models have exhibited efficacy in neutralizing mAbs against many viral infections, such as HIV-1, Lassa, Ebola, and SARS. During the COVID-19 pandemic, several immunotherapeutic reagents, such as Etesevimab, Bamlanivimab, and Sotrovimab, based on mAbs were formulated. However, reduced efficacy of mAb was reported against the Omicron variant.
About the study The construction of a potent ACE2-based immunoadhesin that remained effective against the original SARS-CoV-2 strain and VOCs was demonstrated in this study. The long helical segment of ACE2 at the N-terminus formed the most potential receptor binding domain recognition site. Based on multiple sequence alignments of over 200 ACE2 sequences, scientists detected several regions comprising the SARS-CoV-2 recognition site, which are not conserved.
Enzymatic activity of ACE2-Fc and ACE2mod-Fc were assessed. These two immunoadhesins were immobilized on a plasmon resonance sensor chip and their binding affinities were determined using purified SARS-CoV-2 RBD.
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