Abstract
The newly emerging SARS-CoV-2 variants are potential threat and posing new challenges for medical intervention due to high transmissibility and escaping neutralizing antibody (NAb) responses. Many of these variants have mutations in the receptor binding domain (RBD) of SARS-CoV-2 spike protein that interacts with the host cell receptor. Rapid mutation in the RBD through natural selection to improve affinity for host receptor and antibody pressure from vaccinated or infected individual will greatly impact the presently adopted strategies for developing interventions. Understanding the nature of mutations and how they impact the biophysical, biochemical and immunological properties of the RBD will help immensely to improve the intervention strategies. To understand the impact of mutation on the protease sensitivity, thermal stability, affinity for the receptor and immune response, we prepared several mutants of soluble RBD that belong to the variants of concern (VoCs) and interest (VoIs) and characterize them. Our results show that the mutations do not impact the overall structure of the RBD. However, the mutants showed increase in the thermal melting point, few mutants were more sensitive to protease degradation, most of them have enhanced affinity for ACE2 and some of them induced better immune response compared to the parental RBD.
Keywords: Affinity; Mutations; RBD; Receptor; SARS-CoV-2; Variants.
【저자키워드】 SARS-CoV-2, mutations, RBD, receptor, variants., affinity, 【초록키워드】 neutralizing antibody, ACE2, immune response, Mutation, antibody, variant, SARS-CoV-2 variant, variants of concern, Intervention, protease, Receptor binding domain, sensitivity, Transmissibility, SARS-CoV-2 spike protein, Rapid, understanding, natural selection, mutant, Degradation, thermal stability, biochemical, host receptor, infected individual, help, host cell receptor, medical intervention, responses, immunological, IMPROVE, interact, adopted, the RBD, increase in, parental, 【제목키워드】 characterization,