Epistasis leads to the reduction in genetic barrier to COVID-19 neutralizing antibody escape biorxivpreprint RockefellerUniv SARSCoV2 COVID19 Coronavirus AntibodyEscape Epistasis
By Dr. Priyom Bose, Ph.D.Aug 23 2022Reviewed by Aimee Molineux Severe acute respiratory syndrome coronavirus-2 , the causal agent of the ongoing coronavirus disease 2019 pandemic, has undergone genomic mutations, which have led to the emergence of new variants.
RBD-specific antibodies generated via COVID-19 vaccination or natural infection are grouped into four prototype classes. Two types of antibodies, belonging to classes 1 and 2, bind epitopes overlapping the ACE-2 binding site. Class 3 and 4 antibodies bind outside the ACE-2-binding site on the opposite side of the RBD.
A total of 40 antibodies were isolated from the memory B-cells of multiple volunteer cohorts, and each participant was exposed to SARS-CoV-2 to varying degrees. Antibodies were isolated from participants who received one or two doses of mRNA-based COVID-19 vaccine and were previously infected with ancestral Wuhan-Hu-1 RBD. Neutralizing antibodies were also isolated from individuals who received three doses of mRNA vaccines and had no history of COVID-19.
Related StoriesTwenty-three substitutions were selected, and using them, spike plasmids were constructed. Infection was quantified based on the uninhibited virus, while a 5-fold increase in infection defined antibody escape compared to the antibody-inhibited parental pseudotype. Most of the substitutions were related to resistance to one or more antibodies of the same class. Importantly, some class 4 antibodies were found to be less effective against BA.2.
Based on mutations selected in vitro, it was observed that substitutions that altered during the BA.2 to BA.5 transition were responsible for the resistance of multiple classes of antibodies. Importantly, 7 of the 14 antibodies exhibited resistance to L452 or F486 substitutions.
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