To assess the impact of the key non-synonymous amino acid substitutions in the RBD of the spike protein of SARS-CoV-2 variant B.1.617.1(dominant variant identified in the current India outbreak)on the infectivity and ...
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To assess the impact of the key non-synonymous amino acid substitutions in the RBD of the spike protein of SARS-CoV-2 variant B.1.617.1(dominant variant identified in the current India outbreak)on the infectivity and neutralization activities of the immune sera,L452R and e484q(L452R-e484q variant),pseudotyped virus was constructed(with the D614G background).The impact on binding with the neutralizing antibodies was also assessed with an eLISA *** virus carrying a L452R-e484q variant showed a comparable infectivity compared with ***,there was a significant reduction in the neutralization activity of the immune sera from non-human primates vaccinated with a recombinant receptor binding domain(RBD)protein,convalescent patients,and healthy vaccinees vaccinated with anmRNA *** addition,there was a reduction in binding of L452R-e484q-D614G protein to the antibodies of theimmune sera fromvaccinated nonhuman *** results highlight the interplay between infectivity and other biologic factors involved in the natural evolution of *** neutralization activities against the L452R-e484q variant will have an impact on health authority planning and implications for the vaccination strategy/newvaccine development.
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