![]() Previously emerged SARS-CoV-2 variants of concern (VOCs) have developed resistance to neutralizing antibodies, including some clinical antibodies that are used as therapeutics 6, 7, 8. The evolution of RNA viruses can result in immune escape and modulation of binding to host receptors through the accumulation of mutations 5. Broadly neutralizing monoclonal antibodies that recognize RBD epitopes that are conserved among SARS-CoV-2 variants and other sarbecoviruses may prove key to controlling the ongoing pandemic and future zoonotic spillovers. The magnitude of Omicron-mediated immune evasion marks a major antigenic shift in SARS-CoV-2. Furthermore, a fraction of broadly neutralizing sarbecovirus monoclonal antibodies neutralized Omicron through recognition of antigenic sites outside the receptor-binding motif, including sotrovimab 2, S2X259 3 and S2H97 4. Most monoclonal antibodies that are directed against the receptor-binding motif lost in vitro neutralizing activity against Omicron, with only 3 out of 29 monoclonal antibodies retaining unaltered potency, including the ACE2-mimicking S2K146 antibody 1. Marked reductions in neutralizing activity were observed against Omicron compared to the ancestral pseudovirus in plasma from convalescent individuals and from individuals who had been vaccinated against SARS-CoV-2, but this loss was less pronounced after a third dose of vaccine. Here we show that the Omicron RBD binds to human ACE2 with enhanced affinity, relative to the Wuhan-Hu-1 RBD, and binds to mouse ACE2. The recently emerged SARS-CoV-2 Omicron variant encodes 37 amino acid substitutions in the spike protein, 15 of which are in the receptor-binding domain (RBD), thereby raising concerns about the effectiveness of available vaccines and antibody-based therapeutics. Nature volume 602, pages 664–670 ( 2022) Cite this article Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift ![]()
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