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Summary: On November 24, 2021, the sequence of a new SARS-CoV-2 variant, Omicron-B.1.1.529, was announced. Compared to previous variants, Omicron has a higher number of mutations in the Spike (S) protein. Serum neutralization of Omicron by individuals vaccinated or previously infected with Alpha, Beta, Gamma, or Delta variants is significantly reduced or ineffective. Third vaccine doses can boost neutralization titers against Omicron, and high titers are observed in both vaccinated individuals and those infected with the Delta variant. Most potent monoclonal antibodies and antibodies under development are unable to effectively neutralize Omicron due to mutations in its Spike protein. Omicron has structural changes compared to earlier viruses and utilizes mutations that enhance its binding to ACE2, allowing for immune escape. This results in a large number of mutations in the ACE2 binding site and a rebalancing of receptor affinity similar to earlier pandemic viruses.
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Delphine Planas et al.
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Anna-Lena Mader et al.
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Jun Siong Low et al.
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Victoria Stalls et al.
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Pengfei Wang et al.
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Supaporn Wacharapluesadee et al.
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Deborah Delaune et al.
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Renhong Yan et al.
Summary: This study investigated the structural basis for the potent neutralizing activity of nAbs against SARS-CoV-2, finding that the bivalent binding of full-length IgG associates with more RBDs in the up conformation, leading to enhanced neutralization and shedding of the S1 subunit from the S protein. Comparing a large number of nAbs revealed common and unique structural features associated with their potent neutralizing activities.
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Wei Yu et al.
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