Effect of natural mutations of SARS-CoV-2 on spike structure, conformation and antigenicity.

bioRxiv : the preprint server for biology(2021)

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摘要
Cryo-EM structures reveal changes in SARS-CoV-2 S protein during inter-species transmission or immune evasion.Adaptation to mink resulted in increased ACE2 binding and spike destabilization.B.1.1.7 S mutations reveal an intricate balance of stabilizing and destabilizing effects that impact receptor and antibody binding.E484K mutation in B.1.351 and B.1.1.28 S proteins drives immune evasion by altering RBD conformation.S protein uses different mechanisms to converge upon similar solutions for altering RBD up/down positioning.
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关键词
spike structure,natural mutations,sars-cov
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