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10.1128/mbio.03227-21

http://scihub22266oqcxt.onion/10.1128/mbio.03227-21
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35164561!8844933!35164561
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suck abstract from ncbi


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pmid35164561      mBio 2021 ; 13 (1): e0322721
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  • SARS-CoV-2 Variants Increase Kinetic Stability of Open Spike Conformations as an Evolutionary Strategy #MMPMID35164561
  • Yang Z; Han Y; Ding S; Shi W; Zhou T; Finzi A; Kwong PD; Mothes W; Lu M
  • mBio 2021[Feb]; 13 (1): e0322721 PMID35164561show ga
  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) harbor mutations in the spike (S) glycoprotein that confer more efficient transmission and dampen the efficacy of COVID-19 vaccines and antibody therapies. S mediates virus entry and is the primary target for antibody responses, with structural studies of soluble S variants revealing an increased propensity toward conformations accessible to the human angiotensin-converting enzyme 2 (hACE2) receptor. However, real-time observations of conformational dynamics that govern the structural equilibriums of the S variants have been lacking. Here, we report single-molecule Forster resonance energy transfer (smFRET) studies of critical mutations observed in VOCs, including D614G and E484K, in the context of virus particles. Investigated variants predominately occupied more open hACE2-accessible conformations, agreeing with previous structures of soluble trimers. Additionally, these S variants exhibited slower transitions in hACE2-accessible/bound states. Our finding of increased S kinetic stability in the open conformation provides a new perspective on SARS-CoV-2 adaptation to the human population. IMPORTANCE SARS-CoV-2 surface S glycoprotein-the target of antibodies and vaccines-is responsible for binding to the cellular receptor hACE2. The interactions between S and hACE2 trigger structural rearrangements of S from closed to open conformations prerequisite for virus entry. Under the selection pressure imposed by adaptation to the human host and increasing vaccinations and convalescent patients, SARS-CoV-2 is evolving and has adopted numerous mutations on S variants. These promote virus spreading and immune evasion, partially by increasing the propensity of S to adopt receptor-binding competent open conformations. Here, we determined a time dimension, using smFRET to delineate the temporal prevalence of distinct structures of S in the context of virus particles. We present the first experimental evidence of decelerated transition dynamics from the open state, revealing increased stability of S open conformations to be part of the SARS-CoV-2 adaption strategies.
  • |*COVID-19[MESH]
  • |*SARS-CoV-2/genetics[MESH]
  • |Biological Evolution[MESH]
  • |COVID-19 Vaccines[MESH]
  • |Humans[MESH]
  • |Protein Binding[MESH]
  • |Protein Conformation[MESH]
  • |Receptors, Virus/metabolism[MESH]


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