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10.7554/eLife.75433

http://scihub22266oqcxt.onion/10.7554/eLife.75433
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35323111!8963877!35323111
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suck abstract from ncbi


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pmid35323111      Elife 2022 ; 11 (ä): ä
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  • Conformational dynamics and allosteric modulation of the SARS-CoV-2 spike #MMPMID35323111
  • Diaz-Salinas MA; Li Q; Ejemel M; Yurkovetskiy L; Luban J; Shen K; Wang Y; Munro JB
  • Elife 2022[Mar]; 11 (ä): ä PMID35323111show ga
  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infects cells through binding to angiotensin-converting enzyme 2 (ACE2). This interaction is mediated by the receptor-binding domain (RBD) of the viral spike (S) glycoprotein. Structural and dynamic data have shown that S can adopt multiple conformations, which controls the exposure of the ACE2-binding site in the RBD. Here, using single-molecule Forster resonance energy transfer (smFRET) imaging, we report the effects of ACE2 and antibody binding on the conformational dynamics of S from the Wuhan-1 strain and in the presence of the D614G mutation. We find that D614G modulates the energetics of the RBD position in a manner similar to ACE2 binding. We also find that antibodies that target diverse epitopes, including those distal to the RBD, stabilize the RBD in a position competent for ACE2 binding. Parallel solution-based binding experiments using fluorescence correlation spectroscopy (FCS) indicate antibody-mediated enhancement of ACE2 binding. These findings inform on novel strategies for therapeutic antibody cocktails.
  • |*SARS-CoV-2[MESH]
  • |*Spike Glycoprotein, Coronavirus/chemistry[MESH]
  • |Angiotensin-Converting Enzyme 2/chemistry[MESH]
  • |COVID-19[MESH]
  • |Humans[MESH]


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