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10.7554/eLife.69091 http://scihub22266oqcxt.onion/10.7554/eLife.69091 34414884!8455130!34414884     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Elife 2021 ; 10 (ä): ä Nephropedia Template TP {{tp|p=34414884|t=2021. N501Y mutation of spike protein in SARS-CoV-2 strengthens its binding to receptor ACE2 |pdf=|usr=}}{{34414884}} gab.com Text N501Y mutation of spike protein in SARS-CoV-2 strengthens its binding to receptor ACE2 JO: Elife http://www.kidney.de/pget.php?&tw=1&pmid=34414884 #FOAvip SARS-CoV-2 has been spreading around the world for the past year. Recently, several variants such as B.1.1.7 (alpha), B.1.351 (beta), and P.1 (gamma), which share a key mutation N501Y on the receptor-binding domain (RBD), appear to be more infectious to humans. To understand the underlying mechanism, we used a cell surface-binding assay, a kinetics study, a single-molecule technique, and a computational method to investigate the interaction between these RBD (mutations) and ACE2. Remarkably, RBD with the N501Y mutation exhibited a considerably stronger interaction, with a faster association rate and a slower dissociation rate. Atomic force microscopy (AFM)-based single-molecule force microscopy (SMFS) consistently quantified the interaction strength of RBD with the mutation as having increased binding probability and requiring increased unbinding force. Molecular dynamics simulations of RBD-ACE2 complexes indicated that the N501Y mutation introduced additional pi-pi and pi-cation interactions that could explain the changes observed by force microscopy. Taken together, these results suggest that the reinforced RBD-ACE2 interaction that results from the N501Y mutation in the RBD should play an essential role in the higher rate of transmission of SARS-CoV-2 variants, and that future mutations in the RBD of the virus should be under surveillance. Twit Text FOAVip N501Y mutation of spike protein in SARS-CoV-2 strengthens its binding to receptor ACE2 ????Elife http://www.kidney.de/pget.php?&tw=1&pmid=34414884 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34414884 #FOAvip English Wikipedia <ref>{{Cite pmid|34414884}}</ref> N501Y mutation of spike protein in SARS-CoV-2 strengthens its binding to receptor ACE2 #MMPMID34414884 Tian F; Tong B; Sun L; Shi S; Zheng B; Wang Z; Dong X; Zheng P Elife 2021[Aug]; 10 (ä): ä PMID34414884show ga SARS-CoV-2 has been spreading around the world for the past year. Recently, several variants such as B.1.1.7 (alpha), B.1.351 (beta), and P.1 (gamma), which share a key mutation N501Y on the receptor-binding domain (RBD), appear to be more infectious to humans. To understand the underlying mechanism, we used a cell surface-binding assay, a kinetics study, a single-molecule technique, and a computational method to investigate the interaction between these RBD (mutations) and ACE2. Remarkably, RBD with the N501Y mutation exhibited a considerably stronger interaction, with a faster association rate and a slower dissociation rate. Atomic force microscopy (AFM)-based single-molecule force microscopy (SMFS) consistently quantified the interaction strength of RBD with the mutation as having increased binding probability and requiring increased unbinding force. Molecular dynamics simulations of RBD-ACE2 complexes indicated that the N501Y mutation introduced additional pi-pi and pi-cation interactions that could explain the changes observed by force microscopy. Taken together, these results suggest that the reinforced RBD-ACE2 interaction that results from the N501Y mutation in the RBD should play an essential role in the higher rate of transmission of SARS-CoV-2 variants, and that future mutations in the RBD of the virus should be under surveillance. |*Mutation[MESH] |Angiotensin-Converting Enzyme 2/*metabolism[MESH] |Binding Sites[MESH] |Cell Line[MESH] |Humans[MESH] |Protein Binding[MESH] |SARS-CoV-2/*genetics/*metabolism[MESH]N501Y mutation of spike protein in SARS-CoV-2 strengthens its binding (epmc).pdf DeepDyve Pubget Overpricing