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10.1038/s41422-021-00558-x http://scihub22266oqcxt.onion/10.1038/s41422-021-00558-x 34465913!8406658!34465913     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\34465913.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Res 2021 ; 31 (10): 1047-1060 Nephropedia Template TP {{tp|p=34465913|t=2021. Mechanical activation of spike fosters SARS-CoV-2 viral infection |pdf=|usr=}}{{34465913}} gab.com Text Mechanical activation of spike fosters SARS-CoV-2 viral infection JO: Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=34465913 #FOAvip The outbreak of SARS-CoV-2 (SARS2) has caused a global COVID-19 pandemic. The spike protein of SARS2 (SARS2-S) recognizes host receptors, including ACE2, to initiate viral entry in a complex biomechanical environment. Here, we reveal that tensile force, generated by bending of the host cell membrane, strengthens spike recognition of ACE2 and accelerates the detachment of spike's S1 subunit from the S2 subunit to rapidly prime the viral fusion machinery. Mechanistically, such mechano-activation is fulfilled by force-induced opening and rotation of spike's receptor-binding domain to prolong the bond lifetime of spike/ACE2 binding, up to 4 times longer than that of SARS-S binding with ACE2 under 10 pN force application, and subsequently by force-accelerated S1/S2 detachment which is up to ~10(3) times faster than that in the no-force condition. Interestingly, the SARS2-S D614G mutant, a more infectious variant, shows 3-time stronger force-dependent ACE2 binding and 35-time faster force-induced S1/S2 detachment. We also reveal that an anti-S1/S2 non-RBD-blocking antibody that was derived from convalescent COVID-19 patients with potent neutralizing capability can reduce S1/S2 detachment by 3 x 10(6) times under force. Our study sheds light on the mechano-chemistry of spike activation and on developing a non-RBD-blocking but S1/S2-locking therapeutic strategy to prevent SARS2 invasion. Twit Text FOAVip Mechanical activation of spike fosters SARS-CoV-2 viral infection ????Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=34465913 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34465913 #FOAvip English Wikipedia <ref>{{Cite pmid|34465913}}</ref> Mechanical activation of spike fosters SARS-CoV-2 viral infection #MMPMID34465913 Hu W; Zhang Y; Fei P; Zhang T; Yao D; Gao Y; Liu J; Chen H; Lu Q; Mudianto T; Zhang X; Xiao C; Ye Y; Sun Q; Zhang J; Xie Q; Wang PH; Wang J; Li Z; Lou J; Chen W Cell Res 2021[Oct]; 31 (10): 1047-1060 PMID34465913show ga The outbreak of SARS-CoV-2 (SARS2) has caused a global COVID-19 pandemic. The spike protein of SARS2 (SARS2-S) recognizes host receptors, including ACE2, to initiate viral entry in a complex biomechanical environment. Here, we reveal that tensile force, generated by bending of the host cell membrane, strengthens spike recognition of ACE2 and accelerates the detachment of spike's S1 subunit from the S2 subunit to rapidly prime the viral fusion machinery. Mechanistically, such mechano-activation is fulfilled by force-induced opening and rotation of spike's receptor-binding domain to prolong the bond lifetime of spike/ACE2 binding, up to 4 times longer than that of SARS-S binding with ACE2 under 10 pN force application, and subsequently by force-accelerated S1/S2 detachment which is up to ~10(3) times faster than that in the no-force condition. Interestingly, the SARS2-S D614G mutant, a more infectious variant, shows 3-time stronger force-dependent ACE2 binding and 35-time faster force-induced S1/S2 detachment. We also reveal that an anti-S1/S2 non-RBD-blocking antibody that was derived from convalescent COVID-19 patients with potent neutralizing capability can reduce S1/S2 detachment by 3 x 10(6) times under force. Our study sheds light on the mechano-chemistry of spike activation and on developing a non-RBD-blocking but S1/S2-locking therapeutic strategy to prevent SARS2 invasion. |*Tensile Strength[MESH] |Angiotensin-Converting Enzyme 2/chemistry/metabolism[MESH] |Antibodies, Neutralizing/immunology[MESH] |Binding Sites[MESH] |COVID-19 Serotherapy[MESH] |COVID-19/*diagnosis/therapy/virology[MESH] |Humans[MESH] |Hydrogen-Ion Concentration[MESH] |Immunization, Passive[MESH] |Molecular Dynamics Simulation[MESH] |Protein Binding[MESH] |Protein Domains/immunology[MESH] |Protein Subunits/chemistry/immunology/metabolism[MESH] |SARS-CoV-2/isolation & purification/*metabolism[MESH] |Spike Glycoprotein, Coronavirus/chemistry/immunology/*metabolism[MESH]Mechanical activation of spike fosters SARS-CoV-2 viral infection (epmc).pdf DeepDyve Pubget Overpricing