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10.1016/j.celrep.2022.110786 http://scihub22266oqcxt.onion/10.1016/j.celrep.2022.110786 35477024!9015963!35477024     free     free     free Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Rep 2022 ; 39 (5): 110786 Nephropedia Template TP {{tp|p=35477024|t=2022. Inter-domain communication in SARS-CoV-2 spike proteins controls protease-triggered cell entry |pdf=|usr=}}{{35477024}} gab.com Text Inter-domain communication in SARS-CoV-2 spike proteins controls protease-triggered cell entry JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=35477024 #FOAvip SARS-CoV-2 continues to evolve into variants of concern (VOC), with greatest variability in the multidomain, entry-facilitating spike proteins. To recognize the significance of adaptive spike protein changes, we compare variant SARS-CoV-2 virus particles in several assays reflecting authentic virus-cell entry. Virus particles with adaptive changes in spike amino-terminal domains (NTDs) are hypersensitive to proteolytic activation of membrane fusion, an essential step in virus-cell entry. Proteolysis is within fusion domains (FDs), at sites over 10 nm from the VOC-specific NTD changes, indicating allosteric inter-domain control of fusion activation. In addition, NTD-specific antibodies block FD cleavage, membrane fusion, and virus-cell entry, suggesting restriction of inter-domain communication as a neutralization mechanism. Finally, using structure-guided mutagenesis, we identify an inter-monomer beta sheet structure that facilitates NTD-to-FD transmissions and subsequent fusion activation. This NTD-to-FD axis that sensitizes viruses to infection and to NTD-specific antibody neutralization provides new context for understanding selective forces driving SARS-CoV-2 evolution. Twit Text FOAVip Inter-domain communication in SARS-CoV-2 spike proteins controls protease-triggered cell entry ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=35477024 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35477024 #FOAvip English Wikipedia <ref>{{Cite pmid|35477024}}</ref> Inter-domain communication in SARS-CoV-2 spike proteins controls protease-triggered cell entry #MMPMID35477024 Qing E; Li P; Cooper L; Schulz S; Jack HM; Rong L; Perlman S; Gallagher T Cell Rep 2022[May]; 39 (5): 110786 PMID35477024show ga SARS-CoV-2 continues to evolve into variants of concern (VOC), with greatest variability in the multidomain, entry-facilitating spike proteins. To recognize the significance of adaptive spike protein changes, we compare variant SARS-CoV-2 virus particles in several assays reflecting authentic virus-cell entry. Virus particles with adaptive changes in spike amino-terminal domains (NTDs) are hypersensitive to proteolytic activation of membrane fusion, an essential step in virus-cell entry. Proteolysis is within fusion domains (FDs), at sites over 10 nm from the VOC-specific NTD changes, indicating allosteric inter-domain control of fusion activation. In addition, NTD-specific antibodies block FD cleavage, membrane fusion, and virus-cell entry, suggesting restriction of inter-domain communication as a neutralization mechanism. Finally, using structure-guided mutagenesis, we identify an inter-monomer beta sheet structure that facilitates NTD-to-FD transmissions and subsequent fusion activation. This NTD-to-FD axis that sensitizes viruses to infection and to NTD-specific antibody neutralization provides new context for understanding selective forces driving SARS-CoV-2 evolution. |*COVID-19[MESH] |*Spike Glycoprotein, Coronavirus[MESH] |Communication[MESH] |Humans[MESH] |Peptide Hydrolases[MESH] |SARS-CoV-2[MESH]Inter-domain communication in SARS-CoV-2 spike proteins controls prot(epmc).pdf DeepDyve Pubget Overpricing