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10.1016/j.bpj.2021.02.023 http://scihub22266oqcxt.onion/10.1016/j.bpj.2021.02.023 33631204!7899928!33631204     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 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\33631204.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biophys+J 2021 ; 120 (6): 1105-1119 Nephropedia Template TP {{tp|p=33631204|t=2021. Ca(2+)-dependent mechanism of membrane insertion and destabilization by the SARS-CoV-2 fusion peptide |pdf=|usr=}}{{33631204}} gab.com Text Ca(2+)-dependent mechanism of membrane insertion and destabilization by the SARS-CoV-2 fusion peptide JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=33631204 #FOAvip Cell penetration after recognition of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus by the ACE2 receptor and the fusion of its viral envelope membrane with cellular membranes are the early steps of infectivity. A region of the Spike protein of the virus, identified as the "fusion peptide" (FP), is liberated at its N-terminal site by a specific cleavage occurring in concert with the interaction of the receptor-binding domain of the Spike. Studies have shown that penetration is enhanced by the required binding of Ca(2+) ions to the FPs of coronaviruses, but the mechanisms of membrane insertion and destabilization remain unclear. We have predicted the preferred positions of Ca(2+) binding to the SARS-CoV-2-FP, the role of Ca(2+) ions in mediating peptide-membrane interactions, the preferred mode of insertion of the Ca(2+)-bound SARS-CoV-2-FP, and consequent effects on the lipid bilayer from extensive atomistic molecular dynamics simulations and trajectory analyses. In a systematic sampling of the interactions of the Ca(2+)-bound peptide models with lipid membranes, SARS-CoV-2-FP penetrated the bilayer and disrupted its organization only in two modes involving different structural domains. In one, the hydrophobic residues F833/I834 from the middle region of the peptide are inserted. In the other, more prevalent mode, the penetration involves residues L822/F823 from the LLF motif, which is conserved in CoV-2-like viruses, and is achieved by the binding of Ca(2+) ions to the D830/D839 and E819/D820 residue pairs. FP penetration is shown to modify the molecular organization in specific areas of the bilayer, and the extent of membrane binding of the SARS-CoV-2 FP is significantly reduced in the absence of Ca(2+) ions. These findings provide novel mechanistic insights regarding the role of Ca(2+) in mediating SARS-CoV-2 fusion and provide a detailed structural platform to aid the ongoing efforts in rational design of compounds to inhibit SARS-CoV-2 cell entry. Twit Text FOAVip Ca(2+)-dependent mechanism of membrane insertion and destabilization by the SARS-CoV-2 fusion peptide ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=33631204 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33631204 #FOAvip English Wikipedia <ref>{{Cite pmid|33631204}}</ref> Ca(2+)-dependent mechanism of membrane insertion and destabilization by the SARS-CoV-2 fusion peptide #MMPMID33631204 Khelashvili G; Plante A; Doktorova M; Weinstein H Biophys J 2021[Mar]; 120 (6): 1105-1119 PMID33631204show ga Cell penetration after recognition of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus by the ACE2 receptor and the fusion of its viral envelope membrane with cellular membranes are the early steps of infectivity. A region of the Spike protein of the virus, identified as the "fusion peptide" (FP), is liberated at its N-terminal site by a specific cleavage occurring in concert with the interaction of the receptor-binding domain of the Spike. Studies have shown that penetration is enhanced by the required binding of Ca(2+) ions to the FPs of coronaviruses, but the mechanisms of membrane insertion and destabilization remain unclear. We have predicted the preferred positions of Ca(2+) binding to the SARS-CoV-2-FP, the role of Ca(2+) ions in mediating peptide-membrane interactions, the preferred mode of insertion of the Ca(2+)-bound SARS-CoV-2-FP, and consequent effects on the lipid bilayer from extensive atomistic molecular dynamics simulations and trajectory analyses. In a systematic sampling of the interactions of the Ca(2+)-bound peptide models with lipid membranes, SARS-CoV-2-FP penetrated the bilayer and disrupted its organization only in two modes involving different structural domains. In one, the hydrophobic residues F833/I834 from the middle region of the peptide are inserted. In the other, more prevalent mode, the penetration involves residues L822/F823 from the LLF motif, which is conserved in CoV-2-like viruses, and is achieved by the binding of Ca(2+) ions to the D830/D839 and E819/D820 residue pairs. FP penetration is shown to modify the molecular organization in specific areas of the bilayer, and the extent of membrane binding of the SARS-CoV-2 FP is significantly reduced in the absence of Ca(2+) ions. These findings provide novel mechanistic insights regarding the role of Ca(2+) in mediating SARS-CoV-2 fusion and provide a detailed structural platform to aid the ongoing efforts in rational design of compounds to inhibit SARS-CoV-2 cell entry. |Amino Acid Sequence[MESH] |Calcium/*metabolism[MESH] |Cell Membrane Permeability[MESH] |Cell Membrane/*metabolism[MESH] |Membrane Lipids/chemistry[MESH] |Molecular Dynamics Simulation[MESH] |Pressure[MESH] |Probability[MESH] |Protein Stability[MESH] |Recombinant Fusion Proteins/chemistry/*metabolism[MESH] |SARS-CoV-2/*metabolism[MESH]Ca(2+)-dependent mechanism of membrane insertion and destabilization b(epmc).pdf DeepDyve Pubget Overpricing