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10.1016/j.chom.2020.08.004 http://scihub22266oqcxt.onion/10.1016/j.chom.2020.08.004 32841605!7443692!32841605     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 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 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       Cell+Host+Microbe 2020 ; 28 (4): 586-601.e6 Nephropedia Template TP {{tp|p=32841605|t=2020. Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor |pdf=|usr=}}{{32841605}} gab.com Text Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor JO: Cell Host Microbe http://www.kidney.de/pget.php?&tw=1&pmid=32841605 #FOAvip The SARS-CoV-2 betacoronavirus uses its highly glycosylated trimeric Spike protein to bind to the cell surface receptor angiotensin converting enzyme 2 (ACE2) glycoprotein and facilitate host cell entry. We utilized glycomics-informed glycoproteomics to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2. We combined this information with bioinformatics analyses of natural variants and with existing 3D structures of both glycoproteins to generate molecular dynamics simulations of each glycoprotein both alone and interacting with one another. Our results highlight roles for glycans in sterically masking polypeptide epitopes and directly modulating Spike-ACE2 interactions. Furthermore, our results illustrate the impact of viral evolution and divergence on Spike glycosylation, as well as the influence of natural variants on ACE2 receptor glycosylation. Taken together, these data can facilitate immunogen design to achieve antibody neutralization and inform therapeutic strategies to inhibit viral infection. Twit Text FOAVip Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor ????Cell Host Microbe http://www.kidney.de/pget.php?&tw=1&pmid=32841605 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32841605 #FOAvip English Wikipedia <ref>{{Cite pmid|32841605}}</ref> Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor #MMPMID32841605 Zhao P; Praissman JL; Grant OC; Cai Y; Xiao T; Rosenbalm KE; Aoki K; Kellman BP; Bridger R; Barouch DH; Brindley MA; Lewis NE; Tiemeyer M; Chen B; Woods RJ; Wells L Cell Host Microbe 2020[Oct]; 28 (4): 586-601.e6 PMID32841605show ga The SARS-CoV-2 betacoronavirus uses its highly glycosylated trimeric Spike protein to bind to the cell surface receptor angiotensin converting enzyme 2 (ACE2) glycoprotein and facilitate host cell entry. We utilized glycomics-informed glycoproteomics to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2. We combined this information with bioinformatics analyses of natural variants and with existing 3D structures of both glycoproteins to generate molecular dynamics simulations of each glycoprotein both alone and interacting with one another. Our results highlight roles for glycans in sterically masking polypeptide epitopes and directly modulating Spike-ACE2 interactions. Furthermore, our results illustrate the impact of viral evolution and divergence on Spike glycosylation, as well as the influence of natural variants on ACE2 receptor glycosylation. Taken together, these data can facilitate immunogen design to achieve antibody neutralization and inform therapeutic strategies to inhibit viral infection. |Angiotensin-Converting Enzyme 2[MESH] |Betacoronavirus/*metabolism[MESH] |COVID-19[MESH] |Coronavirus Infections/*enzymology/*virology[MESH] |Glycosylation[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Molecular Dynamics Simulation[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/chemistry/*metabolism[MESH] |Pneumonia, Viral/*enzymology/*virology[MESH] |Protein Domains[MESH] |Protein Interaction Domains and Motifs[MESH] |Receptors, Virus/chemistry/metabolism[MESH] |SARS-CoV-2[MESH] |Spike Glycoprotein, Coronavirus/chemistry/*metabolism[MESH]Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human(epmc).pdf DeepDyve Pubget Overpricing