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10.1126/science.abi6226 http://scihub22266oqcxt.onion/10.1126/science.abi6226 34168071!8611377!34168071     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       Science 2021 ; 373 (6555): ä Nephropedia Template TP {{tp|p=34168071|t=2021. Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity |pdf=|usr=}}{{34168071}} gab.com Text Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=34168071 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants with multiple spike mutations enable increased transmission and antibody resistance. We combined cryo-electron microscopy (cryo-EM), binding, and computational analyses to study variant spikes, including one that was involved in transmission between minks and humans, and others that originated and spread in human populations. All variants showed increased angiotensin-converting enzyme 2 (ACE2) receptor binding and increased propensity for receptor binding domain (RBD)-up states. While adaptation to mink resulted in spike destabilization, the B.1.1.7 (UK) spike balanced stabilizing and destabilizing mutations. A local destabilizing effect of the RBD E484K mutation was implicated in resistance of the B.1.1.28/P.1 (Brazil) and B.1.351 (South Africa) variants to neutralizing antibodies. Our studies revealed allosteric effects of mutations and mechanistic differences that drive either interspecies transmission or escape from antibody neutralization. Twit Text FOAVip Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity ????Science http://www.kidney.de/pget.php?&tw=1&pmid=34168071 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34168071 #FOAvip English Wikipedia <ref>{{Cite pmid|34168071}}</ref> Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity #MMPMID34168071 Gobeil SM; Janowska K; McDowell S; Mansouri K; Parks R; Stalls V; Kopp MF; Manne K; Li D; Wiehe K; Saunders KO; Edwards RJ; Korber B; Haynes BF; Henderson R; Acharya P Science 2021[Aug]; 373 (6555): ä PMID34168071show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants with multiple spike mutations enable increased transmission and antibody resistance. We combined cryo-electron microscopy (cryo-EM), binding, and computational analyses to study variant spikes, including one that was involved in transmission between minks and humans, and others that originated and spread in human populations. All variants showed increased angiotensin-converting enzyme 2 (ACE2) receptor binding and increased propensity for receptor binding domain (RBD)-up states. While adaptation to mink resulted in spike destabilization, the B.1.1.7 (UK) spike balanced stabilizing and destabilizing mutations. A local destabilizing effect of the RBD E484K mutation was implicated in resistance of the B.1.1.28/P.1 (Brazil) and B.1.351 (South Africa) variants to neutralizing antibodies. Our studies revealed allosteric effects of mutations and mechanistic differences that drive either interspecies transmission or escape from antibody neutralization. |Amino Acid Substitution[MESH] |Angiotensin-Converting Enzyme 2/metabolism[MESH] |Animals[MESH] |Antibodies, Neutralizing/immunology[MESH] |Antibodies, Viral/immunology[MESH] |Antigens, Viral/immunology[MESH] |COVID-19/transmission/veterinary/virology[MESH] |Cryoelectron Microscopy[MESH] |Host Adaptation[MESH] |Humans[MESH] |Immune Evasion[MESH] |Mink/virology[MESH] |Models, Molecular[MESH] |Mutation[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Interaction Domains and Motifs[MESH] |Protein Structure, Quaternary[MESH] |Protein Subunits/chemistry[MESH] |Receptors, Coronavirus/metabolism[MESH] |SARS-CoV-2/*chemistry/*genetics/immunology[MESH]Effect of natural mutations of SARS-CoV-2 on spike structure, conforma(epmc).pdf DeepDyve Pubget Overpricing