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10.1126/science.abn7760 http://scihub22266oqcxt.onion/10.1126/science.abn7760 35050643!9799367!35050643     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2022 ; 375 (6582): 760-764 Nephropedia Template TP {{tp|p=35050643|t=2022. SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein-ACE2 complex |pdf=|usr=}}{{35050643}} gab.com Text SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein-ACE2 complex JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=35050643 #FOAvip The newly reported Omicron variant is poised to replace Delta as the most prevalent SARS-CoV-2 variant across the world. Cryo-EM structural analysis of the Omicron variant spike protein in complex with human ACE2 reveals new salt bridges and hydrogen bonds formed by mutated residues R493, S496 and R498 in the RBD with ACE2. These interactions appear to compensate for other Omicron mutations such as K417N known to reduce ACE2 binding affinity, resulting in similar biochemical ACE2 binding affinities for Delta and Omicron variants. Neutralization assays show that pseudoviruses displaying the Omicron spike protein exhibit increased antibody evasion. The increase in antibody evasion, together with retention of strong interactions at the ACE2 interface, thus represent important molecular features that likely contribute to the rapid spread of the Omicron variant. Twit Text FOAVip SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein-ACE2 complex ????Science http://www.kidney.de/pget.php?&tw=1&pmid=35050643 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35050643 #FOAvip English Wikipedia <ref>{{Cite pmid|35050643}}</ref> SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein-ACE2 complex #MMPMID35050643 Mannar D; Saville JW; Zhu X; Srivastava SS; Berezuk AM; Tuttle KS; Marquez AC; Sekirov I; Subramaniam S Science 2022[Feb]; 375 (6582): 760-764 PMID35050643show ga The newly reported Omicron variant is poised to replace Delta as the most prevalent SARS-CoV-2 variant across the world. Cryo-EM structural analysis of the Omicron variant spike protein in complex with human ACE2 reveals new salt bridges and hydrogen bonds formed by mutated residues R493, S496 and R498 in the RBD with ACE2. These interactions appear to compensate for other Omicron mutations such as K417N known to reduce ACE2 binding affinity, resulting in similar biochemical ACE2 binding affinities for Delta and Omicron variants. Neutralization assays show that pseudoviruses displaying the Omicron spike protein exhibit increased antibody evasion. The increase in antibody evasion, together with retention of strong interactions at the ACE2 interface, thus represent important molecular features that likely contribute to the rapid spread of the Omicron variant. |*Immune Evasion[MESH] |Angiotensin-Converting Enzyme 2/*chemistry/metabolism[MESH] |Antibodies, Monoclonal/immunology[MESH] |Antibodies, Neutralizing/immunology[MESH] |Antibodies, Viral/*immunology[MESH] |COVID-19 Vaccines/immunology[MESH] |COVID-19/immunology[MESH] |Cryoelectron Microscopy[MESH] |Humans[MESH] |Hydrogen Bonding[MESH] |Models, Molecular[MESH] |Mutation[MESH] |Neutralization Tests[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Protein Interaction Domains and Motifs[MESH] |Receptors, Coronavirus/*chemistry/metabolism[MESH] |SARS-CoV-2/*chemistry/genetics/*immunology/pathogenicity[MESH]SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of (epmc).pdf DeepDyve Pubget Overpricing