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10.1038/s41467-021-25903-x http://scihub22266oqcxt.onion/10.1038/s41467-021-25903-x 34580297!8476561!34580297     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\34580297.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Commun 2021 ; 12 (1): 5654 Nephropedia Template TP {{tp|p=34580297|t=2021. Characterization and structural basis of a lethal mouse-adapted SARS-CoV-2 |pdf=|usr=}}{{34580297}} gab.com Text Characterization and structural basis of a lethal mouse-adapted SARS-CoV-2 JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=34580297 #FOAvip There is an urgent need for animal models to study SARS-CoV-2 pathogenicity. Here, we generate and characterize a novel mouse-adapted SARS-CoV-2 strain, MASCp36, that causes severe respiratory symptoms, and mortality. Our model exhibits age- and gender-related mortality akin to severe COVID-19. Deep sequencing identified three amino acid substitutions, N501Y, Q493H, and K417N, at the receptor binding domain (RBD) of MASCp36, during in vivo passaging. All three RBD mutations significantly enhance binding affinity to its endogenous receptor, ACE2. Cryo-electron microscopy analysis of human ACE2 (hACE2), or mouse ACE2 (mACE2), in complex with the RBD of MASCp36, at 3.1 to 3.7 A resolution, reveals the molecular basis for the receptor-binding switch. N501Y and Q493H enhance the binding affinity to hACE2, whereas triple mutations at N501Y/Q493H/K417N decrease affinity and reduce infectivity of MASCp36. Our study provides a platform for studying SARS-CoV-2 pathogenesis, and unveils the molecular mechanism for its rapid adaptation and evolution. Twit Text FOAVip Characterization and structural basis of a lethal mouse-adapted SARS-CoV-2 ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=34580297 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34580297 #FOAvip English Wikipedia <ref>{{Cite pmid|34580297}}</ref> Characterization and structural basis of a lethal mouse-adapted SARS-CoV-2 #MMPMID34580297 Sun S; Gu H; Cao L; Chen Q; Ye Q; Yang G; Li RT; Fan H; Deng YQ; Song X; Qi Y; Li M; Lan J; Feng R; Guo Y; Zhu N; Qin S; Wang L; Zhang YF; Zhou C; Zhao L; Chen Y; Shen M; Cui Y; Yang X; Wang X; Tan W; Wang H; Wang X; Qin CF Nat Commun 2021[Sep]; 12 (1): 5654 PMID34580297show ga There is an urgent need for animal models to study SARS-CoV-2 pathogenicity. Here, we generate and characterize a novel mouse-adapted SARS-CoV-2 strain, MASCp36, that causes severe respiratory symptoms, and mortality. Our model exhibits age- and gender-related mortality akin to severe COVID-19. Deep sequencing identified three amino acid substitutions, N501Y, Q493H, and K417N, at the receptor binding domain (RBD) of MASCp36, during in vivo passaging. All three RBD mutations significantly enhance binding affinity to its endogenous receptor, ACE2. Cryo-electron microscopy analysis of human ACE2 (hACE2), or mouse ACE2 (mACE2), in complex with the RBD of MASCp36, at 3.1 to 3.7 A resolution, reveals the molecular basis for the receptor-binding switch. N501Y and Q493H enhance the binding affinity to hACE2, whereas triple mutations at N501Y/Q493H/K417N decrease affinity and reduce infectivity of MASCp36. Our study provides a platform for studying SARS-CoV-2 pathogenesis, and unveils the molecular mechanism for its rapid adaptation and evolution. |Amino Acid Substitution[MESH] |Angiotensin-Converting Enzyme 2/metabolism[MESH] |Animals[MESH] |Binding Sites/genetics[MESH] |COVID-19/*diagnosis/mortality/virology[MESH] |Disease Models, Animal[MESH] |Female[MESH] |Humans[MESH] |Male[MESH] |Mice[MESH] |Protein Binding/genetics[MESH] |Protein Domains/genetics[MESH] |SARS-CoV-2/genetics/*pathogenicity[MESH] |Severity of Illness Index[MESH]Characterization and structural basis of a lethal mouse-adapted SARS-C(epmc).pdf DeepDyve Pubget Overpricing