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10.1126/science.abd2321 http://scihub22266oqcxt.onion/10.1126/science.abd2321 32661058!7402627!32661058     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32661058&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2020 ; 369 (6507): 1119-1123 Nephropedia Template TP {{tp|p=32661058|t=2020. Structural basis of a shared antibody response to SARS-CoV-2 |pdf=|usr=}}{{32661058}} gab.com Text Structural basis of a shared antibody response to SARS-CoV-2 JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32661058 #FOAvip Molecular understanding of neutralizing antibody responses to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) could accelerate vaccine design and drug discovery. We analyzed 294 anti-SARS-CoV-2 antibodies and found that immunoglobulin G heavy-chain variable region 3-53 (IGHV3-53) is the most frequently used IGHV gene for targeting the receptor-binding domain (RBD) of the spike protein. Co-crystal structures of two IGHV3-53-neutralizing antibodies with RBD, with or without Fab CR3022, at 2.33- to 3.20-angstrom resolution revealed that the germline-encoded residues dominate recognition of the angiotensin I converting enzyme 2 (ACE2)-binding site. This binding mode limits the IGHV3-53 antibodies to short complementarity-determining region H3 loops but accommodates light-chain diversity. These IGHV3-53 antibodies show minimal affinity maturation and high potency, which is promising for vaccine design. Knowledge of these structural motifs and binding mode should facilitate the design of antigens that elicit this type of neutralizing response. Twit Text FOAVip Structural basis of a shared antibody response to SARS-CoV-2 ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32661058 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32661058 #FOAvip English Wikipedia <ref>{{Cite pmid|32661058}}</ref> Structural basis of a shared antibody response to SARS-CoV-2 #MMPMID32661058 Yuan M; Liu H; Wu NC; Lee CD; Zhu X; Zhao F; Huang D; Yu W; Hua Y; Tien H; Rogers TF; Landais E; Sok D; Jardine JG; Burton DR; Wilson IA Science 2020[Aug]; 369 (6507): 1119-1123 PMID32661058show ga Molecular understanding of neutralizing antibody responses to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) could accelerate vaccine design and drug discovery. We analyzed 294 anti-SARS-CoV-2 antibodies and found that immunoglobulin G heavy-chain variable region 3-53 (IGHV3-53) is the most frequently used IGHV gene for targeting the receptor-binding domain (RBD) of the spike protein. Co-crystal structures of two IGHV3-53-neutralizing antibodies with RBD, with or without Fab CR3022, at 2.33- to 3.20-angstrom resolution revealed that the germline-encoded residues dominate recognition of the angiotensin I converting enzyme 2 (ACE2)-binding site. This binding mode limits the IGHV3-53 antibodies to short complementarity-determining region H3 loops but accommodates light-chain diversity. These IGHV3-53 antibodies show minimal affinity maturation and high potency, which is promising for vaccine design. Knowledge of these structural motifs and binding mode should facilitate the design of antigens that elicit this type of neutralizing response. |*Antibody Formation[MESH] |Antibodies, Neutralizing/*chemistry/genetics/immunology[MESH] |Antibodies, Viral/*chemistry/genetics/immunology[MESH] |Betacoronavirus/*immunology[MESH] |Binding Sites[MESH] |COVID-19[MESH] |COVID-19 Vaccines[MESH] |Complementarity Determining Regions/*chemistry/genetics/immunology[MESH] |Coronavirus Infections/genetics/immunology/*prevention & control[MESH] |Crystallography, X-Ray[MESH] |Humans[MESH] |Immunoglobulin Heavy Chains/*chemistry/genetics/immunology[MESH] |Pandemics/*prevention & control[MESH] |Pneumonia, Viral/immunology/*prevention & control[MESH] |Protein Domains[MESH] |SARS-CoV-2[MESH]Structural basis of a shared antibody response to SARS-CoV-2 (epmc).pdf DeepDyve Pubget Overpricing