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10.1016/j.cell.2021.04.032 http://scihub22266oqcxt.onion/10.1016/j.cell.2021.04.032 34015271!8064835!34015271     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell 2021 ; 184 (12): 3205-3221.e24 Nephropedia Template TP {{tp|p=34015271|t=2021. B cell genomics behind cross-neutralization of SARS-CoV-2 variants and SARS-CoV |pdf=|usr=}}{{34015271}} gab.com Text B cell genomics behind cross-neutralization of SARS-CoV-2 variants and SARS-CoV JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=34015271 #FOAvip Monoclonal antibodies (mAbs) are a focus in vaccine and therapeutic design to counteract severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and its variants. Here, we combined B cell sorting with single-cell VDJ and RNA sequencing (RNA-seq) and mAb structures to characterize B cell responses against SARS-CoV-2. We show that the SARS-CoV-2-specific B cell repertoire consists of transcriptionally distinct B cell populations with cells producing potently neutralizing antibodies (nAbs) localized in two clusters that resemble memory and activated B cells. Cryo-electron microscopy structures of selected nAbs from these two clusters complexed with SARS-CoV-2 spike trimers show recognition of various receptor-binding domain (RBD) epitopes. One of these mAbs, BG10-19, locks the spike trimer in a closed conformation to potently neutralize SARS-CoV-2, the recently arising mutants B.1.1.7 and B.1.351, and SARS-CoV and cross-reacts with heterologous RBDs. Together, our results characterize transcriptional differences among SARS-CoV-2-specific B cells and uncover cross-neutralizing Ab targets that will inform immunogen and therapeutic design against coronaviruses. Twit Text FOAVip B cell genomics behind cross-neutralization of SARS-CoV-2 variants and SARS-CoV ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=34015271 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34015271 #FOAvip English Wikipedia <ref>{{Cite pmid|34015271}}</ref> B cell genomics behind cross-neutralization of SARS-CoV-2 variants and SARS-CoV #MMPMID34015271 Scheid JF; Barnes CO; Eraslan B; Hudak A; Keeffe JR; Cosimi LA; Brown EM; Muecksch F; Weisblum Y; Zhang S; Delorey T; Woolley AE; Ghantous F; Park SM; Phillips D; Tusi B; Huey-Tubman KE; Cohen AA; Gnanapragasam PNP; Rzasa K; Hatziioanno T; Durney MA; Gu X; Tada T; Landau NR; West AP Jr; Rozenblatt-Rosen O; Seaman MS; Baden LR; Graham DB; Deguine J; Bieniasz PD; Regev A; Hung D; Bjorkman PJ; Xavier RJ Cell 2021[Jun]; 184 (12): 3205-3221.e24 PMID34015271show ga Monoclonal antibodies (mAbs) are a focus in vaccine and therapeutic design to counteract severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and its variants. Here, we combined B cell sorting with single-cell VDJ and RNA sequencing (RNA-seq) and mAb structures to characterize B cell responses against SARS-CoV-2. We show that the SARS-CoV-2-specific B cell repertoire consists of transcriptionally distinct B cell populations with cells producing potently neutralizing antibodies (nAbs) localized in two clusters that resemble memory and activated B cells. Cryo-electron microscopy structures of selected nAbs from these two clusters complexed with SARS-CoV-2 spike trimers show recognition of various receptor-binding domain (RBD) epitopes. One of these mAbs, BG10-19, locks the spike trimer in a closed conformation to potently neutralize SARS-CoV-2, the recently arising mutants B.1.1.7 and B.1.351, and SARS-CoV and cross-reacts with heterologous RBDs. Together, our results characterize transcriptional differences among SARS-CoV-2-specific B cells and uncover cross-neutralizing Ab targets that will inform immunogen and therapeutic design against coronaviruses. |Antibodies, Monoclonal/chemistry/immunology[MESH] |Antibodies, Neutralizing/blood/chemistry/*immunology[MESH] |Antibodies, Viral/blood/chemistry/immunology[MESH] |Antigen-Antibody Complex/chemistry/metabolism[MESH] |Antigen-Antibody Reactions[MESH] |B-Lymphocytes/cytology/*metabolism/virology[MESH] |COVID-19/pathology/virology[MESH] |Cryoelectron Microscopy[MESH] |Crystallography, X-Ray[MESH] |Gene Expression Profiling[MESH] |Humans[MESH] |Immunoglobulin A/immunology[MESH] |Immunoglobulin Variable Region/chemistry/genetics[MESH] |Protein Domains/immunology[MESH] |Protein Multimerization[MESH] |Protein Structure, Quaternary[MESH] |SARS-CoV-2/*immunology/isolation & purification/metabolism[MESH] |Sequence Analysis, RNA[MESH]B cell genomics behind cross-neutralization of SARS-CoV-2 variants and(epmc).pdf DeepDyve Pubget Overpricing