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10.1126/scitranslmed.abc3539 http://scihub22266oqcxt.onion/10.1126/scitranslmed.abc3539 32513867!7286538!32513867     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Transl+Med 2020 ; 12 (550): ä Nephropedia Template TP {{tp|p=32513867|t=2020. Antibody signature induced by SARS-CoV-2 spike protein immunogens in rabbits |pdf=|usr=}}{{32513867}} gab.com Text Antibody signature induced by SARS-CoV-2 spike protein immunogens in rabbits JO: Sci Transl Med http://www.kidney.de/pget.php?&tw=1&pmid=32513867 #FOAvip Multiple vaccine candidates against SARS-CoV-2 based on viral spike protein are under development. However, there is limited information on the quality of antibody responses generated with these vaccine modalities. To better understand antibody responses induced by spike protein-based vaccines, we performed a qualitative study by immunizing rabbits with various SARS-CoV-2 spike protein antigens: S ectodomain (S1+S2; amino acids 16 to 1213), which lacks the cytoplasmic and transmembrane domains (CT-TM), the S1 domain (amino acids 16 to 685), the receptor binding domain (RBD) (amino acids 319 to 541), and the S2 domain (amino acids 686 to 1213, lacking the RBD, as control). Resulting antibody quality and function were analyzed by enzyme-linked immunosorbent assay (ELISA), RBD competition assay, surface plasmon resonance (SPR) against different spike proteins in native conformation, and neutralization assays. All three antigens (S1+S2 ectodomain, S1 domain, and RBD), but not S2, generated strong neutralizing antibodies against SARS-CoV-2. Vaccination-induced antibody repertoire was analyzed by SARS-CoV-2 spike genome fragment phage display libraries (SARS-CoV-2 GFPDL), which identified immunodominant epitopes in the S1, S1-RBD, and S2 domains. Furthermore, these analyses demonstrated that the RBD immunogen elicited a higher antibody titer with five-fold higher affinity antibodies to native spike antigens compared with other spike antigens, and antibody affinity correlated strongly with neutralization titers. These findings may help guide rational vaccine design and facilitate development and evaluation of effective therapeutics and vaccines against COVID-19 disease. Twit Text FOAVip Antibody signature induced by SARS-CoV-2 spike protein immunogens in rabbits ????Sci Transl Med http://www.kidney.de/pget.php?&tw=1&pmid=32513867 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32513867 #FOAvip English Wikipedia <ref>{{Cite pmid|32513867}}</ref> Antibody signature induced by SARS-CoV-2 spike protein immunogens in rabbits #MMPMID32513867 Ravichandran S; Coyle EM; Klenow L; Tang J; Grubbs G; Liu S; Wang T; Golding H; Khurana S Sci Transl Med 2020[Jul]; 12 (550): ä PMID32513867show ga Multiple vaccine candidates against SARS-CoV-2 based on viral spike protein are under development. However, there is limited information on the quality of antibody responses generated with these vaccine modalities. To better understand antibody responses induced by spike protein-based vaccines, we performed a qualitative study by immunizing rabbits with various SARS-CoV-2 spike protein antigens: S ectodomain (S1+S2; amino acids 16 to 1213), which lacks the cytoplasmic and transmembrane domains (CT-TM), the S1 domain (amino acids 16 to 685), the receptor binding domain (RBD) (amino acids 319 to 541), and the S2 domain (amino acids 686 to 1213, lacking the RBD, as control). Resulting antibody quality and function were analyzed by enzyme-linked immunosorbent assay (ELISA), RBD competition assay, surface plasmon resonance (SPR) against different spike proteins in native conformation, and neutralization assays. All three antigens (S1+S2 ectodomain, S1 domain, and RBD), but not S2, generated strong neutralizing antibodies against SARS-CoV-2. Vaccination-induced antibody repertoire was analyzed by SARS-CoV-2 spike genome fragment phage display libraries (SARS-CoV-2 GFPDL), which identified immunodominant epitopes in the S1, S1-RBD, and S2 domains. Furthermore, these analyses demonstrated that the RBD immunogen elicited a higher antibody titer with five-fold higher affinity antibodies to native spike antigens compared with other spike antigens, and antibody affinity correlated strongly with neutralization titers. These findings may help guide rational vaccine design and facilitate development and evaluation of effective therapeutics and vaccines against COVID-19 disease. |Animals[MESH] |Antibodies, Neutralizing/immunology[MESH] |Antibodies, Viral/*immunology[MESH] |Antibody Formation/immunology[MESH] |Antigens, Viral/immunology[MESH] |Epitopes/immunology[MESH] |Female[MESH] |Immunization[MESH] |Neutralization Tests[MESH] |Rabbits[MESH]Antibody signature induced by SARS-CoV-2 spike protein immunogens in r(epmc).pdf DeepDyve Pubget Overpricing