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10.1002/bit.27355 http://scihub22266oqcxt.onion/10.1002/bit.27355 32297972!7262357!32297972     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       Biotechnol+Bioeng 2020 ; 117 (7): 1990-2007 Nephropedia Template TP {{tp|p=32297972|t=2020. Built-in RNA-mediated chaperone (chaperna) for antigen folding tailored to immunized hosts |pdf=|usr=}}{{32297972}} gab.com Text Built-in RNA-mediated chaperone (chaperna) for antigen folding tailored to immunized hosts JO: Biotechnol Bioeng http://www.kidney.de/pget.php?&tw=1&pmid=32297972 #FOAvip High-quality antibody (Ab) production depends on the availability of immunologically relevant antigens. We present a potentially universal platform for generating soluble antigens from bacterial hosts, tailored to immunized animals for Ab production. A novel RNA-dependent chaperone, in which the target antigen is genetically fused with an RNA-interacting domain (RID) docking tag derived from the immunized host, promotes the solubility and robust folding of the target antigen. We selected the N-terminal tRNA-binding domain of lysyl-tRNA synthetase (LysRS) as the RID for fusion with viral proteins and demonstrated the expression of the RID fusion proteins in their soluble and native conformations; immunization predominantly elicited Ab responses to the target antigen, whereas the "self" RID tag remained nonimmunogenic. Differential immunogenicity of the fusion proteins greatly enriched and simplified the screening of hybridoma clones of monoclonal antibodies (mAbs), enabling specific and sensitive serodiagnosis of MERS-CoV infection. Moreover, mAbs against the consensus influenza hemagglutinin stalk domain enabled a novel assay for trivalent seasonal influenza vaccines. The Fc-mediated effector function was demonstrated, which could be harnessed for the design of next-generation "universal" influenza vaccines. The nonimmunogenic built-in antigen folding module tailored to a repertoire of immunized animal hosts will drive immunochemical diagnostics, therapeutics, and designer vaccines. Twit Text FOAVip Built-in RNA-mediated chaperone (chaperna) for antigen folding tailored to immunized hosts ????Biotechnol Bioeng http://www.kidney.de/pget.php?&tw=1&pmid=32297972 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32297972 #FOAvip English Wikipedia <ref>{{Cite pmid|32297972}}</ref> Built-in RNA-mediated chaperone (chaperna) for antigen folding tailored to immunized hosts #MMPMID32297972 Kim YS; Lim J; Sung J; Cheong Y; Lee EY; Kim J; Oh H; Kim YS; Cho NH; Choi S; Kang SM; Nam JH; Chae W; Seong BL Biotechnol Bioeng 2020[Jul]; 117 (7): 1990-2007 PMID32297972show ga High-quality antibody (Ab) production depends on the availability of immunologically relevant antigens. We present a potentially universal platform for generating soluble antigens from bacterial hosts, tailored to immunized animals for Ab production. A novel RNA-dependent chaperone, in which the target antigen is genetically fused with an RNA-interacting domain (RID) docking tag derived from the immunized host, promotes the solubility and robust folding of the target antigen. We selected the N-terminal tRNA-binding domain of lysyl-tRNA synthetase (LysRS) as the RID for fusion with viral proteins and demonstrated the expression of the RID fusion proteins in their soluble and native conformations; immunization predominantly elicited Ab responses to the target antigen, whereas the "self" RID tag remained nonimmunogenic. Differential immunogenicity of the fusion proteins greatly enriched and simplified the screening of hybridoma clones of monoclonal antibodies (mAbs), enabling specific and sensitive serodiagnosis of MERS-CoV infection. Moreover, mAbs against the consensus influenza hemagglutinin stalk domain enabled a novel assay for trivalent seasonal influenza vaccines. The Fc-mediated effector function was demonstrated, which could be harnessed for the design of next-generation "universal" influenza vaccines. The nonimmunogenic built-in antigen folding module tailored to a repertoire of immunized animal hosts will drive immunochemical diagnostics, therapeutics, and designer vaccines. |*Molecular Chaperones[MESH] |Animals[MESH] |Antibodies, Monoclonal/*biosynthesis/immunology/isolation & purification[MESH] |Antibodies, Viral/*biosynthesis/immunology/isolation & purification[MESH] |Antigens, Viral/*chemistry/genetics/immunology[MESH] |Coronavirus Infections/blood/*diagnosis[MESH] |Enzyme-Linked Immunosorbent Assay[MESH] |Female[MESH] |Hemagglutinin Glycoproteins, Influenza Virus/chemistry/genetics/immunology[MESH] |Humans[MESH] |Hybridomas/*immunology[MESH] |Immunization[MESH] |Influenza Vaccines[MESH] |Lysine-tRNA Ligase/chemistry/genetics[MESH] |Mice[MESH] |Mice, Inbred BALB C[MESH] |Middle East Respiratory Syndrome Coronavirus/*immunology[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Protein Folding[MESH] |Recombinant Fusion Proteins/chemistry/genetics/immunology[MESH] |Serologic Tests[MESH]Built-in RNA-mediated chaperone (chaperna) for antigen folding tailore(epmc).pdf DeepDyve Pubget Overpricing