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10.3390/v13050932 http://scihub22266oqcxt.onion/10.3390/v13050932 34069827!8157297!34069827     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 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Viruses 2021 ; 13 (5): ä Nephropedia Template TP {{tp|p=34069827|t=2021. Aptamer BC 007 s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing Antibodies |pdf=|usr=}}{{34069827}} gab.com Text Aptamer BC 007 s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing Antibodies JO: Viruses http://www.kidney.de/pget.php?&tw=1&pmid=34069827 #FOAvip COVID-19 is a pandemic respiratory disease that is caused by the highly infectious severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Anti-SARS-CoV-2 antibodies are essential weapons that a patient with COVID-19 has to combat the disease. When now repurposing a drug, namely an aptamer that interacts with SARS-CoV-2 proteins for COVID-19 treatment (BC 007), which is, however, a neutralizer of pathogenic autoantibodies in its original indication, the possibility of also binding and neutralizing anti-SARS-CoV-2 antibodies must be considered. Here, the highly specific virus-neutralizing antibodies have to be distinguished from the ones that also show cross-reactivity to tissues. The last-mentioned could be the origin of the widely reported SARS-CoV-2-induced autoimmunity, which should also become a target of therapy. We, therefore, used enzyme-linked immunosorbent assay (ELISA) technology to assess the binding of well-characterized publicly accessible anti-SARS-CoV-2 antibodies (CV07-209 and CV07-270) with BC 007. Nuclear magnetic resonance spectroscopy, isothermal calorimetric titration, and circular dichroism spectroscopy were additionally used to test the binding of BC 007 to DNA-binding sequence segments of these antibodies. BC 007 did not bind to the highly specific neutralizing anti-SARS-CoV-2 antibody but did bind to the less specific one. This, however, was a lot less compared to an autoantibody of its original indication (14.2%, range 11.0-21.5%). It was also interesting to see that the less-specific anti-SARS-CoV-2 antibody also showed a high background signal in the ELISA (binding on NeutrAvidin-coated or activated but noncoated plastic plate). These initial experiments suggest that the risk of binding and neutralizing highly specific anti-SARS CoV-2 antibodies by BC 007 should be low. Twit Text FOAVip Aptamer BC 007 s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing Antibodies ????Viruses http://www.kidney.de/pget.php?&tw=1&pmid=34069827 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34069827 #FOAvip English Wikipedia <ref>{{Cite pmid|34069827}}</ref> Aptamer BC 007 s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing Antibodies #MMPMID34069827 Haberland A; Krylova O; Nikolenko H; Gottel P; Dallmann A; Muller J; Weisshoff H Viruses 2021[May]; 13 (5): ä PMID34069827show ga COVID-19 is a pandemic respiratory disease that is caused by the highly infectious severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Anti-SARS-CoV-2 antibodies are essential weapons that a patient with COVID-19 has to combat the disease. When now repurposing a drug, namely an aptamer that interacts with SARS-CoV-2 proteins for COVID-19 treatment (BC 007), which is, however, a neutralizer of pathogenic autoantibodies in its original indication, the possibility of also binding and neutralizing anti-SARS-CoV-2 antibodies must be considered. Here, the highly specific virus-neutralizing antibodies have to be distinguished from the ones that also show cross-reactivity to tissues. The last-mentioned could be the origin of the widely reported SARS-CoV-2-induced autoimmunity, which should also become a target of therapy. We, therefore, used enzyme-linked immunosorbent assay (ELISA) technology to assess the binding of well-characterized publicly accessible anti-SARS-CoV-2 antibodies (CV07-209 and CV07-270) with BC 007. Nuclear magnetic resonance spectroscopy, isothermal calorimetric titration, and circular dichroism spectroscopy were additionally used to test the binding of BC 007 to DNA-binding sequence segments of these antibodies. BC 007 did not bind to the highly specific neutralizing anti-SARS-CoV-2 antibody but did bind to the less specific one. This, however, was a lot less compared to an autoantibody of its original indication (14.2%, range 11.0-21.5%). It was also interesting to see that the less-specific anti-SARS-CoV-2 antibody also showed a high background signal in the ELISA (binding on NeutrAvidin-coated or activated but noncoated plastic plate). These initial experiments suggest that the risk of binding and neutralizing highly specific anti-SARS CoV-2 antibodies by BC 007 should be low. |Antibodies, Blocking/immunology[MESH] |Antibodies, Neutralizing/*immunology[MESH] |Antibodies, Viral/immunology[MESH] |Aptamers, Nucleotide/*pharmacology[MESH] |Autoantibodies/immunology[MESH] |COVID-19/immunology/metabolism[MESH] |Enzyme-Linked Immunosorbent Assay[MESH] |Humans[MESH] |Immunoglobulin G/immunology[MESH] |Neutralization Tests/methods[MESH] |Pandemics[MESH] |SARS-CoV-2/*immunology/pathogenicity[MESH]Aptamer BC 007 s Affinity to Specific and Less-Specific Anti-SARS-CoV-(epmc).pdf DeepDyve Pubget Overpricing