Aptamer BC 007’s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing Antibodies
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 tha...
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| Format: | Article |
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MDPI AG
2021-05-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/13/5/932 |
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| author | Annekathrin Haberland Oxana Krylova Heike Nikolenko Peter Göttel Andre Dallmann Johannes Müller Hardy Weisshoff |
| author_facet | Annekathrin Haberland Oxana Krylova Heike Nikolenko Peter Göttel Andre Dallmann Johannes Müller Hardy Weisshoff |
| author_sort | Annekathrin Haberland |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T10:48:24Z |
| format | Article |
| id | doaj.art-044548cc94234da4b330218af1bc9a49 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T10:48:24Z |
| publishDate | 2021-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-044548cc94234da4b330218af1bc9a492023-11-21T22:21:23ZengMDPI AGViruses1999-49152021-05-0113593210.3390/v13050932Aptamer BC 007’s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing AntibodiesAnnekathrin Haberland0Oxana Krylova1Heike Nikolenko2Peter Göttel3Andre Dallmann4Johannes Müller5Hardy Weisshoff6Berlin Cures GmbH, Robert-Rössle-Str. 10 Blg. D79, 13125 Berlin, GermanyLeibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Robert-Rössle-Str. 10, 13125 Berlin, GermanyLeibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Robert-Rössle-Str. 10, 13125 Berlin, GermanyBerlin Cures GmbH, Knesebeckstr. 59-61, 10719 Berlin, GermanyDepartment of Chemistry, NMR Facility, Humboldt University of Berlin, Brook-Taylor-Straße 2, 12489 Berlin, GermanyBerlin Cures GmbH, Knesebeckstr. 59-61, 10719 Berlin, GermanyDepartment of Chemistry, NMR Facility, Humboldt University of Berlin, Brook-Taylor-Straße 2, 12489 Berlin, GermanyCOVID-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.https://www.mdpi.com/1999-4915/13/5/932aptamerautoantibodyBC 007COVID-19re-purposingSARS-CoV-2 antibody |
| spellingShingle | Annekathrin Haberland Oxana Krylova Heike Nikolenko Peter Göttel Andre Dallmann Johannes Müller Hardy Weisshoff Aptamer BC 007’s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing Antibodies Viruses aptamer autoantibody BC 007 COVID-19 re-purposing SARS-CoV-2 antibody |
| title | Aptamer BC 007’s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing Antibodies |
| title_full | Aptamer BC 007’s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing Antibodies |
| title_fullStr | Aptamer BC 007’s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing Antibodies |
| title_full_unstemmed | Aptamer BC 007’s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing Antibodies |
| title_short | Aptamer BC 007’s Affinity to Specific and Less-Specific Anti-SARS-CoV-2 Neutralizing Antibodies |
| title_sort | aptamer bc 007 s affinity to specific and less specific anti sars cov 2 neutralizing antibodies |
| topic | aptamer autoantibody BC 007 COVID-19 re-purposing SARS-CoV-2 antibody |
| url | https://www.mdpi.com/1999-4915/13/5/932 |
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