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Specific anti-SARS-CoV-2 S1 IgY-scFv is a promising tool for recognition of the virus
As severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to spread globally, a series of vaccines, antibodies and drugs have been developed to combat coronavirus disease 2019 (COVID-19). High specific antibodies are powerful tool for the development of immunoassay and providing pass...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8840941/ https://www.ncbi.nlm.nih.gov/pubmed/35150368 http://dx.doi.org/10.1186/s13568-022-01355-4 |
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author | Ge, Shikun Wu, Rao Zhou, Tingting Liu, Xiang Zhu, Jin Zhang, Xiaoying |
author_facet | Ge, Shikun Wu, Rao Zhou, Tingting Liu, Xiang Zhu, Jin Zhang, Xiaoying |
author_sort | Ge, Shikun |
collection | PubMed |
description | As severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to spread globally, a series of vaccines, antibodies and drugs have been developed to combat coronavirus disease 2019 (COVID-19). High specific antibodies are powerful tool for the development of immunoassay and providing passive immunotherapy against SARS-CoV-2 and expected with large scale production. SARS-CoV-2 S1 protein was expressed in E. coli BL21 and purified by immobilized metal affinity chromatography, as antigen used to immunize hens, the specific IgY antibodies were extracted form egg yolk by PEG-6000 precipitation, and the titer of anti-S1 IgY antibody reached 1:10,000. IgY single chain variable fragment antibody (IgY-scFv) was generated by using phage display technology and the IgY-scFv showed high binding sensitivity and capacity to S1 protein of SARS-CoV-2, and the minimum detectable antigen S1 protein concentration was 6 ng/µL. The docking study showed that the multiple epitopes on the IgY-scFv interacted with multiple residues on SARS-CoV-2 S1 RBD to form hydrogen bonds. This preliminary study suggests that IgY and IgY-scFv are suitable candidates for the development of immunoassay and passive immunotherapy for COVID-19 to humans and animals. |
format | Online Article Text |
id | pubmed-8840941 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-88409412022-02-18 Specific anti-SARS-CoV-2 S1 IgY-scFv is a promising tool for recognition of the virus Ge, Shikun Wu, Rao Zhou, Tingting Liu, Xiang Zhu, Jin Zhang, Xiaoying AMB Express Original Article As severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to spread globally, a series of vaccines, antibodies and drugs have been developed to combat coronavirus disease 2019 (COVID-19). High specific antibodies are powerful tool for the development of immunoassay and providing passive immunotherapy against SARS-CoV-2 and expected with large scale production. SARS-CoV-2 S1 protein was expressed in E. coli BL21 and purified by immobilized metal affinity chromatography, as antigen used to immunize hens, the specific IgY antibodies were extracted form egg yolk by PEG-6000 precipitation, and the titer of anti-S1 IgY antibody reached 1:10,000. IgY single chain variable fragment antibody (IgY-scFv) was generated by using phage display technology and the IgY-scFv showed high binding sensitivity and capacity to S1 protein of SARS-CoV-2, and the minimum detectable antigen S1 protein concentration was 6 ng/µL. The docking study showed that the multiple epitopes on the IgY-scFv interacted with multiple residues on SARS-CoV-2 S1 RBD to form hydrogen bonds. This preliminary study suggests that IgY and IgY-scFv are suitable candidates for the development of immunoassay and passive immunotherapy for COVID-19 to humans and animals. Springer Berlin Heidelberg 2022-02-12 /pmc/articles/PMC8840941/ /pubmed/35150368 http://dx.doi.org/10.1186/s13568-022-01355-4 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Original Article Ge, Shikun Wu, Rao Zhou, Tingting Liu, Xiang Zhu, Jin Zhang, Xiaoying Specific anti-SARS-CoV-2 S1 IgY-scFv is a promising tool for recognition of the virus |
title | Specific anti-SARS-CoV-2 S1 IgY-scFv is a promising tool for recognition of the virus |
title_full | Specific anti-SARS-CoV-2 S1 IgY-scFv is a promising tool for recognition of the virus |
title_fullStr | Specific anti-SARS-CoV-2 S1 IgY-scFv is a promising tool for recognition of the virus |
title_full_unstemmed | Specific anti-SARS-CoV-2 S1 IgY-scFv is a promising tool for recognition of the virus |
title_short | Specific anti-SARS-CoV-2 S1 IgY-scFv is a promising tool for recognition of the virus |
title_sort | specific anti-sars-cov-2 s1 igy-scfv is a promising tool for recognition of the virus |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8840941/ https://www.ncbi.nlm.nih.gov/pubmed/35150368 http://dx.doi.org/10.1186/s13568-022-01355-4 |
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