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A high-affinity aptamer with base-appended base-modified DNA bound to isolated authentic SARS-CoV-2 strains wild-type and B.1.617.2 (delta variant)
Simple, highly sensitive detection technologies for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are crucial for the effective implementation of public health policies. We used the systematic evolution of ligands by exponential enrichment with a modified DNA library, including a base...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9060713/ https://www.ncbi.nlm.nih.gov/pubmed/35617879 http://dx.doi.org/10.1016/j.bbrc.2022.04.071 |
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author | Minagawa, Hirotaka Sawa, Hirofumi Fujita, Tomoko Kato, Shintaro Inaguma, Asumi Hirose, Miwako Orba, Yasuko Sasaki, Michihito Tabata, Koshiro Nomura, Naoki Shingai, Masashi Suzuki, Yasuhiko Horii, Katsunori |
author_facet | Minagawa, Hirotaka Sawa, Hirofumi Fujita, Tomoko Kato, Shintaro Inaguma, Asumi Hirose, Miwako Orba, Yasuko Sasaki, Michihito Tabata, Koshiro Nomura, Naoki Shingai, Masashi Suzuki, Yasuhiko Horii, Katsunori |
author_sort | Minagawa, Hirotaka |
collection | PubMed |
description | Simple, highly sensitive detection technologies for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are crucial for the effective implementation of public health policies. We used the systematic evolution of ligands by exponential enrichment with a modified DNA library, including a base-appended base (uracil with a guanine base at its fifth position), to create an aptamer with a high affinity for the receptor-binding domain (RBD) of the SARS-CoV-2 spike glycoprotein. The aptamer had a dissociation constant of 1.2 and < 1 nM for the RBD and spike trimer, respectively. Furthermore, enzyme-linked aptamer assays confirmed that the aptamer binds to isolated authentic SARS-CoV-2 wild-type and B.1.617.2 (delta variant). The binding signal was larger that of commercially available anti-SARS-CoV-2 RBD antibody. Thus, this aptamer as a sensing element will enable the highly sensitive detection of SARS-CoV-2. |
format | Online Article Text |
id | pubmed-9060713 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-90607132022-05-03 A high-affinity aptamer with base-appended base-modified DNA bound to isolated authentic SARS-CoV-2 strains wild-type and B.1.617.2 (delta variant) Minagawa, Hirotaka Sawa, Hirofumi Fujita, Tomoko Kato, Shintaro Inaguma, Asumi Hirose, Miwako Orba, Yasuko Sasaki, Michihito Tabata, Koshiro Nomura, Naoki Shingai, Masashi Suzuki, Yasuhiko Horii, Katsunori Biochem Biophys Res Commun Article Simple, highly sensitive detection technologies for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are crucial for the effective implementation of public health policies. We used the systematic evolution of ligands by exponential enrichment with a modified DNA library, including a base-appended base (uracil with a guanine base at its fifth position), to create an aptamer with a high affinity for the receptor-binding domain (RBD) of the SARS-CoV-2 spike glycoprotein. The aptamer had a dissociation constant of 1.2 and < 1 nM for the RBD and spike trimer, respectively. Furthermore, enzyme-linked aptamer assays confirmed that the aptamer binds to isolated authentic SARS-CoV-2 wild-type and B.1.617.2 (delta variant). The binding signal was larger that of commercially available anti-SARS-CoV-2 RBD antibody. Thus, this aptamer as a sensing element will enable the highly sensitive detection of SARS-CoV-2. Elsevier Inc. 2022-07-23 2022-05-02 /pmc/articles/PMC9060713/ /pubmed/35617879 http://dx.doi.org/10.1016/j.bbrc.2022.04.071 Text en © 2022 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Minagawa, Hirotaka Sawa, Hirofumi Fujita, Tomoko Kato, Shintaro Inaguma, Asumi Hirose, Miwako Orba, Yasuko Sasaki, Michihito Tabata, Koshiro Nomura, Naoki Shingai, Masashi Suzuki, Yasuhiko Horii, Katsunori A high-affinity aptamer with base-appended base-modified DNA bound to isolated authentic SARS-CoV-2 strains wild-type and B.1.617.2 (delta variant) |
title | A high-affinity aptamer with base-appended base-modified DNA bound to isolated authentic SARS-CoV-2 strains wild-type and B.1.617.2 (delta variant) |
title_full | A high-affinity aptamer with base-appended base-modified DNA bound to isolated authentic SARS-CoV-2 strains wild-type and B.1.617.2 (delta variant) |
title_fullStr | A high-affinity aptamer with base-appended base-modified DNA bound to isolated authentic SARS-CoV-2 strains wild-type and B.1.617.2 (delta variant) |
title_full_unstemmed | A high-affinity aptamer with base-appended base-modified DNA bound to isolated authentic SARS-CoV-2 strains wild-type and B.1.617.2 (delta variant) |
title_short | A high-affinity aptamer with base-appended base-modified DNA bound to isolated authentic SARS-CoV-2 strains wild-type and B.1.617.2 (delta variant) |
title_sort | high-affinity aptamer with base-appended base-modified dna bound to isolated authentic sars-cov-2 strains wild-type and b.1.617.2 (delta variant) |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9060713/ https://www.ncbi.nlm.nih.gov/pubmed/35617879 http://dx.doi.org/10.1016/j.bbrc.2022.04.071 |
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