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Phages bearing affinity peptides to severe acute respiratory syndromes-associated coronavirus differentiate this virus from other viruses
BACKGROUND: Transmission of SARS-associated coronavirus (SARS-CoV) is now well controlled, nevertheless, it is important to develop effective methods to identify this virus from other pathogens. OBJECTIVES: The purpose of this study was to identify potential ligands and develop a novel diagnostic te...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier B.V.
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7108448/ https://www.ncbi.nlm.nih.gov/pubmed/23664850 http://dx.doi.org/10.1016/j.jcv.2013.04.002 |
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author | Wang, Chao Sun, Xuejiao Suo, Siqingaowa Ren, Yudong Li, Xunliang Herrler, Georg Thiel, Volker Ren, Xiaofeng |
author_facet | Wang, Chao Sun, Xuejiao Suo, Siqingaowa Ren, Yudong Li, Xunliang Herrler, Georg Thiel, Volker Ren, Xiaofeng |
author_sort | Wang, Chao |
collection | PubMed |
description | BACKGROUND: Transmission of SARS-associated coronavirus (SARS-CoV) is now well controlled, nevertheless, it is important to develop effective methods to identify this virus from other pathogens. OBJECTIVES: The purpose of this study was to identify potential ligands and develop a novel diagnostic test to SARS-CoV using phage display technology. STUDY DESIGN: The SARS-CoV spike 1 (S1) protein containing the receptor binding region (RBD) was used as an immobilized target followed by incubation with a 12-mer phage display random peptide library. After four rounds of biopanning, 10 monoclonal phages with specific binding activity to the S1-RBD protein were obtained and subjected to binding and diagnostic assays. RESULTS: DNA sequencing showed that two phage displayed peptides HHKTWHPPVMHL (phage-H) and SQWHPRSASYPM (phage-S) that were specific ligands to the S1 protein. Moreover, the selected phage-H and phage-S were capable of differentiating SARS-CoV from other coronaviruses in indirect enzyme-linked immunosorbent assays. CONCLUSION: The peptides identified in this study are useful reagents for detection of SARS-CoV. |
format | Online Article Text |
id | pubmed-7108448 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71084482020-03-31 Phages bearing affinity peptides to severe acute respiratory syndromes-associated coronavirus differentiate this virus from other viruses Wang, Chao Sun, Xuejiao Suo, Siqingaowa Ren, Yudong Li, Xunliang Herrler, Georg Thiel, Volker Ren, Xiaofeng J Clin Virol Article BACKGROUND: Transmission of SARS-associated coronavirus (SARS-CoV) is now well controlled, nevertheless, it is important to develop effective methods to identify this virus from other pathogens. OBJECTIVES: The purpose of this study was to identify potential ligands and develop a novel diagnostic test to SARS-CoV using phage display technology. STUDY DESIGN: The SARS-CoV spike 1 (S1) protein containing the receptor binding region (RBD) was used as an immobilized target followed by incubation with a 12-mer phage display random peptide library. After four rounds of biopanning, 10 monoclonal phages with specific binding activity to the S1-RBD protein were obtained and subjected to binding and diagnostic assays. RESULTS: DNA sequencing showed that two phage displayed peptides HHKTWHPPVMHL (phage-H) and SQWHPRSASYPM (phage-S) that were specific ligands to the S1 protein. Moreover, the selected phage-H and phage-S were capable of differentiating SARS-CoV from other coronaviruses in indirect enzyme-linked immunosorbent assays. CONCLUSION: The peptides identified in this study are useful reagents for detection of SARS-CoV. Elsevier B.V. 2013-08 2013-05-09 /pmc/articles/PMC7108448/ /pubmed/23664850 http://dx.doi.org/10.1016/j.jcv.2013.04.002 Text en Copyright © 2013 Elsevier B.V. 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 Wang, Chao Sun, Xuejiao Suo, Siqingaowa Ren, Yudong Li, Xunliang Herrler, Georg Thiel, Volker Ren, Xiaofeng Phages bearing affinity peptides to severe acute respiratory syndromes-associated coronavirus differentiate this virus from other viruses |
title | Phages bearing affinity peptides to severe acute respiratory syndromes-associated coronavirus differentiate this virus from other viruses |
title_full | Phages bearing affinity peptides to severe acute respiratory syndromes-associated coronavirus differentiate this virus from other viruses |
title_fullStr | Phages bearing affinity peptides to severe acute respiratory syndromes-associated coronavirus differentiate this virus from other viruses |
title_full_unstemmed | Phages bearing affinity peptides to severe acute respiratory syndromes-associated coronavirus differentiate this virus from other viruses |
title_short | Phages bearing affinity peptides to severe acute respiratory syndromes-associated coronavirus differentiate this virus from other viruses |
title_sort | phages bearing affinity peptides to severe acute respiratory syndromes-associated coronavirus differentiate this virus from other viruses |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7108448/ https://www.ncbi.nlm.nih.gov/pubmed/23664850 http://dx.doi.org/10.1016/j.jcv.2013.04.002 |
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