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The “SARS-unique domain” (SUD) of SARS coronavirus is an oligo(G)-binding protein
Caused by a new coronavirus, severe acute respiratory syndrome (SARS) is a highly contagious disease associated with significant fatality that emerged in 2003. The molecular cause of the unusually high human pathogenicity of the SARS coronavirus (SARS-CoV) is still unknown. In an effort to character...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Inc.
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7092865/ https://www.ncbi.nlm.nih.gov/pubmed/17976532 http://dx.doi.org/10.1016/j.bbrc.2007.10.081 |
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author | Tan, Jinzhi Kusov, Yuri Mutschall, Doris Tech, Stefanie Nagarajan, Krishna Hilgenfeld, Rolf Schmidt, Christian L. |
author_facet | Tan, Jinzhi Kusov, Yuri Mutschall, Doris Tech, Stefanie Nagarajan, Krishna Hilgenfeld, Rolf Schmidt, Christian L. |
author_sort | Tan, Jinzhi |
collection | PubMed |
description | Caused by a new coronavirus, severe acute respiratory syndrome (SARS) is a highly contagious disease associated with significant fatality that emerged in 2003. The molecular cause of the unusually high human pathogenicity of the SARS coronavirus (SARS-CoV) is still unknown. In an effort to characterize molecular components of the virus that are absent in other coronaviruses, all of which are considerably less pathogenic for humans, we recombinantly produced the SARS-unique domain (SUD) within non-structural protein 3 (Nsp3) of SARS-CoV and characterized its nucleic-acid binding properties. Zone-interference gel electrophoresis and electrophoretic mobility shift assays revealed a specific affinity of SUD for oligo(G)-strings. A few such segments are present in the SARS-CoV genome, but also in mRNAs of host proteins involved in the regulation of signaling pathways. A putative role of SUD in virus-induced apoptosis or survival of host cells is discussed. |
format | Online Article Text |
id | pubmed-7092865 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-70928652020-03-25 The “SARS-unique domain” (SUD) of SARS coronavirus is an oligo(G)-binding protein Tan, Jinzhi Kusov, Yuri Mutschall, Doris Tech, Stefanie Nagarajan, Krishna Hilgenfeld, Rolf Schmidt, Christian L. Biochem Biophys Res Commun Article Caused by a new coronavirus, severe acute respiratory syndrome (SARS) is a highly contagious disease associated with significant fatality that emerged in 2003. The molecular cause of the unusually high human pathogenicity of the SARS coronavirus (SARS-CoV) is still unknown. In an effort to characterize molecular components of the virus that are absent in other coronaviruses, all of which are considerably less pathogenic for humans, we recombinantly produced the SARS-unique domain (SUD) within non-structural protein 3 (Nsp3) of SARS-CoV and characterized its nucleic-acid binding properties. Zone-interference gel electrophoresis and electrophoretic mobility shift assays revealed a specific affinity of SUD for oligo(G)-strings. A few such segments are present in the SARS-CoV genome, but also in mRNAs of host proteins involved in the regulation of signaling pathways. A putative role of SUD in virus-induced apoptosis or survival of host cells is discussed. Elsevier Inc. 2007-12-28 2007-10-23 /pmc/articles/PMC7092865/ /pubmed/17976532 http://dx.doi.org/10.1016/j.bbrc.2007.10.081 Text en Copyright © 2007 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 Tan, Jinzhi Kusov, Yuri Mutschall, Doris Tech, Stefanie Nagarajan, Krishna Hilgenfeld, Rolf Schmidt, Christian L. The “SARS-unique domain” (SUD) of SARS coronavirus is an oligo(G)-binding protein |
title | The “SARS-unique domain” (SUD) of SARS coronavirus is an oligo(G)-binding protein |
title_full | The “SARS-unique domain” (SUD) of SARS coronavirus is an oligo(G)-binding protein |
title_fullStr | The “SARS-unique domain” (SUD) of SARS coronavirus is an oligo(G)-binding protein |
title_full_unstemmed | The “SARS-unique domain” (SUD) of SARS coronavirus is an oligo(G)-binding protein |
title_short | The “SARS-unique domain” (SUD) of SARS coronavirus is an oligo(G)-binding protein |
title_sort | “sars-unique domain” (sud) of sars coronavirus is an oligo(g)-binding protein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7092865/ https://www.ncbi.nlm.nih.gov/pubmed/17976532 http://dx.doi.org/10.1016/j.bbrc.2007.10.081 |
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