The interaction of the SARS coronavirus non-structural protein 10 with the cellular oxido-reductase system causes an extensive cytopathic effect

The pathological mechanism of SARS-CoV infection was investigated. The gene for the SARS-CoV non-structural protein 10, which is located in the open reading frame of pp1a/pp1ab gene, was synthesized and used to screen for the specific cellular gene coding for the protein interacting with this nsp10...

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Autores principales: Li, Qihan, Wang, Lichun, Dong, Chenghong, Che, Yanchun, Jiang, Li, Liu, Longding, Zhao, Hongling, Liao, Yun, Sheng, Yi, Dong, Shaozhong, Ma, Shaohui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier B.V. 2005
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7108382/
https://www.ncbi.nlm.nih.gov/pubmed/16157265
http://dx.doi.org/10.1016/j.jcv.2004.12.019
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author Li, Qihan
Wang, Lichun
Dong, Chenghong
Che, Yanchun
Jiang, Li
Liu, Longding
Zhao, Hongling
Liao, Yun
Sheng, Yi
Dong, Shaozhong
Ma, Shaohui
author_facet Li, Qihan
Wang, Lichun
Dong, Chenghong
Che, Yanchun
Jiang, Li
Liu, Longding
Zhao, Hongling
Liao, Yun
Sheng, Yi
Dong, Shaozhong
Ma, Shaohui
author_sort Li, Qihan
collection PubMed
description The pathological mechanism of SARS-CoV infection was investigated. The gene for the SARS-CoV non-structural protein 10, which is located in the open reading frame of pp1a/pp1ab gene, was synthesized and used to screen for the specific cellular gene coding for the protein interacting with this nsp10 protein in a human embryo lung cDNA library using a yeast trap method. The results indicated that apart from the two subunits of cellular RNA polymerase complex, BTF3 and ATF5, this nsp10 protein was also able to interact specifically with the NADH 4L subunit and cytochrome oxidase II. Further study revealed that the activity of the NADH-cytochrome was altered and the inner mitochondrial membrane was depolarized in the transfected human embryo lung fibroblast by the nsp10 protein gene. The cytopathic effect of the Coronavirus 229E strain appeared more extensive in these cells than in the control cells.
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spelling pubmed-71083822020-03-31 The interaction of the SARS coronavirus non-structural protein 10 with the cellular oxido-reductase system causes an extensive cytopathic effect Li, Qihan Wang, Lichun Dong, Chenghong Che, Yanchun Jiang, Li Liu, Longding Zhao, Hongling Liao, Yun Sheng, Yi Dong, Shaozhong Ma, Shaohui J Clin Virol Article The pathological mechanism of SARS-CoV infection was investigated. The gene for the SARS-CoV non-structural protein 10, which is located in the open reading frame of pp1a/pp1ab gene, was synthesized and used to screen for the specific cellular gene coding for the protein interacting with this nsp10 protein in a human embryo lung cDNA library using a yeast trap method. The results indicated that apart from the two subunits of cellular RNA polymerase complex, BTF3 and ATF5, this nsp10 protein was also able to interact specifically with the NADH 4L subunit and cytochrome oxidase II. Further study revealed that the activity of the NADH-cytochrome was altered and the inner mitochondrial membrane was depolarized in the transfected human embryo lung fibroblast by the nsp10 protein gene. The cytopathic effect of the Coronavirus 229E strain appeared more extensive in these cells than in the control cells. Elsevier B.V. 2005-10 2005-04-06 /pmc/articles/PMC7108382/ /pubmed/16157265 http://dx.doi.org/10.1016/j.jcv.2004.12.019 Text en Copyright © 2005 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
Li, Qihan
Wang, Lichun
Dong, Chenghong
Che, Yanchun
Jiang, Li
Liu, Longding
Zhao, Hongling
Liao, Yun
Sheng, Yi
Dong, Shaozhong
Ma, Shaohui
The interaction of the SARS coronavirus non-structural protein 10 with the cellular oxido-reductase system causes an extensive cytopathic effect
title The interaction of the SARS coronavirus non-structural protein 10 with the cellular oxido-reductase system causes an extensive cytopathic effect
title_full The interaction of the SARS coronavirus non-structural protein 10 with the cellular oxido-reductase system causes an extensive cytopathic effect
title_fullStr The interaction of the SARS coronavirus non-structural protein 10 with the cellular oxido-reductase system causes an extensive cytopathic effect
title_full_unstemmed The interaction of the SARS coronavirus non-structural protein 10 with the cellular oxido-reductase system causes an extensive cytopathic effect
title_short The interaction of the SARS coronavirus non-structural protein 10 with the cellular oxido-reductase system causes an extensive cytopathic effect
title_sort interaction of the sars coronavirus non-structural protein 10 with the cellular oxido-reductase system causes an extensive cytopathic effect
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7108382/
https://www.ncbi.nlm.nih.gov/pubmed/16157265
http://dx.doi.org/10.1016/j.jcv.2004.12.019
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