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Identification of amino acid residues important for anti-IFN activity of porcine reproductive and respiratory syndrome virus non-structural protein 1
The non-structural protein 1 (nsp1) of porcine reproductive and respiratory syndrome virus is partly responsible for inhibition of type I interferon (IFN) response by the infected host. By performing alanine-scanning mutagenesis, we have identified amino acid residues in nsp1α and nsp1β (the proteol...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Inc.
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111991/ https://www.ncbi.nlm.nih.gov/pubmed/22995188 http://dx.doi.org/10.1016/j.virol.2012.08.034 |
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author | Beura, Lalit K. Subramaniam, Sakthivel Vu, Hiep L.X. Kwon, Byungjoon Pattnaik, Asit K. Osorio, Fernando A. |
author_facet | Beura, Lalit K. Subramaniam, Sakthivel Vu, Hiep L.X. Kwon, Byungjoon Pattnaik, Asit K. Osorio, Fernando A. |
author_sort | Beura, Lalit K. |
collection | PubMed |
description | The non-structural protein 1 (nsp1) of porcine reproductive and respiratory syndrome virus is partly responsible for inhibition of type I interferon (IFN) response by the infected host. By performing alanine-scanning mutagenesis, we have identified amino acid residues in nsp1α and nsp1β (the proteolytic products of nsp1) that when substituted with alanine(s) exhibited significant relief of IFN-suppression. A mutant virus (16-5A, in which residues 16–20 of nsp1β were substituted with alanines) encoding mutant nsp1β recovered from infectious cDNA clone was shown to be attenuated for growth in vitro and induced significantly higher amount of type I IFN transcripts in infected macrophages. In infected pigs, the 16-5A virus exhibited reduced growth at early times after infection but quickly regained wild type growth properties as a result of substitutions within the mutated sequences. The results indicate a strong selection pressure towards maintaining the IFN-inhibitory property of the virus for successful propagation in pigs. |
format | Online Article Text |
id | pubmed-7111991 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71119912020-04-02 Identification of amino acid residues important for anti-IFN activity of porcine reproductive and respiratory syndrome virus non-structural protein 1 Beura, Lalit K. Subramaniam, Sakthivel Vu, Hiep L.X. Kwon, Byungjoon Pattnaik, Asit K. Osorio, Fernando A. Virology Article The non-structural protein 1 (nsp1) of porcine reproductive and respiratory syndrome virus is partly responsible for inhibition of type I interferon (IFN) response by the infected host. By performing alanine-scanning mutagenesis, we have identified amino acid residues in nsp1α and nsp1β (the proteolytic products of nsp1) that when substituted with alanine(s) exhibited significant relief of IFN-suppression. A mutant virus (16-5A, in which residues 16–20 of nsp1β were substituted with alanines) encoding mutant nsp1β recovered from infectious cDNA clone was shown to be attenuated for growth in vitro and induced significantly higher amount of type I IFN transcripts in infected macrophages. In infected pigs, the 16-5A virus exhibited reduced growth at early times after infection but quickly regained wild type growth properties as a result of substitutions within the mutated sequences. The results indicate a strong selection pressure towards maintaining the IFN-inhibitory property of the virus for successful propagation in pigs. Elsevier Inc. 2012-11-25 2012-09-18 /pmc/articles/PMC7111991/ /pubmed/22995188 http://dx.doi.org/10.1016/j.virol.2012.08.034 Text en Copyright © 2012 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 Beura, Lalit K. Subramaniam, Sakthivel Vu, Hiep L.X. Kwon, Byungjoon Pattnaik, Asit K. Osorio, Fernando A. Identification of amino acid residues important for anti-IFN activity of porcine reproductive and respiratory syndrome virus non-structural protein 1 |
title | Identification of amino acid residues important for anti-IFN activity of porcine reproductive and respiratory syndrome virus non-structural protein 1 |
title_full | Identification of amino acid residues important for anti-IFN activity of porcine reproductive and respiratory syndrome virus non-structural protein 1 |
title_fullStr | Identification of amino acid residues important for anti-IFN activity of porcine reproductive and respiratory syndrome virus non-structural protein 1 |
title_full_unstemmed | Identification of amino acid residues important for anti-IFN activity of porcine reproductive and respiratory syndrome virus non-structural protein 1 |
title_short | Identification of amino acid residues important for anti-IFN activity of porcine reproductive and respiratory syndrome virus non-structural protein 1 |
title_sort | identification of amino acid residues important for anti-ifn activity of porcine reproductive and respiratory syndrome virus non-structural protein 1 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111991/ https://www.ncbi.nlm.nih.gov/pubmed/22995188 http://dx.doi.org/10.1016/j.virol.2012.08.034 |
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