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A single amino acid substitution in the V protein of Nipah virus alters its ability to block interferon signalling in cells from different species
The V protein of the paramyxovirus Nipah virus (NiV) has been shown to antagonize the interferon (IFN) response in human cells via sequestration of STAT1 and STAT2. This study describes a mutant of the NiV V protein, referred to as V(AAHL), that is unable to antagonize IFN signalling and demonstrate...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Society for General Microbiology
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2884973/ https://www.ncbi.nlm.nih.gov/pubmed/17098981 http://dx.doi.org/10.1099/vir.0.82261-0 |
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author | Hagmaier, Kathrin Stock, Nicola Goodbourn, Steve Wang, Lin-Fa Randall, Richard |
author_facet | Hagmaier, Kathrin Stock, Nicola Goodbourn, Steve Wang, Lin-Fa Randall, Richard |
author_sort | Hagmaier, Kathrin |
collection | PubMed |
description | The V protein of the paramyxovirus Nipah virus (NiV) has been shown to antagonize the interferon (IFN) response in human cells via sequestration of STAT1 and STAT2. This study describes a mutant of the NiV V protein, referred to as V(AAHL), that is unable to antagonize IFN signalling and demonstrates that a single amino acid substitution is responsible for its inactivity. The molecular basis for this was identified as a failure to interact with STAT1 and STAT2. It was also shown that NiV V, but not V(AAHL), was functional as an IFN antagonist in human, monkey, rabbit, dog, horse, pig and bat cells, which suggests that the ability of NiV to block IFN signalling is not a major constraint that prevents this virus from crossing species barriers. |
format | Text |
id | pubmed-2884973 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | Society for General Microbiology |
record_format | MEDLINE/PubMed |
spelling | pubmed-28849732010-07-06 A single amino acid substitution in the V protein of Nipah virus alters its ability to block interferon signalling in cells from different species Hagmaier, Kathrin Stock, Nicola Goodbourn, Steve Wang, Lin-Fa Randall, Richard J Gen Virol Animal The V protein of the paramyxovirus Nipah virus (NiV) has been shown to antagonize the interferon (IFN) response in human cells via sequestration of STAT1 and STAT2. This study describes a mutant of the NiV V protein, referred to as V(AAHL), that is unable to antagonize IFN signalling and demonstrates that a single amino acid substitution is responsible for its inactivity. The molecular basis for this was identified as a failure to interact with STAT1 and STAT2. It was also shown that NiV V, but not V(AAHL), was functional as an IFN antagonist in human, monkey, rabbit, dog, horse, pig and bat cells, which suggests that the ability of NiV to block IFN signalling is not a major constraint that prevents this virus from crossing species barriers. Society for General Microbiology 2006-12 /pmc/articles/PMC2884973/ /pubmed/17098981 http://dx.doi.org/10.1099/vir.0.82261-0 Text en Copyright © 2006, SGM http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Animal Hagmaier, Kathrin Stock, Nicola Goodbourn, Steve Wang, Lin-Fa Randall, Richard A single amino acid substitution in the V protein of Nipah virus alters its ability to block interferon signalling in cells from different species |
title | A single amino acid substitution in the V protein of Nipah virus alters its ability to block interferon signalling in cells from different species |
title_full | A single amino acid substitution in the V protein of Nipah virus alters its ability to block interferon signalling in cells from different species |
title_fullStr | A single amino acid substitution in the V protein of Nipah virus alters its ability to block interferon signalling in cells from different species |
title_full_unstemmed | A single amino acid substitution in the V protein of Nipah virus alters its ability to block interferon signalling in cells from different species |
title_short | A single amino acid substitution in the V protein of Nipah virus alters its ability to block interferon signalling in cells from different species |
title_sort | single amino acid substitution in the v protein of nipah virus alters its ability to block interferon signalling in cells from different species |
topic | Animal |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2884973/ https://www.ncbi.nlm.nih.gov/pubmed/17098981 http://dx.doi.org/10.1099/vir.0.82261-0 |
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