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A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence
Although an effective interferon antagonist in human and avian cells, the novel H7N9 influenza virus NS1 protein is defective at inhibiting CPSF30. An I106M substitution in H7N9 NS1 can restore CPSF30 binding together with the ability to block host gene expression. Furthermore, a recombinant virus e...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Microbiology
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4178744/ https://www.ncbi.nlm.nih.gov/pubmed/25078692 http://dx.doi.org/10.1128/JVI.01567-14 |
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author | Ayllon, Juan Domingues, Patricia Rajsbaum, Ricardo Miorin, Lisa Schmolke, Mirco Hale, Benjamin G. García-Sastre, Adolfo |
author_facet | Ayllon, Juan Domingues, Patricia Rajsbaum, Ricardo Miorin, Lisa Schmolke, Mirco Hale, Benjamin G. García-Sastre, Adolfo |
author_sort | Ayllon, Juan |
collection | PubMed |
description | Although an effective interferon antagonist in human and avian cells, the novel H7N9 influenza virus NS1 protein is defective at inhibiting CPSF30. An I106M substitution in H7N9 NS1 can restore CPSF30 binding together with the ability to block host gene expression. Furthermore, a recombinant virus expressing H7N9 NS1-I106M replicates to higher titers in vivo, and is subtly more virulent, than the parental virus. Natural polymorphisms in H7N9 NS1 that enhance CPSF30 binding may be cause for concern. |
format | Online Article Text |
id | pubmed-4178744 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American Society for Microbiology |
record_format | MEDLINE/PubMed |
spelling | pubmed-41787442015-04-01 A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence Ayllon, Juan Domingues, Patricia Rajsbaum, Ricardo Miorin, Lisa Schmolke, Mirco Hale, Benjamin G. García-Sastre, Adolfo J Virol Pathogenesis and Immunity Although an effective interferon antagonist in human and avian cells, the novel H7N9 influenza virus NS1 protein is defective at inhibiting CPSF30. An I106M substitution in H7N9 NS1 can restore CPSF30 binding together with the ability to block host gene expression. Furthermore, a recombinant virus expressing H7N9 NS1-I106M replicates to higher titers in vivo, and is subtly more virulent, than the parental virus. Natural polymorphisms in H7N9 NS1 that enhance CPSF30 binding may be cause for concern. American Society for Microbiology 2014-10 /pmc/articles/PMC4178744/ /pubmed/25078692 http://dx.doi.org/10.1128/JVI.01567-14 Text en Copyright © 2014 Ayllon et al. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution 3.0 Unported license (http://creativecommons.org/licenses/by/3.0/) . |
spellingShingle | Pathogenesis and Immunity Ayllon, Juan Domingues, Patricia Rajsbaum, Ricardo Miorin, Lisa Schmolke, Mirco Hale, Benjamin G. García-Sastre, Adolfo A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence |
title | A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence |
title_full | A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence |
title_fullStr | A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence |
title_full_unstemmed | A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence |
title_short | A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence |
title_sort | single amino acid substitution in the novel h7n9 influenza a virus ns1 protein increases cpsf30 binding and virulence |
topic | Pathogenesis and Immunity |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4178744/ https://www.ncbi.nlm.nih.gov/pubmed/25078692 http://dx.doi.org/10.1128/JVI.01567-14 |
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