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Annexin A2 (ANXA2) interacts with nonstructural protein 1 and promotes the replication of highly pathogenic H5N1 avian influenza virus
BACKGROUND: Non-structural protein 1 (NS1) is a multifunctional protein and a crucial regulatory factor in the replication and pathogenesis of avian influenza virus (AIV). Studies have shown that NS1 can interact with a variety of host proteins to modulate the viral life cycle. We previously generat...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5594581/ https://www.ncbi.nlm.nih.gov/pubmed/28893180 http://dx.doi.org/10.1186/s12866-017-1097-0 |
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author | Ma, Yong Sun, Jiashan Gu, Linlin Bao, Hongmei Zhao, Yuhui Shi, Lin Yao, Wei Tian, Guobin Wang, Xiurong Chen, Hualan |
author_facet | Ma, Yong Sun, Jiashan Gu, Linlin Bao, Hongmei Zhao, Yuhui Shi, Lin Yao, Wei Tian, Guobin Wang, Xiurong Chen, Hualan |
author_sort | Ma, Yong |
collection | PubMed |
description | BACKGROUND: Non-structural protein 1 (NS1) is a multifunctional protein and a crucial regulatory factor in the replication and pathogenesis of avian influenza virus (AIV). Studies have shown that NS1 can interact with a variety of host proteins to modulate the viral life cycle. We previously generated a monoclonal antibody against NS1 protein; In the current research study, using this antibody, we immunoprecipitated host proteins that interact with NS1 to better understand the roles played by NS1 in communications between virus and host. RESULTS: Co-immunoprecipitation experiments identified annexin A2 (ANXA2) as a target molecule interacting with NS1. Results from confocal laser scanning microscopy indicated that NS1 co-localized with ANXA2 in the cell cytoplasm. Overexpression of ANXA2 significantly increased the titer of H5N1 subtype HPAIV, whereas siRNA-mediated knockdown of ANXA2 markedly inhibited the expression of viral proteins and reduced the progeny virus titer. CONCLUSIONS: Our results indicate that ANXA2 interacts with NS1 and ANXA2 expression increases HPAIV replication. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12866-017-1097-0) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5594581 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-55945812017-09-15 Annexin A2 (ANXA2) interacts with nonstructural protein 1 and promotes the replication of highly pathogenic H5N1 avian influenza virus Ma, Yong Sun, Jiashan Gu, Linlin Bao, Hongmei Zhao, Yuhui Shi, Lin Yao, Wei Tian, Guobin Wang, Xiurong Chen, Hualan BMC Microbiol Research Article BACKGROUND: Non-structural protein 1 (NS1) is a multifunctional protein and a crucial regulatory factor in the replication and pathogenesis of avian influenza virus (AIV). Studies have shown that NS1 can interact with a variety of host proteins to modulate the viral life cycle. We previously generated a monoclonal antibody against NS1 protein; In the current research study, using this antibody, we immunoprecipitated host proteins that interact with NS1 to better understand the roles played by NS1 in communications between virus and host. RESULTS: Co-immunoprecipitation experiments identified annexin A2 (ANXA2) as a target molecule interacting with NS1. Results from confocal laser scanning microscopy indicated that NS1 co-localized with ANXA2 in the cell cytoplasm. Overexpression of ANXA2 significantly increased the titer of H5N1 subtype HPAIV, whereas siRNA-mediated knockdown of ANXA2 markedly inhibited the expression of viral proteins and reduced the progeny virus titer. CONCLUSIONS: Our results indicate that ANXA2 interacts with NS1 and ANXA2 expression increases HPAIV replication. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12866-017-1097-0) contains supplementary material, which is available to authorized users. BioMed Central 2017-09-11 /pmc/articles/PMC5594581/ /pubmed/28893180 http://dx.doi.org/10.1186/s12866-017-1097-0 Text en © The Author(s). 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Ma, Yong Sun, Jiashan Gu, Linlin Bao, Hongmei Zhao, Yuhui Shi, Lin Yao, Wei Tian, Guobin Wang, Xiurong Chen, Hualan Annexin A2 (ANXA2) interacts with nonstructural protein 1 and promotes the replication of highly pathogenic H5N1 avian influenza virus |
title | Annexin A2 (ANXA2) interacts with nonstructural protein 1 and promotes the replication of highly pathogenic H5N1 avian influenza virus |
title_full | Annexin A2 (ANXA2) interacts with nonstructural protein 1 and promotes the replication of highly pathogenic H5N1 avian influenza virus |
title_fullStr | Annexin A2 (ANXA2) interacts with nonstructural protein 1 and promotes the replication of highly pathogenic H5N1 avian influenza virus |
title_full_unstemmed | Annexin A2 (ANXA2) interacts with nonstructural protein 1 and promotes the replication of highly pathogenic H5N1 avian influenza virus |
title_short | Annexin A2 (ANXA2) interacts with nonstructural protein 1 and promotes the replication of highly pathogenic H5N1 avian influenza virus |
title_sort | annexin a2 (anxa2) interacts with nonstructural protein 1 and promotes the replication of highly pathogenic h5n1 avian influenza virus |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5594581/ https://www.ncbi.nlm.nih.gov/pubmed/28893180 http://dx.doi.org/10.1186/s12866-017-1097-0 |
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