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influenza ns1

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https://www.readbyqxmd.com/read/29034629/-comparison-of-cellular-localization-of-ns1-from-different-subtypes-of-influenza-a-virus
#1
Meng Yu, Shuaishuai Cao, Weinan Zheng, Xiaoxiao Jia, Jing Li, Wenjun Liu
The non-structural (NS1) protein is a multifunctional molecular protein encoded by influenza A virus genome. NS1 plays an important role in inhibition of host immune responses. In order to assess the cellular localization of NS1 in different influenza A virus subtypes, we performed the immunofluorescence assay to observe the cellular location of NS1 after infection with influenza A virus WSN (H1N1), PR8 (H1N1), CA04 (H1N1), SD (H9N2) and AH01 (H7N9) in A549 cells and MDCK cells respectively. According to the results, NS1-WSN and NS1-PR8 accumulated mainly in cytoplasm at 24 h post infection, while the NS1-CA04 and NS1-SD appeared major in the nucleus...
November 25, 2016: Sheng Wu Gong Cheng Xue Bao, Chinese Journal of Biotechnology
https://www.readbyqxmd.com/read/28992616/ns1-of-h7n9-influenza-a-virus-induces-no-mediated-cellular-senescence-in-neuro2a-cells
#2
Yinxia Yan, Yongming Du, Huali Zheng, Gefei Wang, Rui Li, Jieling Chen, Kangsheng Li
BACKGROUND/AIMS: The novel avian H7N9 influenza A virus has been detected in brain tissues and associated with central nervous system (CNS) symptoms in infected human and mice. Roles of its virulence factor, NS1 protein in influenza virus infected neuron has yet to be explored. METHODS: Nitric oxide (NO) release and inducible nitric oxide synthase (iNOS) expression in H7N9/NS1-expressed Neuro2a cells were detected by Griess test and western blotting. Cell proliferation rate of H7N9/NS1-expressing cells was recorded by Cell Counting Kit-8...
October 9, 2017: Cellular Physiology and Biochemistry
https://www.readbyqxmd.com/read/28955326/influenza-a-virus-pa-antagonizes-interferon-%C3%AE-by-interacting-with-interferon-regulatory-factor-3
#3
Chenyang Yi, Zongzheng Zhao, Shengyu Wang, Xin Sun, Dan Zhang, Xiaomei Sun, Anding Zhang, Meilin Jin
The influenza A virus (IAV) can be recognized by retinoic acid-inducible gene I (RIG-I) to activate the type I interferon response and induce antiviral effects. The virus has evolved several strategies to evade the innate immune response, including non-structural protein 1 (NS1) and its polymerase subunits. The mechanism by which NS1 inhibits interferon-β (IFN-β) is well understood, whereas the mechanism by which polymerase acid protein (PA) inhibits IFN-β remains to be elucidated. In this study, we observed that the IAV PA protein could inhibit the production of IFN-β and interferon-stimulated genes induced by Sendai virus through interferon regulatory factor 3 (IRF3), but not through nuclear factor-kappaB (NF-kappaB)...
2017: Frontiers in Immunology
https://www.readbyqxmd.com/read/28953980/influenza-virus-differentially-activates-mtorc1-and-mtorc2-signaling-to-maximize-late-stage-replication
#4
Sharon K Kuss-Duerkop, Juan Wang, Ignacio Mena, Kris White, Giorgi Metreveli, Ramanavelan Sakthivel, Miguel A Mata, Raquel Muñoz-Moreno, Xiang Chen, Florian Krammer, Michael S Diamond, Zhijian J Chen, Adolfo García-Sastre, Beatriz M A Fontoura
Influenza A virus usurps host signaling factors to regulate its replication. One example is mTOR, a cellular regulator of protein synthesis, growth and motility. While the role of mTORC1 in viral infection has been studied, the mechanisms that induce mTORC1 activation and the substrates regulated by mTORC1 during influenza virus infection have not been established. In addition, the role of mTORC2 during influenza virus infection remains unknown. Here we show that mTORC2 and PDPK1 differentially phosphorylate AKT upon influenza virus infection...
September 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/28940727/whole-genome-sequencing-and-antigenic-analysis-of-the-first-equine-influenza-virus-identified-in-turkey
#5
Jacinta Gahan, Marie Garvey, Sarah Gildea, Gildea Gür, Anil Kagankaya, Ann Cullinane
BACKGROUND: In 2013 there was an outbreak of acute respiratory disease in racehorses in Turkey. The clinical signs were consistent with equine influenza (EI). OBJECTIVE: The aim was to confirm the cause of the outbreak and characterise the causal virus. METHODS: A pan-reactive influenza type A real time RT-PCR and a rapid antigen detection kit were used for confirmatory diagnosis of equine influenza virus (EIV). Immunological susceptibility to EIV was examined using Single Radial Haemolysis and ELISA...
September 21, 2017: Influenza and Other Respiratory Viruses
https://www.readbyqxmd.com/read/28903072/the-role-of-nuclear-ns1-protein-in-highly-pathogenic-h5n1-influenza-viruses
#6
Bobo Wing-Yee Mok, Honglian Liu, Pin Chen, Siwen Liu, Siu-Ying Lau, Xiaofeng Huang, Yen-Chin Liu, Pui Wang, Kwok-Yung Yuen, Honglin Chen
The non-structural protein (NS1) of influenza A viruses (IAV) performs multiple functions during viral infection. NS1 contains two nuclear localization signals (NLS): NLS1 and NLS2. The NS1 protein is located predominantly in the nucleus during the early stages of infection and subsequently exported to the cytoplasm. A nonsense mutation that results in a large deletion in the carboxy-terminal region of the NS1 protein that contains the NLS2 domain was found in some IAV subtypes, including highly pathogenic avian influenza (HPAI) H7N9 and H5N1 viruses...
September 10, 2017: Microbes and Infection
https://www.readbyqxmd.com/read/28893180/annexin-a2-anxa2-interacts-with-nonstructural-protein-1-and-promotes-the-replication-of-highly-pathogenic-h5n1-avian-influenza-virus
#7
Yong Ma, Jiashan Sun, Linlin Gu, Hongmei Bao, Yuhui Zhao, Lin Shi, Wei Yao, Guobin Tian, Xiurong Wang, Hualan Chen
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...
September 11, 2017: BMC Microbiology
https://www.readbyqxmd.com/read/28892164/mcpip1-attenuates-the-innate-immune-response-to-influenza-a-viruse-by-suppressing-rig-i-expression-in-lung-epithelial-cells
#8
Xiaoning Sun, Wenjing Feng, Yidi Guo, Qi Wang, Chunyan Dong, Maolin Zhang, Zhenhong Guan, Ming Duan
The pattern recognition receptor retinoic acid-inducible gene I (RIG-I) reportedly plays a key role in sensing influenza A virus (IAV) infection and activating type I interferon (IFN) response. MCP-1-induced protein 1 (MCPIP1) can directly degrade cytokine mRNAs, such as IL-6, IL-12, IL-1β and IL-2, by functioning as an RNase. Here, we initially observed that MCPIP1 exhibited virus supportive functions later in the course of IAV infection in A549 cells, and negatively regulated IAV-induced RIG-I-dependent innate antiviral response...
September 11, 2017: Journal of Medical Virology
https://www.readbyqxmd.com/read/28878070/effect-of-the-phosphorylation-of-the-cm2-protein-on-influenza-c-virus-replication
#9
Takanari Goto, Yoshitaka Shimotai, Yoko Matsuzaki, Yasushi Muraki, Ri Sho, Kanetsu Sugawara, Seiji Hongo
CM2 is the second membrane protein of the influenza C virus and has been demonstrated to play a role in the uncoating and genome packaging processes in influenza C virus replication. Although the effects of N-linked glycosylation, disulfide-linked oligomerization, and palmitoylation of CM2 on virus replication have been analyzed, the effect of the phosphorylation of CM2 on virus replication remains to be determined. In this study, phosphorylation site(s) at residues 78 and/or 103 of CM2 were substituted with alanine residue(s) and the effects of the loss of phosphorylation on influenza C virus replication were analyzed...
September 6, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28874549/molecular-basis-of-mammalian-transmissibility-of-avian-h1n1-influenza-viruses-and-their-pandemic-potential
#10
Mark Zanin, Sook-San Wong, Subrata Barman, Challika Kaewborisuth, Peter Vogel, Adam Rubrum, Daniel Darnell, Atanaska Marinova-Petkova, Scott Krauss, Richard J Webby, Robert G Webster
North American wild birds are an important reservoir of influenza A viruses, yet the potential of viruses in this reservoir to transmit and cause disease in mammals is not well understood. Our surveillance of avian influenza viruses (AIVs) at Delaware Bay, USA, revealed a group of similar H1N1 AIVs isolated in 2009, some of which were airborne-transmissible in the ferret model without prior adaptation. Comparison of the genomes of these viruses revealed genetic markers of airborne transmissibility in the Polymerase Basic 2 (PB2), PB1, PB1-F2, Polymerase Acidic-X (PA-X), Nonstructural Protein 1 (NS1), and Nuclear Export Protein (NEP) genes...
September 5, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28869005/human-interactome-of-the-influenza-b-virus-ns1-protein
#11
Corinna Patzina, Catherine H Botting, Adolfo García-Sastre, Richard E Randall, Benjamin G Hale
NS1 proteins of influenza A and B viruses share limited sequence homology, yet both are potent manipulators of host cell processes, particularly interferon (IFN) induction. Although many cellular partners are reported for A/NS1, only a few (e.g. PKR and ISG15) have been identified for B/NS1. Here, affinity-purification and mass spectrometry were used to expand the known host interactome of B/NS1. We identified 22 human proteins as new putative targets for B/NS1, validating several, including DHX9, ILF3, YBX1 and HNRNPC...
September 2017: Journal of General Virology
https://www.readbyqxmd.com/read/28837667/influenza-ns1-directly-modulates-hedgehog-signaling-during-infection
#12
Margery G Smelkinson, Annabel Guichard, John R Teijaro, Meghana Malur, Maria Eugenia Loureiro, Prashant Jain, Sundar Ganesan, Elina I Zúñiga, Robert M Krug, Michael B Oldstone, Ethan Bier
The multifunctional NS1 protein of influenza A viruses suppresses host cellular defense mechanisms and subverts other cellular functions. We report here on a new role for NS1 in modifying cell-cell signaling via the Hedgehog (Hh) pathway. Genetic epistasis experiments and FRET-FLIM assays in Drosophila suggest that NS1 interacts directly with the transcriptional mediator, Ci/Gli1. We further confirmed that Hh target genes are activated cell-autonomously in transfected human lung epithelial cells expressing NS1, and in infected mouse lungs...
August 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/28835506/amino-acid-substitution-k186e-in-the-canine-influenza-virus-h3n8-ns1-protein-restores-its-ability-to-inhibit-host-gene-expression
#13
Aitor Nogales, Caroline Chauché, Marta L DeDiego, David J Topham, Colin R Parrish, Pablo R Murcia, Luis Martínez-Sobrido
Canine influenza viruses (CIVs) are the causative agents of canine influenza, a contagious respiratory disease in dogs, and include the equine-origin H3N8 and the avian-origin H3N2. Influenza A virus (IAV) non-structural protein 1 (NS1) is a virulence factor essential for counteracting the innate immune response. Here, we evaluated the ability of H3N8 CIV NS1 to inhibit host innate immune responses. We found that H3N8 CIV NS1 was able to efficiently counteract interferon (IFN) responses but was unable to block general gene expression in human or canine cells...
August 23, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28814525/structure-guided-functional-annotation-of-the-influenza-a-virus-ns1-protein-reveals-dynamic-evolution-of-the-p85%C3%AE-binding-site-during-circulation-in-humans
#14
Antonio M Lopes, Patricia Domingues, Roland Zell, Benjamin G Hale
Rational characterization of virulence and host-adaptive markers in the multifunctional influenza A virus NS1 protein is hindered by a lack of comprehensive knowledge about NS1-host protein protein interfaces. Here, we surveyed the impact of amino acid variation in NS1 at its structurally defined binding site for host p85β, a regulator of phosphoinositide 3-kinase (PI3K) signaling. Structure-guided alanine scanning of all viral residues at this interface defined 10 positions contributing to the interaction, with residues 89, 95, 98, 133, 145, and 162 being the most important...
November 1, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28796576/antibody-affinity-against-2009-a-h1n1-influenza-and-pandemrix-vaccine-nucleoproteins-differs-between-childhood-narcolepsy-patients-and-controls
#15
Alexander Lind, Eva Freyhult, Anita Ramelius, Tomas Olsson, Lisen Arnheim-Dahlström, Favelle Lamb, Mohsen Khademi, Aditya Ambati, Markus Maeurer, Izaura Lima Bomfim, Katharina Fink, Malin Fex, Carina Törn, Helena Elding Larsson, Åke Lernmark
Increased narcolepsy incidence was observed in Sweden following the 2009 influenza vaccination with Pandemrix(®). A substitution of the 2009 nucleoprotein for the 1934 variant has been implicated in narcolepsy development. The aims were to determine (a) antibody levels toward wild-type A/H1N1-2009[A/California/04/2009(H1N1)] (NP-CA2009) and Pandemrix-[A/Puerto Rico/8/1934(H1N1)] (NP-PR1934) nucleoproteins in 43 patients and 64 age-matched controls; (b) antibody affinity in reciprocal competitive assays in 11 childhood narcolepsy patients compared with 21 age-matched controls; and (c) antibody levels toward wild-type A/H1N1-2009[A/California/04/2009(H1N1)] (H1N1 NS1), not a component of the Pandemrix vaccine...
October 2017: Viral Immunology
https://www.readbyqxmd.com/read/28765967/influenza-virus-non%C3%A2-structural-protein-1-inhibits-the-production-of-interferon-%C3%AE-of-alveolar-epithelial-cells-upon-the-infection-of-influenza-a-h1n1
#16
Hao Jiang, Si-Mei Shen, Jie Yin, Peng-Peng Zhang, Yi Shi
Influenza A affects a large population worldwide. Influenza virus evades immune responses via various mechanisms, including through the modification of the immune microenvironment. Influenza virus non‑structural protein 1 (NS1) encoded by the virus genome inhibits type I interferon (IFN) signaling pathways, which is essential for viral clearance. However, the precise mechanisms of NS1‑mediated immune suppression remain poorly understood. The results of the present study demonstrated that mice infected with NS1‑expressing influenza A H1N1 virus had lower expression levels of IFNβ in the lung...
October 2017: Molecular Medicine Reports
https://www.readbyqxmd.com/read/28757142/influenza-virus-ns1-protein-mutations-at-position-171-impact-innate-interferon-responses-by-respiratory-epithelial-cells
#17
Ewan P Plant, Natalia A Ilyushina, Faruk Sheikh, Raymond P Donnelly, Zhiping Ye
The influenza virus NS1 protein interacts with a wide range of proteins to suppress the host cell immune response and facilitate virus replication. The amino acid sequence of the 2009 pandemic virus NS1 protein differed from sequences of earlier related viruses. The functional impact of these differences has not been fully defined. Therefore, we made mutations to the NS1 protein based on these sequence differences, and assessed the impact of these changes on host cell interferon (IFN) responses. We found that viruses with mutations at position 171 replicated efficiently but did not induce expression of interferon genes as effectively as wild-type viruses in A459 lung epithelial cells...
July 27, 2017: Virus Research
https://www.readbyqxmd.com/read/28717359/the-c-terminal-effector-domain-of-non-structural-protein-1-of-influenza-a-virus-blocks-ifn-%C3%AE-production-by-targeting-tnf-receptor-associated-factor-3
#18
Wei Qian, Xiaoqin Wei, Kelei Guo, Yongtao Li, Xian Lin, Zhong Zou, Hongbo Zhou, Meilin Jin
Influenza A virus non-structural protein 1 (NS1) antagonizes interferon response through diverse strategies, particularly by inhibiting the activation of interferon regulatory factor 3 (IRF3) and IFN-β transcription. However, the underlying mechanisms used by the NS1 C-terminal effector domain (ED) to inhibit the activation of IFN-β pathway are not well understood. In this study, we used influenza virus subtype of H5N1 to demonstrate that the NS1 C-terminal ED but not the N-terminal RNA-binding domain, binds TNF receptor-associated factor 3 (TRAF3)...
2017: Frontiers in Immunology
https://www.readbyqxmd.com/read/28696227/translational-regulation-of-viral-secretory-proteins-by-the-5-coding-regions-and-a-viral-rna-binding-protein
#19
Johan Nordholm, Jeanne Petitou, Henrik Östbye, Diogo V da Silva, Dan Dou, Hao Wang, Robert Daniels
A primary function of 5' regions in many secretory protein mRNAs is to encode an endoplasmic reticulum (ER) targeting sequence. In this study, we show how the regions coding for the ER-targeting sequences of the influenza glycoproteins NA and HA also function as translational regulatory elements that are controlled by the viral RNA-binding protein (RBP) NS1. The translational increase depends on the nucleotide composition and 5' positioning of the ER-targeting sequence coding regions and is facilitated by the RNA-binding domain of NS1, which can associate with ER membranes...
August 7, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28659900/efficacy-of-live-attenuated-h9n2-influenza-vaccine-candidates-containing-ns1-truncations-against-h9n2-avian-influenza-viruses
#20
Sujuan Chen, Yinbiao Zhu, Da Yang, Yang Yang, Shaohua Shi, Tao Qin, Daxin Peng, Xiufan Liu
H9N2 avian influenza virus is a zoonotic agent with a broad host range that can contribute genetic information to H5 or H7N9 subtype viruses, which are significant threats to both humans and birds. Thus, there is a great need for a vaccine to control H9N2 avian influenza. Three mutant viruses of an H9N2 virus A/chicken/Taixing/10/2010 (rTX-NS1-73, rTX-NS1-100, and rTX-NS1-128) were constructed with different NS1 gene truncations and confirmed by western blot analysis. The genetic stability, pathogenicity, transmissibility, and host immune responses toward these mutants were evaluated...
2017: Frontiers in Microbiology
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