Skip to main content
Key Specialties
Cardiology Diabetology Endocrinology Gastroenterology Geriatrics and Gerontology Gynecology and Obstetrics Hematology Infectious Disease Internal Medicine Nephrology Neurology Oncology Pediatrics Respiratory Medicine Rheumatology Surgery
Congress Coverage
2024 ACC Congress 2023 ESMO Congress 2023 EASD Congress 2023 ERS Congress 2023 ESC Congress
Clinical Collections
Advances in Alzheimer’s

Keynote webinar | Spotlight on medication adherence

LIVE: Thursday 27th June 2024, 18:00-19:30 (CEST)
Join our expert panel to discover why you need to understand the drivers of non-adherence in your patients, and how you can optimize medication adherence in your clinics to drastically improve patient outcomes.
ADVANCED SEARCH
Log in
Top
Virology Journal
Published in: Virology Journal 1/2011

Open Access 01-12-2011 | Research

The interaction between the PARP10 protein and the NS1 protein of H5N1 AIV and its effect on virus replication

Authors: Mengbin Yu, Chuanfu Zhang, Yutao Yang, Zhixin Yang, Lixia Zhao, Long Xu, Rong Wang, Xiaowei Zhou, Peitang Huang

Published in: Virology Journal | Issue 1/2011

Login to get access

Abstract

Background

During the process that AIV infect hosts, the NS1 protein can act on hosts, change corresponding signal pathways, promote the translation of virus proteins and result in virus replication.

Results

In our study, we found that PARP domain and Glu-rich region of PARP10 interacted with NS1, and the presence of NS1 could induce PARP10 migrate from cytoplasm to nucleus. NS1 high expression could reduce the endogenous PARP10 expression. Cell cycle analysis showed that with inhibited PARP10 expression, NS1 could induce cell arrest in G2-M stage, and the percentage of cells in G2-M stage rise from the previous 10%-45%, consistent with the cell proliferation result. Plague forming unit measurement showed that inhibited PARP10 expression could help virus replication.

Conclusions

In a word, our results showed that NS1 acts on host cells and PARP10 plays a regulating role in virus replication.
Appendix
Available only for authorised users
Literature
1.
Akarsu H, Burmeister WP, Petosa C, Petit I, Müller CW, Ruigrok RW, Baudin F: Crystal structure of the M1 protein-binding domain of the influenza A nuclear export protein (NEP/NS2). EMBO J 2003,22(18):4646-4655. 10.1093/emboj/cdg449PubMedCentralCrossRefPubMed
2.
Geiss GK, Salvatore M, Tumpey TM, Carter VS, Wang X, Basler CF, Taubenberger JK, Bumgarner RE, Palese P, Katze MG, García-Sastre A: Cellular transcriptional profiling in influenza A virus-infected lung epithelial cells: The role of the nonstructural NS1 protein in the evasion of the host innate defense and its potential contribution to pandemic influenza. PNAS 2002, 99: 10736-10741. 10.1073/pnas.112338099PubMedCentralCrossRefPubMed
3.
Qiu Y, Krug RM: The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear export of mRNAs containing poly(A). J Virol 1994,68(4):2425-2432.PubMedCentralPubMed
4.
Qian XY, Alonso-Caplen F, Krug RM: Two functional domains of the influenza virus NS1 protein are required for regulation of nuclear export of mRNA. J Virol 1994,68(4):2433-2441.PubMedCentralPubMed
5.
Nemeroff ME, Barabino SM, Li Y, Keller W, Krug RM: Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs. Mol Cell 1998,1(7):991-1000. 10.1016/S1097-2765(00)80099-4CrossRefPubMed
6.
Lu Y, Qian XY, Kurg RM: The influenza virus NS1 protein: a novel inhibitor of pre-mRNA splicing. Genes Dov 1994,8(15):1817-1828. 10.1101/gad.8.15.1817CrossRef
7.
Benjamin GH, Richard ER, Juan O, David J: The multifunctional NS1 protein of influenza A viruses. J Gen Virol 2008, 89: 2359-2376. 10.1099/vir.0.2008/004606-0CrossRef
8.
García-Sastre A: Inhibition of interferon-mediated antiviral responses by Influenza a viruses and other negative strand RNA viruses. Virol 2001, 279: 375-384. 10.1006/viro.2000.0756CrossRef
9.
D'Amours D, Desnoyers S, D'Silva I, Poirier GG: Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem J 1999, 342: 249-268. 10.1042/0264-6021:3420249PubMedCentralCrossRefPubMed
10.
Mortusewicz O, Amé JC, Schreiber V, Leonhardt H: Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells. Nucleic Acids Res 2007,35(22):7665-7675. 10.1093/nar/gkm933PubMedCentralCrossRefPubMed
11.
Horton JK, Watson M, Stefanick DF, Shaughnessy DT, Taylor JA, Wilson SH: XRCC1 and DNA polymerase β in cellular protection against cytotoxic DNA single-strand breaks. Cell Res 2008,18(1):48-63. 10.1038/cr.2008.7PubMedCentralCrossRefPubMed
12.
Wacker DA, Ruhl DD, Balagamwala EH, Hope KM, Zhang T, Kraus WL: The DNA binding and catalytic domains of poly(ADP-Ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription. Mol Cell Biol 2007,27(21):7475-7485. 10.1128/MCB.01314-07PubMedCentralCrossRefPubMed
13.
Saenz L, Lozano JJ, Valdor R, Baroja-Mazo A, Ramirez P, Parrilla P, Aparicio P, Sumoy L, Yélamos J: Transcriptional regulation by poly(ADP-ribose) polymerase-1 during T cell activation. BMC Genomics 2008,9(171):1-11.
14.
Choi HS, Hwang CK, Kim CS, Song KY, Law PY, Loh HH, Wei LN: Transcriptional regulation of mouse mu opioid receptor gene in neuronal cells by Poly(ADP-ribose) polymerase-1. J Cell Mol Med 2008,12(6A):2319-33. 10.1111/j.1582-4934.2008.00259.xPubMedCentralCrossRefPubMed
15.
Augustin A, Spenlehauer C, Dumond H, Ménissier-De Murcia J, Piel M, Schmit AC, Apiou F, Vonesch JL, Kock M, Bornens M, De Murcia G: PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression. J Cell Sci 2003,116(8):1551-1562. 10.1242/jcs.00341CrossRefPubMed
16.
Yu M, Schreek S, Cerni C, Schamberger C, Lesniewicz K, Poreba E, Vervoorts J, Walsemann G, Grötzinger J, Kremmer E, Mehraein Y, Mertsching J, Kraft R, Austen M, Lüscher-Firzlaff J, Lüscher B: PARP-10, a novel Myc- interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation. Oncogene 2005, 24: 1982-1993. 10.1038/sj.onc.1208410CrossRefPubMed
17.
Yu SW, Andrabi SA, Wang H, Kim NS, Poirier GG, Dawson TM, Dawson VL: Apoptosis-inducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death. PNAS 2006,103(48):18314-18319. 10.1073/pnas.0606528103PubMedCentralCrossRefPubMed
18.
Mok CK, Lee DC, Cheung CY, Peiris M, Lau AS: Differential onset of apoptosis in influenza A virus H5N1- and H1N1-infected human blood Macrophages. J Gen Virol 2007, 88: 1275-1280. 10.1099/vir.0.82423-0CrossRefPubMed
19.
Mattiussi S, Tempera I, Matusali G, Mearini G, Lenti L, Fratarcangeli S, Mosca L, D'Erme M, Mattia E: Inhibition of Poly(ADP-ribose)polymerase impairs Epstein Barr Virus lytic cycle progression. Infectious Agents and Cancer 2007,2(18):1-9.
20.
Aldinucci A, Gerlini G, Fossati S, Cipriani G, Ballerini C, Biagioli T, Pimpinelli N, Borgognoni L, Massacesi L, Moroni F, Chiarugi A: A key role for poly(ADP-Ribose) polymerase-1 activity during human dendritic cell maturation. The J Immunol 2007, 179: 305-312.CrossRefPubMed
21.
Ratnam K, Low J: Current development of clinical inhibitors of Poly(ADP-Ribose) polymerase in Oncology. Clin Cancer Res 2007,13(5):1383-1388. 10.1158/1078-0432.CCR-06-2260CrossRefPubMed
22.
Albert JM, Cao C, Kim KW, Willey CD, Geng L, Xiao D, Wang H, Sandler A, Johnson DH, Colevas AD, Low J, Rothenberg ML, Lu B: Inhibition of Poly(ADP-Ribose) polymerase enhances cell death and improves tumor growth delay in irradiated lung cancer models. Clin Cancer Res 2007,13(10):3033-3042. 10.1158/1078-0432.CCR-06-2872CrossRefPubMed
23.
24.
Piskunova TS, Yurova MN, Ovsyannikov AI, Semenchenko AV, Zabezhinski MA, Popovich IG, Wang ZQ, Anisimov VN: Deficiency in poly(ADP-ribose) polymerase-1 (PARP-1) accelerates aging and spontaneous carcinogenesis in mice. Curr Gerontology and Geriatrics Res 2008, 1-10.
25.
Chou HY, Chou HT, Lee SC: CDK-dependent activation of poly(ADP-ribose) polymerase member 10 (PARP10). J Biol Chem 2006,281(22):15201-15207. 10.1074/jbc.M506745200CrossRefPubMed
26.
Polo S, Sigismund S, Faretta M, Guidi M, Capua MR, Bossi G, Chen H, De Camilli P, Di Fiore PP: A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature 2002, 416: 451-455. 10.1038/416451aCrossRefPubMed
27.
Shih SC, Prag G, Francis SA, Sutanto MA, Hurley JH, Hicke L: A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain. EMBO J 2003, 22: 1273-1281. 10.1093/emboj/cdg140PubMedCentralCrossRefPubMed
28.
Plafker SM, Plafker KS, Weissman AM, Macara IG: Ubiquitin charging of human class III ubiquitinconjugating enzymes triggers their nuclear import. J C B 2004,167(4):649-659.
Metadata
Title
The interaction between the PARP10 protein and the NS1 protein of H5N1 AIV and its effect on virus replication
Authors
Mengbin Yu
Chuanfu Zhang
Yutao Yang
Zhixin Yang
Lixia Zhao
Long Xu
Rong Wang
Xiaowei Zhou
Peitang Huang
Publication date
01-12-2011
Publisher
BioMed Central
Published in
Virology Journal / Issue 1/2011
Electronic ISSN: 1743-422X
DOI
https://doi.org/10.1186/1743-422X-8-546

Other articles of this Issue 1/2011

Virology Journal 1/2011 Go to the issue

Short report

Isolation and characterization of a novel podovirus which infects burkholderia pseudomallei

Research

Effect of oral care gel on the quality of life for oral lichen planus in patients with chronic HCV infection

Research

The assessment of efficacy of porcine reproductive respiratory syndrome virus inactivated vaccine based on the viral quantity and inactivation methods

Research

Prevalence, correlates and pattern of hepatitis B surface antigen in a low resource setting

Research

Development and validation of a prokaryotically expressed foot-and-mouth disease virus non-structural protein 2C'3AB-based immunochromatographic strip to differentiate between infected and vaccinated animals

Research

Experimental infection of Bama miniature pigs with a highly virulent classical swine fever virus
Live Webinar | 27-06-2024 | 18:00 (CEST)

Keynote webinar | Spotlight on medication adherence

Reserve your place

Live: Thursday 27th June 2024, 18:00-19:30 (CEST)

WHO estimates that half of all patients worldwide are non-adherent to their prescribed medication. The consequences of poor adherence can be catastrophic, on both the individual and population level.

Join our expert panel to discover why you need to understand the drivers of non-adherence in your patients, and how you can optimize medication adherence in your clinics to drastically improve patient outcomes.

Prof. Kevin Dolgin
Prof. Florian Limbourg
Prof. Anoop Chauhan
Developed by: Springer Medicine
Obesity Clinical Trial Summary

At a glance: The STEP trials

Read more

A round-up of the STEP phase 3 clinical trials evaluating semaglutide for weight loss in people with overweight or obesity.

Developed by: Springer Medicine
Image Credits