The structural protein VP3 of infectious bursal disease virus (IBDV) plays a critical role in viral assembly, replication, immune escape, and anti-apoptosis. Interaction between VP3 and host protein factors can affect stages in the viral replication cycle. In this study, 137 host proteins interacting with VP3 protein were screened through liquid chromatography–tandem mass spectrometry (LC–MS/MS)-based proteomics approach. The functions and relevance of the proteins were obtained through bioinformatics analysis. Most VP3-interacting proteins were linked to binding, catalytic activity, and structural molecular activity, and performed functions in cell parts and cells. Biological functions of VP3-interacting proteins were mainly relevant to "Cytoskeleton", "Translation", and "Signal transduction mechanisms", involving ribosomes, "Tight junction", regulation of actin cytoskeleton, and other pathways. Six potential VP3-interacting proteins in host cells were knocked down, and vimentin, myosin-9, and annexin A2 were found to be related to IBDV replication. This study would help explore regulatory pathways and cellular mechanisms in IBDV-infected cells, and also provided clues for the in-depth study of VP3 biological functions and IBDV replication or pathogenesis.
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Müller H, Mundt E, Eterradossi N, Islam MR (2012) Current status of vaccines against infectious bursal disease. Avian Pathology 41:133–139
Jackwood DJ (2017) Advances in vaccine research against economically important viral diseases of food animals: Infectious bursal disease virus. Vet Microbiol 206:121–125
Rautenschlein S, Alkie TN (2016) Infectious bursal disease virus in poultry: current status and future prospects. Vet Med (Auckl) 7:9–18
Mei Y, Wang Y, Ouyang W, Pan Q, Meng K, Wang X, Xia X, Zhu Y, Dong C, Bi Z, Wang J, Wu H, Yao H (2016) Isolation and characterization of biological properties of infectious bursal disease viruses from eastern China in recent years. Chinese Veterinary Science 46:550–557
Fan L, Wu T, Hussain A, Gao Y, Zeng X, Wang Y, Gao Li, Li K, Wang Y, Liu C, Cui H, Pan Q, Zhang Y, Liu Y, He H, Wang X, Qi X (2019) Novel variant strains of infectious bursal disease virus isolated in China. Vet Microbiol 230:212–220
Fan L, Wu T, Wang Y, Hussain A, Qi X (2020) Novel variants of infectious bursal disease virus can severely damage the bursa of fabricius of immunized chickens. Vet Microbiol 240:108507
Einem UI, Gorbalenya AE, Schirrmeier H, Behrens SE, Letzel T, Mundt E (2004) VP1 of infectious bursal disease virus is an RNA-dependent RNA polymerase. J Gen Virol 85:2221–2229
Maraver A, Ona A, Abaitua F, González D, Clemente R, Ruiz-Díaz JA, Castón JR, Pazos F, Rodriguez JF (2003) The oligomerization domain of VP3, the scaffolding protein of infectious bursal disease virus, plays a critical role in capsid assembly. J Virol 77:6438–6449
Méndez F, Romero N, Cubas LL, Delgui LR, Rodríguez D, Rodríguez JF (2017) Non-lytic egression of infectious bursal disease virus (IBDV) particles from infected cells. PLoS ONE 12:e0170080
Qin Y, Zheng SJ (2017) Infectious Bursal Disease Virus-Host Interactions: Multifunctional Viral Proteins that Perform Multiple and Differing Jobs. Int J Mol Sci 18:161–173
Garriga D, Navarro A, Querol-Audi J, Abaitua F, Rodriguez JF, Verdaguer N (2007) Activation mechanism of a noncanonical RNA-dependent RNA polymerase. Proc Natl Acad Sci USA 104:20540–20545
Jackwood DJ, Sommer-Wagner SE (2011) Amino acids contributing to antigenic drift in the infectious bursal disease Birnavirus (IBDV). Virology 409:33–37
Busnadiego I, Maestre AM, Rodríguez D, Rodríguez JF (2012) The infectious bursal disease virus RNA-binding VP3 polypeptide inhibits PKR-mediated apoptosis. PLoS ONE 7:e46768
Ye C, Jia L, Sun Y, Hu B, Wang L, Lu X, Zhou J (2014) Inhibition of Antiviral Innate Immunity by Birnavirus VP3 Protein via Blockage of Viral Double-Stranded RNA Binding to the Host Cytoplasmic RNA Detector MDA5. J Virol 88:11154
Schwanhäusser B, Busse D, Li N, Dittmar G, Schuchhardt J, Wolf J, Chen W, Selbach M (2011) Global quantification of mammalian gene expression control. Nature 473:337–342
Galperin MY, Kristensen DM, Makarova KS, Wolf YI, Koonin EV (2019) Microbial genome analysis: the COG approach. Brief Bioinform 20:1063–1070
Kanehisa M, Araki M, Goto S, Hattori M, Hirakawa M, Itoh M, Katayama T, Kawashima S, Okuda S, Tokimatsu T, Yamanishi Y (2008) KEGG for linking genomes to life and the environment. Nucleic Acids Res. https://doi.org/10.1093/nar/gkm882
Szklarczyk D, Gable AL, Lyon D, Junge A, Wyder S, Huerta-Cepas J, Simonovic M, Doncheva NT, Morris JH, Bork P, Jensen LJ, von Mering C (2019) STRING v11: protein-protein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets. Nucleic Acids Res 47:D607-613
Wulff NH, Tzatzaris M, Young PJ (2012) Monte Carlo simulation of the Spearman-Kaerber TCID50. J Clin Bioinforma 2:5
Du C, Liu HF, Lin YZ, Wang XF, Ma J, Li YJ, Wang X, Zhou JH (2015) Proteomic alteration of equine monocyte-derived macrophages infected with equine infectious anemia virus. Proteomics 15:1843–1858
Liu HW, Liang CQ, Liu PF, Luo LX, Li JQ (2015) Quantitative proteomics identifies 38 proteins that are differentially expressed in cucumber in response to cucumber green mottle mosaic virus infection. Virol J 15:216
Zheng X, Hong L, Shi L, Guo J, Sun Z, Zhou J (2008) Proteomics analysis of host cells infected with infectious bursal disease virus. Molecular & Cellular Proteomics Mcp 7:612–625
Sun Y, Hu B, Fan C, Jia L, Zhang Y, Du A, Zheng X, Zhou J (2015) iTRAQ-based quantitative subcellular proteomic analysis of Avibirnavirus-infected cells. Electrophoresis 36:1596–1611
Stradal TEB, Schelhaas M (2018) Actin dynamics in host-pathogen interaction. FEBS Lett 592:3658–3669
Gimenez MC, Zanetti FA, Terebiznik MR, Colombo MI, Delgui LR (2018) Infectious Bursal Disease Virus, hijacks endosomal membranes as the scaffolding structure for viral replication. J Virol 92:e01964-e2017
Paula T, Mira L, Malin Flodström T, Varpu M (2020) Human enterovirus group B viruses rely on vimentin dynamics for efficient processing of viral non-structural proteins. J Virol 94:e01393-e1419
Teo CSH, Chu JJH (2014) Cellular Vimentin Regulates Construction of Dengue Virus Replication Complexes through Interaction with NS4A Protein. J Virol 88:1897–1913
Fujita T, Kitaura F, Fujii H (2015) A critical role of the Thy28-MYH9 axis in B cell-specific expression of the Pax5 gene in chicken B cells. PLoS ONE 10:e0116579
Ganaie SS, Haque A, Cheng E, Bonny TS, Salim NN, Mir MA (2014) Ribosomal protein S19-binding domain provides insights into hantavirus nucleocapsid protein-mediated translation initiation mechanism. Biochem J 464:109–121
Huang JY, Su WC, Jeng KS, Chang TH, Lai MM (2012) Attenuation of 40S ribosomal subunit abundance differentially affects host and HCV translation and suppresses HCV replication. PLoS Pathog 8:e1002766
Filbin ME, Kieft JS (2009) Toward a structural understanding of IRES RNA function. Curr Opin Struct Biol 19:267–276
Chen Y, Lu Z, Zhang L, Gao L, Wang N, Gao Q, Wang Y, Li K, Gao Y, Cui H, Gao H, Liu C, Zhang Y, Qi X, Wang X (2016) Ribosomal protein L4 interacts with viral protein VP3 and regulates the replication of infectious bursal disease virus. Virus Research An International Journal of Molecular & Cellular Virology 211:73–78
Wang B, Duan X, Fu M, Liu Y, Wang Y, Li X, Cao H, Zheng SJ (2018) The association of ribosomal protein L18 (RPL18) with infectious bursal disease virus viral protein VP3 enhances viral replication. Virus Res 245:69–79
The present studies were sequenced by Guangzhou Gene Denovo Biotechnology Co., Ltd.
This work was supported by National Key R&D Program of China (Grant No. 2018YFD0500106), Jiangsu Provincial Natural Science Foundation of China (Grant No. BK20180299), Jiangsu Agriculture Science and Technology Innovation Fund (CX(19)3019, CX(20)3095), and National Natural Science Foundation of China (Grant No. 31772723, No. 32002274, No. 32072872).
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Ma, ST., Wang, YS., Wang, XL. et al. Mass spectrometry-based proteomic analysis of potential infectious bursal disease virus VP3-interacting proteins in chicken embryo fibroblasts cells. Virus Genes 57, 194–204 (2021). https://doi.org/10.1007/s11262-021-01828-x
- Infectious bursal disease virus
- VP3 protein
- Host protein factor
- Immunoprecipitation technique
- Mass spectrometry