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Screening and analysis on the protein interaction of the protein VP7 in grass carp reovirus


Grass carp reovirus (GCRV) has caused serious economic losses for several decades in China. The protein VP7 is one of the important structural proteins in GCRV. Recent studies indicated that the protein VP7 had the commendable antigenicity and immunogenicity. The protein VP7 cooperated with VP5 could change the conformation of the cell membrane and facilitate entry of GCRV into host cells. We speculated that the protein VP7 should play an important role in the pathogenesis of GCRV. In order to explore the function of the protein VP7, the bait protein expression plasmid pGBKT7-vp7 and the cDNA library of CIK cells were constructed. By yeast two-hybrid system, after multiple screening with the high screening rate medium, rotary verification, sequencing and bioinformatics analysis, the interactions of the protein VP7 with ribosomal protein S20 (RPS20) and eukaryotic translation initiation factor 3 subunit b (eIF3b) in CIK cells were identified. RPS20 played the important roles in the generation of influenza B virus and a variety of diseases. eIF3b was relative to the infection of some viruses. This study suggested that the protein VP7 played the role in viral replication and most likely interacted with host proteins by RPS20 and eIF3b. The interaction mechanisms of the protein VP7 with RPS20 and eIF3b, and the subsequent effector mechanisms needed to be further studied. The corresponding protein interaction of the protein VP7 was not acquired in bioinformatics. The protein VP7 and its untranslated region may have the unknown special function. This study laid the foundation for deeply exploring the function of the protein VP7 in GCRV and had the important scientific significance for exploring the pathogenic mechanism of GCRV.

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  1. 1.

    Y.S. Chen, Y.L. Jiang, Chin. Sci. Bull. 28, 1138–1140 (1983). In Chinese

  2. 2.

    Y.A. Lu, C.N. Lannan, J.S. Rohovec, J.L. Fryer, In. Vitro. Cell. Dev. Biol 26(3 Pt 1), 275–279 (1990)

  3. 3.

    F.A. Murphy, C.M. Fauquet, D.H.L. Bishop, S. Ghabrial, A.W. Jarvis, G.P. Martelli, M.A. Mayo, M.D. Summers, Arch. Virol [Suppl] 10 208–239 (1995)

  4. 4.

    Q. Fang, Q.Q. Ding, Y.P. Wang, Z.Y. Zhu, Virologica. Siniga. 18(5), 464–467 (2003)

  5. 5.

    J. Li, T.H. Wang, L.R. Zhou, H.S. Xu, J. Fish. Sci. China 5(3), 115–118 (1998). In Chinese

  6. 6.

    T. Qiu, R.H. Lu, J. Zhang, Z.Y. Zhu, Dis. Aquat. Organ. 44(1), 69–74 (2001)

  7. 7.

    X.Y. Yan, Y. Wang, L.F. Xiong, J.C. Jian, Z.H. Wu, SpringerPlus 3(1), 190–199 (2014)

  8. 8.

    Q. Zhang, High. Tech. Let. 9(2), 7–13 (2003)

  9. 9.

    J. Tian, G.P. Zou, Q. Fang, Virologa. Sinica. 14(1), 87–92 (1999)

  10. 10.

    Q. Fang, S. Shah, Y. Liang, Z.H. Zhou, Sci. In. China. Series. C. 48(6), 593–600 (2005)

  11. 11.

    Q. Fang, E.K. Seng, Q.Q. Ding, L.L. Zhang, Arch. Virol. 153(4), 675–682 (2008)

  12. 12.

    L.L. Zhang, J.Y. Shen, C.F. Lei, X.M. Li, Q. Fang, Virologica. Sinica. 23(1), 51–56 (2008)

  13. 13.

    C. Chen, X. Sun, L. Liao, S. Luo, Z. Li, X. Zhang, Y. Wang, Q. Guo, Q. Fang, H. Dai, Sci. China. Life. Sci. 56(1), 59–65 (2013)

  14. 14.

    S.Y. Xu, J.H. Li, Y. Zou, L. Liu, C.L. Gong, G.L. Cao, R.Y. Xue, H. Chen, J. Hunan. Agric. Univ. (Nat. Sci). 37(6), 659–664 (2011). In Chinese

  15. 15.

    L. Shao, X. Sun, Q. Fang, Virol J. 8, 347 (2011)

  16. 16.

    K. Xu, L.L. Wang, T.T. Zhang, G. Zhou, Z.Q. Zhang, Z.Y. zhang, Chinese. J. Biochem. Mol. Biol. 28(3), 267–275 (2012). In Chinese

  17. 17.

    L. Cai, X.Y. Sun, L. Shao, Q. Fang, Virol. J. 8(1), 168–177 (2011)

  18. 18.

    J. Chen, H.Y. Yang, Y.H. Shi, M.Y. Li, Fish. Shellfish. Immunol. 26(3), 536–542 (2009)

  19. 19.

    S.K. Otta, Indian. J. Virol. 23(2), 184–190 (2012)

  20. 20.

    P. Sangsuriya, J.Y. Huang, Y.F. Chu, K. Phiwsaiya, P. Leekitcharoenphon, W. Meemetta, S. Senapin, W.P. Huang, B. Withyachumnarnkul, T.W. Flegel, C.F. Lo, Mol. Cell. Proteomics. 13(1), 269–282 (2014)

  21. 21.

    W.G. Zuo, H.X. Qian, Y.F. Xu, S.Y. Du, X.L. Yang, J. PF. Fish. China. 10(1), 11–17 (1986). In Chinese

  22. 22.

    S. Li, C.M. Armstrong, N. Bertin, H. Ge, S. Milstein, M. Boxem, P.O. Vidalain, J.D. Han, A. Chesneau, T. Hao, D.S. Goldberg, N. Li, M. Martinez, J.F. Rual, P. Lamesch, L. Xu, M. Tewari, S.L. Wong, L.V. Zhang, G.F. Berriz, L. Jacotot, P. Vaglio, J. Reboul, T. Hirozane-Kishikawa, Q. Li, H.W. Gabel, A. Elewa, B. Baumgartner, D.J. Rose, H. Yu, S. Bosak, R. Sequerra, A. Fraser, S.E. Mango, W.M. Saxton, S. Strome, S. Van Den Heuvel, F. Piano, J. Vandenhaute, C. Sardet, M. Gerstein, L. Doucette-Stamm, K.C. Gunsalus, J.W. Harper, M.E. Cusick, F.P. Roth, D.E. Hill, M. Vidal, Science 303(5657), 540–543 (2004)

  23. 23.

    F.W. Chen, Y.A. Ioannou, Int. Rev. Immunol. 18(5–6), 429–448 (1999)

  24. 24.

    G. Wang, T. Inaoka, S. Okamoto, K. Ochi, Antimicrob. Agents Chemother. 53(3), 1019–1026 (2009)

  25. 25.

    L.R. Rapaport, G.A. Maekie, J. Bacteriol. 176(4), 992–998 (1994)

  26. 26.

    K.A. McGowan, J.Z. Li, C.Y. Park, V. Beaudry, H.K. Tabor, A.J. Sabnis, W. Zhang, H. Fuchs, M.H. de Angelis, R.M. Myers, L.D. Attardi, G.S. Barsh, Nat. Genet. 40(8), 963–970 (2008)

  27. 27.

    M. De Bortolil, R.C. Castellinol, X.Y. Lu, J. Deyo, L.M. Sturla, A.M. Adesina, L. Perlaky, S.L. Pomeroy, C.C. Lau, T.K. Man, P.H. Rao, J.Y. Kim, BMC Cancer 6, 223 (2006)

  28. 28.

    E.H. Kemp, L.M. Herd, E.A. Waterman, A.G. Wilson, A.P. Weetman, P.P. Watson, Biochem. Biophys. Res. Commun. 298(1), 169–177 (2002)

  29. 29.

    S.D. Goldstone, M.F. Lavin, Biochem. Biophys. Res. Commun. 196(2), 619–623 (1993)

  30. 30.

    H. Yu, L.H. Yao, A.J. Chen, J. He, R.Q. Jia, C.S. Cheng, Z.Q. Zhang, Zhonghua. Shi. Yan. He. Lin. Chuang. Bing. Du. Xue. Za. Zhi 19(2): 182–184 (2005)

  31. 31.

    X.P. Sun, Changchun: Jilin University (2013) In Chinese

  32. 32.

    L. Daftuar, Y. Zhu, X. Jacq, C. Prives, PLoS ONE 8(7), e68667 (2013)

  33. 33.

    H. Liang, X.H. Ding, C. Zhou, Y. Zhang, M. Xu, C. Zhang, L. Xu, Neurol. Sci 33(5), 1057–1062 (2012)

  34. 34.

    B.L. Jones, J. VanLoozen, M.H. Kim, S.J. Miles, C.M. Dunham, L.D. Williams, T.W. Snell, Comp. Biochem. Physiol. A. Mol. Integr. Physiol 166(2), 375–384 (2013)

  35. 35.

    Y. Liu, P. Neumann, B. Kuhle, T. Monecke, S. Schell, A. Chari, R. Ficner, Structure 22(6), 923–930 (2014)

  36. 36.

    H. Wang, Y. Ru, M. Sanchez-Carbayo, X. Wang, J.S. Kieft, D. Theodorescu, Clin. Cancer Res. 19(11), 2850–2860 (2013)

  37. 37.

    Z. Wang, J.X. Chen, J.H. Sun, Z. Cui, H. Wu, World J. Surg. Oncol. 10, 119 (2012)

  38. 38.

    M. Rodríguez Pulido, P. Serrano, M. Sáiz, E. Martínez-Salas, Virology 364(2), 466–474 (2007)

  39. 39.

    A. Souii, J. Gharbi, M. Ben M’hadheb-Gharbi, Diagn Pathol 8, 161 (2013)

  40. 40.

    A. Fathinajafabadi, E. Pérez-Jiménez, M. Riera, E. Knecht, R. Gonzàlez-Duarte, PLoS ONE 9, e87898 (2014)

  41. 41.

    J. Pérard, R. Rasia, J. Medenbach, I. Ayala, J. Boisbouvier, E. Drouet, F. Baudin, FEBS Lett. 583(1), 70–74 (2009)

  42. 42.

    Y. Hashem, A. des Georges, V. Dhote, R. Langlois, H.Y. Liao, R.A. Grassucci, T.V. Pestova, C.U. Hellen, J. Frank, Nature 503(7477), 539–543 (2013)

  43. 43.

    D. Khan, P. Bhat, S. Das, Trends Microbiol. 22(2), 57–58 (2014)

  44. 44.

    A. Herrmannová, D. Daujotyte, J.C. Yang, L. Cuchalová, F. Gorrec, S. Wagner, I. Dányi, P.J. Lukavsky, L.S. Valásek, Nucleic Acids Res. 40(5), 2294–2311 (2012)

  45. 45.

    Q. Cai, A. Todorovic, A. Andaya, J. Gao, J.A. Leary, J.H. Cate, J. Mol. Biol. 403(2), 185–196 (2010)

  46. 46.

    M. López-Lastra, A. Rivas, M.I. Barría, Biol. Res. 38(2–3), 121–146 (2005)

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The study was supported by the National 973 Plan Project in China (No. 2009CB118704).

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Correspondence to Jichang Jian.

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Edited by Zhen F. Fu.

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Yan, X., Xie, J., Li, J. et al. Screening and analysis on the protein interaction of the protein VP7 in grass carp reovirus. Virus Genes 50, 425–433 (2015).

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  • Grass carp reovirus 096 (GCRV 096)
  • The protein VP7
  • Yeast two-hybrid system
  • Protein interaction
  • Ribosomal protein S20 (RPS20)
  • Eukaryotic translation initiation factor 3 subunit b (eIF3b)