1887

Abstract

Defining how each ORF of porcine circovirus type 2 (PCV2) manipulates the host immune system may be helpful to understand the disease progression of post-weaning multisystemic wasting syndrome. In this study, we demonstrated a direct interaction between the PCV2 ORF2 and complement component 1, q subcomponent binding protein (C1QBP) within the cytoplasm of host macrophages. The physical interaction between PCV2 ORF2 and C1QBP inhibited ubiquitin-mediated proteasomal degradation of C1QBP in macrophages. Increased stability of C1QBP by the interaction with PCV2 ORF2 further enhanced the phagocytic activity of porcine macrophages through the phosphoinositol 3-kinase signalling pathway. This may explain the molecular basis of how PCV2 ORF2 enhances the phagocytic activity of host macrophages.

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2015-11-01
2020-01-23
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References

  1. Allan G.M., Ellis J.A.. ( 2000;). Porcine circoviruses: a review. J Vet Diagn Invest 12: 3–14 [CrossRef] [PubMed].
    [Google Scholar]
  2. Allan G.M., Kennedy S., McNeilly F., Foster J.C., Ellis J.A., Krakowka S.J., Meehan B.M., Adair B.M.. ( 1999;). Experimental reproduction of severe wasting disease by co-infection of pigs with porcine circovirus and porcine parvovirus. J Comp Pathol 121: 1–11 [CrossRef] [PubMed].
    [Google Scholar]
  3. Bierne H., Gouin E., Roux P., Caroni P., Yin H.L., Cossart P.. ( 2001;). A role for cofilin and LIM kinase in Listeria-induced phagocytosis. J Cell Biol 155: 101–112 [CrossRef] [PubMed].
    [Google Scholar]
  4. Bobak D.A., Gaither T.A., Frank M.M., Tenner A.J.. ( 1987;). Modulation of FcR function by complement: subcomponent C1q enhances the phagocytosis of IgG-opsonized targets by human monocytes and culture-derived macrophages. J Immunol 138: 1150–1156 [PubMed].
    [Google Scholar]
  5. Bobak D.A., Frank M.M., Tenner A.J.. ( 1988;). C1q acts synergistically with phorbol dibutyrate to activate CR1-mediated phagocytosis by human mononuclear phagocytes. Eur J Immunol 18: 2001–2007 [CrossRef] [PubMed].
    [Google Scholar]
  6. Darwich L., Pié S., Rovira A., Segalés J., Domingo M., Oswald I.P., Mateu E.. ( 2003;). Cytokine mRNA expression profiles in lymphoid tissues of pigs naturally affected by postweaning multisystemic wasting syndrome. J Gen Virol 84: 2117–2125 [CrossRef] [PubMed].
    [Google Scholar]
  7. Dvorak C.M.T., Puvanendiran S., Murtaugh M.P.. ( 2013;). Cellular pathogenesis of porcine circovirus type 2 infection. Virus Res 174: 60–68 [CrossRef] [PubMed].
    [Google Scholar]
  8. Finsterbusch T., Steinfeldt T., Doberstein K., Rödner C., Mankertz A.. ( 2009;). Interaction of the replication proteins and the capsid protein of porcine circovirus type 1 and 2 with host proteins. Virology 386: 122–131 [CrossRef] [PubMed].
    [Google Scholar]
  9. Ghebrehiwet B., Kew R.R., Gruber B.L., Marchese M.J., Peerschke E.I., Reid K.B.. ( 1995;). Murine mast cells express two types of C1q receptors that are involved in the induction of chemotaxis and chemokinesis. J Immunol 155: 2614–2619 [PubMed].
    [Google Scholar]
  10. Ghebrehiwet B., Lim B.L., Kumar R., Feng X., Peerschke E.I.. ( 2001;). gC1q-R/p33, a member of a new class of multifunctional and multicompartmental cellular proteins, is involved in inflammation and infection. Immunol Rev 180: 65–77 [CrossRef] [PubMed].
    [Google Scholar]
  11. Goodman E.B., Tenner A.J.. ( 1992;). Signal transduction mechanisms of C1q-mediated superoxide production. Evidence for the involvement of temporally distinct staurosporine-insensitive and sensitive pathways. J Immunol 148: 3920–3928 [PubMed].
    [Google Scholar]
  12. Guan E.N., Burgess W.H., Robinson S.L., Goodman E.B., McTigue K.J., Tenner A.J.. ( 1991;). Phagocytic cell molecules that bind the collagen-like region of C1q. Involvement in the C1q-mediated enhancement of phagocytosis. J Biol Chem 266: 20345–20355 [PubMed].
    [Google Scholar]
  13. He J., Cao J., Zhou N., Jin Y., Wu J., Zhou J.. ( 2013;). Identification and functional analysis of the novel ORF4 protein encoded by porcine circovirus type 2. J Virol 87: 1420–1429 [CrossRef] [PubMed].
    [Google Scholar]
  14. Liu J., Chen I., Kwang J.. ( 2005;). Characterization of a previously unidentified viral protein in porcine circovirus type 2-infected cells and its role in virus-induced apoptosis. J Virol 79: 8262–8274 [CrossRef] [PubMed].
    [Google Scholar]
  15. Liu J., Chen I., Du Q., Chua H., Kwang J.. ( 2006;). The ORF3 protein of porcine circovirus type 2 is involved in viral pathogenesis in vivo. J Virol 80: 5065–5073 [CrossRef] [PubMed].
    [Google Scholar]
  16. Liu J., Zhu Y., Chen I., Lau J., He F., Lau A., Wang Z., Karuppannan A.K., Kwang J.. ( 2007;). The ORF3 protein of porcine circovirus type 2 interacts with porcine ubiquitin E3 ligase Pirh2 and facilitates p53 expression in viral infection. J Virol 81: 9560–9567 [CrossRef] [PubMed].
    [Google Scholar]
  17. Mankertz A., Mankertz J., Wolf K., Buhk H.-J.. ( 1998;). Identification of a protein essential for replication of porcine circovirus. J Gen Virol 79: 381–384 [CrossRef] [PubMed].
    [Google Scholar]
  18. Nawagitgul P., Morozov I., Bolin S.R., Harms P.A., Sorden S.D., Paul P.S.. ( 2000;). Open reading frame 2 of porcine circovirus type 2 encodes a major capsid protein. J Gen Virol 81: 2281–2287 [CrossRef] [PubMed].
    [Google Scholar]
  19. Opriessnig T., Meng X.J., Halbur P.G.. ( 2007;). Porcine circovirus type 2 associated disease: update on current terminology, clinical manifestations, pathogenesis, diagnosis, and intervention strategies. J Vet Diagn Invest 19: 591–615 [CrossRef] [PubMed].
    [Google Scholar]
  20. Peerschke E.I., Reid K.B., Ghebrehiwet B.. ( 1993;). Platelet activation by C1q results in the induction of (IIb/(3 integrins (GPIIb-IIIa) and the expression of P-selectin and procoagulant activity. J Exp Med 178: 579–587 [CrossRef] [PubMed].
    [Google Scholar]
  21. Segalés J., Allan G.M., Domingo M.. ( 2005;). Porcine circovirus diseases. Anim Health Res Rev 6: 119–142 [CrossRef] [PubMed].
    [Google Scholar]
  22. Segalés J., Kekarainen T., Cortey M.. ( 2013;). The natural history of porcine circovirus type 2: from an inoffensive virus to a devastating swine disease?. Vet Microbiol 165: 13–20 [CrossRef] [PubMed].
    [Google Scholar]
  23. Shen Y., Naujokas M., Park M., Ireton K.. ( 2000;). InIB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase. Cell 103: 501–510 [CrossRef] [PubMed].
    [Google Scholar]
  24. Tischer I., Bode L., Peters D., Pociuli S., Germann B.. ( 1995;). Distribution of antibodies to porcine circovirus in swine populations of different breeding farms. Arch Virol 140: 737–743 [CrossRef] [PubMed].
    [Google Scholar]
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