J Vet Sci.  2014 Dec;15(4):511-517. 10.4142/jvs.2014.15.4.511.

Proteomic analysis of chicken peripheral blood mononuclear cells after infection by Newcastle disease virus

Affiliations
  • 1Laboratory of Infectious Diseases, College of Veterinary Medicine, Jilin University, Changchun 130062, China. dingzhuangjlu@126.com
  • 2Engineering Research Center of Jilin Province for Animals Probiotics, College of Animal Science and Technology, Jilin Agricultural University, Changchun 130118, China.
  • 3Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, China.
  • 4Animal Infectious Disease Laboratory, College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China.
  • 5Engineering Research Center of Chinese Ministry of Education for Edible and Medicinal Fungi, Jilin Agricultural University, Changchun 130118, China.

Abstract

Characteristic clinical manifestations of Newcastle disease include leukopenia and immunosuppression. Peripheral blood mononuclear cells (PBMCs) are the main targets of Newcastle disease virus (NDV) infection. To survey changes in proteomic expression in chicken PBMCs following NDV infection, PBMC proteins from 30 chickens were separated using two-dimensional electrophoresis (2-DE) and subjected to mass spectrometry analysis. Quantitative intensity analysis showed that the expression of 78 proteins increased more than two-fold. Thirty-five proteins exhibited consistent changes in expression and 13 were identified as unique proteins by matrix assisted laser desorption ionization-time of flight mass spectrometer/mass spectrometer including three that were down-regulated and 10 that were up-regulated. These proteins were sorted into five groups based on function: macromolecular biosynthesis, cytoskeleton organization, metabolism, stress responses, and signal transduction. Furthermore, Western blot analysis confirmed the down-regulation of integrin-linked kinase expression and up-regulation of lamin A production. These data provide insight into the in vivo response of target cells to NDV infection at the molecular level. Additionally, results from this study have helped elucidate the molecular pathogenesis of NDV and may facilitate the development of new antiviral therapies as well as innovative diagnostic methods.

Keyword

Newcastle disease virus; peripheral blood mononuclear cells; proteomics

MeSH Terms

Animals
Avian Proteins/*genetics/metabolism
*Chickens
*Gene Expression Regulation
Leukocytes, Mononuclear/enzymology/virology
Newcastle Disease/*genetics/virology
Newcastle disease virus/*physiology
Poultry Diseases/*genetics/virology
*Proteome
Specific Pathogen-Free Organisms
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/veterinary
Tandem Mass Spectrometry/veterinary
Avian Proteins
Proteome

Figure

  • Fig. 1 RT-PCR results for specific detection of partial Newcastle disease virus (NDV) M gene. Lane 1, infected group; Lane 2, mock-infected group; Lane M, DL2000 marker.

  • Fig. 2 Representative 2-dimensional electrophoresis (DE) gel images obtained for peripheral blood mononuclear cells (PBMCs) from chickens that were infected by NDV or mock-infected. (A) Mock-infected control group and (B) day 5 post-infected group. The protein spots were visualized by silver staining. MM denotes the molecular mass.

  • Fig. 3 Validation of altered lamin A and integrin-linked kinase (ILK) expression by Western blot analysis. (A) Magnified 2-DE images of lamin A and ILK for the mock-infected control and NDV-infected groups. (B) Western blot analysis of lamin A and ILK expression.


Reference

1. Aldous EW, Alexander DJ. Newcastle disease in pheasants (Phasianus colchicus): a review. Vet J. 2008; 175:181–185.
2. Chambers P, Millar NS, Bingham RW, Emmerson PT. Molecular cloning of complementary DNA to Newcastle disease virus, and nucleotide sequence analysis of the junction between the genes encoding the haemagglutinin-neuraminidase and the large protein. J Gen Virol. 1986; 67:475–486.
Article
3. Davidson WS, Hazlett T, Mantulin WW, Jonas A. The role of apolipoprotein AI domains in lipid binding. Proc Natl Acad Sci U S A. 1996; 93:13605–13610.
4. Didelot C, Schmitt E, Brunet M, Maingret L, Parcellier A, Garrido C. Heat shock proteins: endogenous modulators of apoptotic cell death. Handb Exp Pharmacol. 2006; 172:171–198.
Article
5. Ding Z, Li ZJ, Zhang XD, Li YG, Liu CJ, Zhang YP, Li Y. Proteomic alteration of Marc-145 cells and PAMs after infection by porcine reproductive and respiratory syndrome virus. Vet Immunol Immunopathol. 2012; 145:206–213.
Article
6. Esfandiarei M, Suarez A, Amaral A, Si X, Rahmani M, Dedhar S, McManus BM. Novel role for integrin-linked kinase in modulation of coxsackievirus B3 replication and virus-induced cardiomyocyte injury. Circ Res. 2006; 99:354–361.
Article
7. Fauquet CM, Fargette D. International Committee on Taxonomy of Viruses and the 3,142 unassigned species. Virol J. 2005; 2:64.
Article
8. Gruenbaum Y, Wilson KL, Harel A, Goldberg M, Cohen M. Review: nuclear lamins-structural proteins with fundamental functions. J Struct Biol. 2000; 129:313–323.
Article
9. Handschumacher RE, Harding MW, Rice J, Drugge RJ, Speicher DW. Cyclophilin: a specific cytosolic binding protein for cyclosporin A. Science. 1984; 226:544–547.
Article
10. Hannigan G, Troussard AA, Dedhar S. Integrin-linked kinase: a cancer therapeutic target unique among its ILK. Nat Rev Cancer. 2005; 5:51–63.
Article
11. Harris TK, Cole RN, Comer FI, Mildvan AS. Proton transfer in the mechanism of triosephosphate isomerase. Biochemistry. 1998; 37:16828–16838.
Article
12. Kamath S, Lip GY. Fibrinogen: biochemistry, epidemiology and determinants. QJM. 2003; 96:711–729.
Article
13. Kasyapa CS, Kunapuli P, Cowell JK. Mass spectroscopy identifies the splicing-associated proteins, PSF, hnRNP H3, hnRNP A2/B1, and TLS/FUS as interacting partners of the ZNF198 protein associated with rearrangement in myeloproliferative disease. Exp cell Res. 2005; 309:78–85.
Article
14. Kobayashi K, Ohgitani E, Tanaka Y, Kita M, Imanishi J. Herpes simplex virus-induced expression of 70 kDa heat shock protein (HSP70) requires early protein synthesis but not viral DNA replication. Microbiol Immunol. 1994; 38:321–325.
Article
15. Lam KM. Growth of Newcastle disease virus in chicken macrophages. J Comp Pathol. 1996; 115:253–263.
Article
16. Lam KM. Newcastle disease virus-induced apoptosis in the peripheral blood mononuclear cells of chickens. J Comp Pathol. 1996; 114:63–71.
Article
17. Lam KM, Kabbur MB, Eiserich JP. Newcastle disease virus-induced functional impairments and biochemical changes in chicken heterophils. Vet Immunol Immunopathol. 1996; 53:313–327.
Article
18. Lazebnik YA, Takahashi A, Moir RD, Goldman RD, Poirier GG, Kaufmann SH, Earnshaw WC. Studies of the lamin proteinase reveal multiple parallel biochemical pathways during apoptotic execution. Proc Natl Acad Sci U S A. 1995; 92:9042–9046.
Article
19. Liu N, Song W, Wang P, Lee K, Chan W, Chen H, Cai Z. Proteomics analysis of differential expression of cellular proteins in response to avian H9N2 virus infection in human cells. Proteomics. 2008; 8:1851–1858.
Article
20. Lowenstein CJ. Integrin-linked kinase plays a key role in coxsackievirus replication. Circ Res. 2006; 99:346–347.
Article
21. Mathesius U, Keijzers G, Natera SH, Weinman JJ, Djordjevic MA, Rolfe BG. Establishment of a root proteome reference map for the model legume Medicago truncatula using the expressed sequence tag database for peptide mass fingerprinting. Proteomics. 2006; 1:1424–1440.
Article
22. Meighan-Mantha RL, Tolan DR. Noncoordinate changes in the steady-state mRNA expressed from aldolase A and aldolase C genes during differentiation of chicken myoblasts. J Cell Biochem. 1995; 57:423–431.
Article
23. Miller PJ, Decanini EL, Afonso CL. Newcastle disease: evolution of genotypes and the related diagnostic challenges. Infect Genet Evol. 2010; 10:26–35.
Article
24. Miralles F, Visa N. Actin in transcription and transcription regulation. Curr Opin Cell Biol. 2006; 18:261–266.
Article
25. Roulston A, Marcellus RC, Branton PE. Viruses and apoptosis. Annu Rev Microbiol. 1999; 53:577–628.
Article
26. Shiojima I, Walsh K. Role of Akt signaling in vascular homeostasis and angiogenesis. Circ Res. 2002; 90:1243–1250.
Article
27. Stuurman N, Heins S, Aebi U. Nuclear lamins: their structure, assembly, and interactions. J Struct Biol. 1998; 122:42–66.
Article
28. Taipale M, Jarosz DF, Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol. 2010; 11:515–528.
Article
29. van der Pouw Kraan TCMT, Kasperkovitz PV, Verbeet N, Verweij CL. Genomics in the immune system. Clin Immunol. 2004; 111:175–185.
Article
30. Wang J, Ying G, Wang J, Jung Y, Lu J, Zhu J, Pienta KJ, Taichman RS. Characterization of phosphoglycerate kinase-1 expression of stromal cells derived from tumor microenvironment in prostate cancer progression. Cancer Res. 2010; 70:471–480.
Article
31. White SR, Williams P, Wojcik KR, Sun S, Hiemstra PS, Rabe KF, Dorscheid DR. Initiation of apoptosis by actin cytoskeletal derangement in human airway epithelial cells. Am J Respir Cell Mol Biol. 2001; 24:282–294.
Article
32. Wilhelm AJ, Zabalawi M, Grayson JM, Weant AE, Major AS, Owen J, Bharadwaj M, Walzem R, Chan L, Oka K, Thomas MJ, Sorci-Thomas MG. Apolipoprotein A-I and its role in lymphocyte cholesterol homeostasis and autoimmunity. Arterioscler Thromb Vasc Biol. 2009; 29:843–849.
Article
33. Xu C, Meng S, Liu X, Sun L, Liu W. Chicken cyclophilin A is an inhibitory factor to influenza virus replication. Virol J. 2010; 7:372.
Article
34. Yuan W, Xie J, Long C, Erdjument-Bromage H, Ding X, Zheng Y, Tempst P, Chen S, Zhu B, Reinberg D. Heterogeneous nuclear ribonucleoprotein L is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo. J Biol Chem. 2009; 284:15701–15707.
Article
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