Journal of Microbiology and Biotechnology

  • 제29권3호
  • /
  • Pages.482-488
  • /
  • 2019
  • /
  • 1017-7825(pISSN)
  • /
  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
권호 표지
DOI QR코드

DOI QR Code

Comparison of Immune Responses to the PCV2 Replicase-Capsid and Capsid Virus-Like Particle Vaccines in Mice

  • Jung, Bo-Kyoung (Department of Clinical Laboratory Science, Catholic University of Pusan) ;
  • Kim, Hye-Ran (Department of Clinical Laboratory Science, Catholic University of Pusan) ;
  • Lee, Young-Hyeon (Department of Clinical Laboratory Science, Catholic University of Pusan) ;
  • Jang, Hyun (WooGene B&G) ;
  • Chang, Kyung-Soo (Department of Clinical Laboratory Science, Catholic University of Pusan)
  • 투고 : 2018.09.17
  • 심사 : 2019.01.03
  • 발행 : 2019.03.28
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Porcine circovirus type 2 (PCV2) is the causative agent of postweaning multisystemic wasting syndrome (PMWS) in pigs. Replicase (Rep) proteins are considered essential for viral replication. Capsid (Cap) protein is the primary immunogenic protein that induces protective immunity. Little is known about comparison on the immunogenicity of PCV2 Rep and Cap fusion protein and Cap protein. In the present study, recombinant baculoviruses expressing the Rep-Cap fusion protein (Bac-Rep-Cap) and the Cap protein (Bac-Cap) of PCV2 were constructed and confirmed with western blot and indirect fluorescence assay. Immunogenicities of the two recombinant proteins were tested in mice. The titers of antibodies were determined with a PCV2-specific enzyme-linked immunosorbent assay (ELISA) and a serum neutralization assay. The $IFN-{\gamma}$ response of immunized mice was measured by ELISA. The mice immunized with the Bac-Rep-Cap and Bac-Cap successfully produced Cap-specific immunoreaction. The mice immunized with the Bac-Cap developed higher PCV2-specific neutralizing antibody titers than mice injected with the Bac-Rep-Cap. $IFN-{\gamma}$ in the Bac-Rep-Cap group was increased compared to those in the Bac-Cap group. Vaccination of mice with the Bac-Rep-Cap showed significantly decreased protective efficacy compared to the Bac-Cap. Our findings will indubitably not only lead to a better understanding of the immunogenicity of PCV2, but also improved vaccines.

키워드

참고문헌

  1. Allan GM, Ellis JA. 2000. Porcine circoviruses: a review. J. Vet. Diagn. Invest. 12: 3-14. https://doi.org/10.1177/104063870001200102
  2. An DJ, Song DS, Park BK. 2008. Systemic cytokine profiles of mice vaccinated with naked DNAs encoding six open reading frame antigens of porcine circovirus type 2 (PCV2). Res. Vet. Sci. 85: 503-509. https://doi.org/10.1016/j.rvsc.2008.03.006
  3. Blanchard P, Mahe D, Cariolet R, Keranflec'h A, Baudouard MA, Cordioli P, et al. 2003. Protection of swine against postweaning multisystemic wasting syndrome (PMWS) by porcine circovirus type 2 (PCV2) proteins. Vaccine 21: 4565-4575. https://doi.org/10.1016/S0264-410X(03)00503-6
  4. Cheung AK. 2003. The essential and nonessential transcription units for viral protein synthesis and DNA replication of porcine circovirus type 2. Virology 313: 452-459. https://doi.org/10.1016/S0042-6822(03)00373-8
  5. Cheung AK. 2003. Transcriptional analysis of porcine circovirus type 2. Virology 305: 168-180. https://doi.org/10.1006/viro.2002.1733
  6. Crisci E, Barcena J, Montoya M. 2012. Virus-like particles: the new frontier of vaccines for animal viral infections. Vet. Immunol. Immunopathol. 148: 211-225. https://doi.org/10.1016/j.vetimm.2012.04.026
  7. Darwich L, Balasch M, Plana-Duran J, Segales J, Domingo M, Mateu E. 2003. Cytokine profiles of peripheral blood mononuclear cells from pigs with postweaning multisystemic wasting syndrome in response to mitogen, superantigen or recall viral antigens. J. Gen. Virol. 84: 3453-3457. https://doi.org/10.1099/vir.0.19364-0
  8. Fan H, Xiao S, Tong T, Wang S, Xie L, Jiang Y, et al. 2008. Immunogenicity of porcine circovirus type 2 capsid protein targeting to different subcellular compartments. Mol. Immunol. 45: 653-660. https://doi.org/10.1016/j.molimm.2007.07.009
  9. Fenaux M, Opriessnig T, Halbur PG, Meng XJ. 2003. Immunogenicity and pathogenicity of chimeric infectious DNA clones of pathogenic porcine circovirus type 2 (PCV2) and nonpathogenic PCV1 in weanling pigs. J. Virol. 77: 11232-11243. https://doi.org/10.1128/JVI.77.20.11232-11243.2003
  10. Fort M, Olvera A, Sibila M, Segales J, Mateu E. 2007. Detection of neutralizing antibodies in postweaning multisystemic wasting syndrome (PMWS)-affected and non-PMWS-affected pigs. Vet. Microbiol. 125: 244-255. https://doi.org/10.1016/j.vetmic.2007.06.004
  11. Genmei L, Manlin L, Ruiai C, Hongliang H, Dangshuai P. 2011. Construction and immunogenicity of recombinant adenovirus expressing ORF2 of PCV2 and porcine IFN gamma. Vaccine 29: 8677-8682. https://doi.org/10.1016/j.vaccine.2011.08.118
  12. Groner A, Granados RR, Burand JP. 1984. Interaction of Autographa californica nuclear polyhedrosis virus with two nonpermissive cell lines. Intervirology 21: 203-209. https://doi.org/10.1159/000149522
  13. Kamstrup S, Barfoed AM, Frimann TH, Ladekjaer-Mikkelsen AS, Botner A. 2004. Immunisation against PCV2 structural protein by DNA vaccination of mice. Vaccine 22: 1358-1361. https://doi.org/10.1016/j.vaccine.2004.01.032
  14. Lin YH, Lee LH, Shih WL, Hu YC, Liu HJ. 2008. Baculovirus surface display of sigmaC and sigmaB proteins of avian reovirus and immunogenicity of the displayed proteins in a mouse model. Vaccine 26: 6361-6367. https://doi.org/10.1016/j.vaccine.2008.09.008
  15. 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. https://doi.org/10.1128/JVI.79.13.8262-8274.2005
  16. Liu LJ, Suzuki T, Tsunemitsu H, Kataoka M, Ngata N, Takeda N, et al. 2008. Efficient production of type 2 porcine circovirus-like particles by a recombinant baculovirus. Arch. Virol. 153: 2291-2295. https://doi.org/10.1007/s00705-008-0248-x
  17. Mankertz A, Hillenbrand B. 2001. Replication of porcine circovirus type 1 requires two proteins encoded by the viral rep gene. Virology 279: 429-438. https://doi.org/10.1006/viro.2000.0730
  18. Mankertz A, Mankertz J, Wolf K, Buhk HJ. 1998. Identification of a protein essential for replication of porcine circovirus. J. Gen. Virol. 79 (Pt 2): 381-384. https://doi.org/10.1099/0022-1317-79-2-381
  19. Meerts P, Misinzo G, Nauwynck HJ. 2005. Enhancement of porcine circovirus 2 replication in porcine cell lines by IFNgamma before and after treatment and by IFN-alpha after treatment. J. Interferon Cytokine Res. 25: 684-693. https://doi.org/10.1089/jir.2005.25.684
  20. Nawagitgul P, Morozov I, Bolin SR, Harms PA, Sorden SD, Paul PS. 2000. Open reading frame 2 of porcine circovirus type 2 encodes a major capsid protein. J. Gen. Virol. 81: 2281-2287. https://doi.org/10.1099/0022-1317-81-9-2281
  21. Opriessnig T, Meng XJ, Halbur PG. 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. https://doi.org/10.1177/104063870701900601
  22. Sedegah M, Charoenvit Y, Minh L, Belmonte M, Majam VF, Abot S, et al. 2004. Reduced immunogenicity of DNA vaccine plasmids in mixtures. Gene Ther. 11: 448-456. https://doi.org/10.1038/sj.gt.3302139
  23. Shen HG, Zhou JY, Zhang X, Huang ZY, He JL, Yan Y. 2009. Interference of porcine circovirus type 2 ORF2 immunogenicity by ORF1 and ORF3 mixed DNA immunizations in mice. Virology 393: 104-111. https://doi.org/10.1016/j.virol.2009.07.035
  24. Sipos W, Duvigneau JC, Pietschmann P, Schilcher F, Hofbauer G, Hartl RT, et al. 2005. Porcine dermatitis and nephropathy syndrome (PDNS) is associated with a systemic cytokine expression profile indicative of proinflammation and a Th1 bias. Vet. Immunol. Immunopathol. 107: 303-313. https://doi.org/10.1016/j.vetimm.2005.05.003
  25. Song Y, Jin M, Zhang S, Xu X, Xiao S, Cao S, et al. 2007. Generation and immunogenicity of a recombinant pseudorabies virus expressing cap protein of porcine circovirus type 2. Vet. Microbiol. 119: 97-104. https://doi.org/10.1016/j.vetmic.2006.08.026
  26. Strauss R, Huser A, Ni S, Tuve S, Kiviat N, Sow PS, et al. 2007. Baculovirus-based vaccination vectors allow for efficient induction of immune responses against plasmodium falciparum circumsporozoite protein. Mol. Ther. 15: 193-202. https://doi.org/10.1038/sj.mt.6300008
  27. Tegerstedt K, Franzen AV, Andreasson K, Joneberg J, Heidari S, Ramqvist T, et al. 2005. Murine polyomavirus virus-like particles (VLPs) as vectors for gene and immune therapy and vaccines against viral infections and cancer. Anticancer Res. 25: 2601-2608.
  28. Tischer I, Gelderblom H, Vettermann W, Koch MA. 1982. A very small porcine virus with circular single-stranded DNA. Nature 295: 64-66. https://doi.org/10.1038/295064a0
  29. Tjia ST, zu Altenschildesche GM, Doerfler W. 1983. Autographa californica nuclear polyhedrosis virus (AcNPV) DNA does not persist in mass cultures of mammalian cells. Virology 125: 107-117. https://doi.org/10.1016/0042-6822(83)90067-3
  30. van Oers MM. 2011. Opportunities and challenges for the baculovirus expression system. J. Invertebr. Pathol. 107 Suppl: S3-15. https://doi.org/10.1016/j.jip.2011.05.001
  31. Wang X, Jiang P, Li Y, Jiang W, Dong X. 2007. Protection of pigs against post-weaning multisystemic wasting syndrome by a recombinant adenovirus expressing the capsid protein of porcine circovirus type 2. Vet. Microbiol. 121: 215-224. https://doi.org/10.1016/j.vetmic.2006.11.027
  32. Wang X, Jiang W, Jiang P, Li Y, Feng Z, Xu J. 2006. Construction and immunogenicity of recombinant adenovirus expressing the capsid protein of porcine circovirus 2 (PCV2) in mice. Vaccine 24: 3374-3380. https://doi.org/10.1016/j.vaccine.2005.12.068
  33. Wang YP, Liu D, Guo LJ, Tang QH, Wei YW, Wu HL, et al. 2013. Enhanced protective immune response to PCV2 subunit vaccine by co-administration of recombinant porcine IFNgamma in mice. Vaccine 31: 833-838. https://doi.org/10.1016/j.vaccine.2012.11.062
  34. Xu XG, Chiou MT, Zhang YM, Tong DW, Hu JH, Zhang MT, et al. 2008. Baculovirus surface display of E(rns) envelope glycoprotein of classical swine fever virus. J. Virol. Methods 153: 149-155. https://doi.org/10.1016/j.jviromet.2008.07.019
  35. Xu XG, Tong DW, Wang ZS, Zhang Q, Li ZC, Zhang K, et al. 2011. Baculovirus virions displaying infectious bursal disease virus VP2 protein protect chickens against infectious bursal disease virus infection. Avian Dis. 55: 223-229. https://doi.org/10.1637/9597-111210-Reg.1
  36. Xu XG, Wang ZS, Zhang Q, Li ZC, Zhao HN, Li W, et al. 2011. Baculovirus surface display of E envelope glycoprotein of Japanese encephalitis virus and its immunogenicity of the displayed proteins in mouse and swine models. Vaccine 29: 636-643. https://doi.org/10.1016/j.vaccine.2010.11.045
  37. Ye Y, Cheng X, Zhang J, Tong T, Lin W, Liao M, et al. 2013. Induction of robust immunity response in mice by dualexpression-system-based recombinant baculovirus expressing the capsid protein of porcine circovirus type 2. Virol. J. 10: 316. https://doi.org/10.1186/1743-422X-10-316

피인용 문헌

  1. Oral vaccination with the porcine circovirus type 2 (PCV‐2) capsid protein expressed by Lactococcus lactis induces a specific immune response against PCV‐2 in mice vol.128, pp.1, 2020, https://doi.org/10.1111/jam.14473
  2. Comparative immunopathogenesis and biology of recently discovered porcine circoviruses vol.68, pp.6, 2021, https://doi.org/10.1111/tbed.14244