Skip to main content

Advertisement

SpringerLink
Log in

Deletion of a decoy epitope in porcine circovirus 2 (PCV2) capsid protein affects the protective immune response in mice

  • Original Article
  • Published:
Archives of Virology Aims and scope Submit manuscript

Abstract

The swine pathogen porcine circovirus type 2 (PCV2) causes significant economic damage worldwide. The PCV2 capsid (CP) residues 169-STIDYFQPNNKR-180 have been identified as a decoy epitope that diverts the host immune response away from protective epitopes. However, the decoy epitope may include important linear or conformational protective epitopes against PCV2. In this study, we used the baculovirus system to express recombinant complete CP (1–233) and mutant CP (Δ169–180), in which the decoy epitope was deleted, and evaluated the immune response to these in mice. Immunization with mutant CP (Δ169–180) protein, which formed very low level of virus-like particles (VLPs), elicited significantly lower levels of PCV2 CP-specific IgG antibodies and a slightly lower neutralizing activity than immunization with the complete CP (1–233) protein. This finding suggests that the complete CP is important for efficient VLP assembly and induction of PCV2-specific IgG antibodies and neutralizing antibodies in mice. This study may provide useful information for next-generation vaccine design for PCV2 control.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3

Similar content being viewed by others

References

  1. Davies B, Wang X et al (2016) Diagnostic phylogenetics reveals a new porcine circovirus 2 cluster. Virus Res 217:32–37

    Article  CAS  Google Scholar 

  2. Dustin LB, Cashman SB et al (2014) Immune control and failure in HCV infection-tipping the balance. J Leukoc Biol 96(4):535–548

    Article  CAS  Google Scholar 

  3. Fu Y, Jiang L et al (2017) Immunomodulatory and antioxidant effects of total flavonoids of Spatholobus suberectus Dunn on PCV2 infected mice. Sci Rep 7(1):1–9

    Article  CAS  Google Scholar 

  4. Ilha M, Nara P et al (2020) Early antibody responses map to non-protective, PCV2 capsid protein epitopes. Virology 540:23–29

    Article  CAS  Google Scholar 

  5. Jin J, Park C et al (2018) The level of decoy epitope in PCV2 vaccine affects the neutralizing activity of sera in the immunized animals. Biochem Biophys Res Commun 496:846–851

    Article  CAS  Google Scholar 

  6. Khayat R, Brunn N et al (2011) The 2.3-angstrom structure of porcine circovirus 2. J Virol 85(15):7856–7862

  7. Kim K, Choi J et al (2018) Genetic variations in open reading frame 2 gene of porcine circovirus type 2 isolated in Korea during 2016–2017. Korean J Vet Res 58(3):143–146

    Google Scholar 

  8. Kim S, Nazki S et al (2018) The prevalence and genetic characteristics of porcine circovirus type 2 and 3 in Korea. BMC Vet Res 14(1):294

    Article  CAS  Google Scholar 

  9. Lekcharoensuk P, Morozov I et al (2004) Epitope mapping of the major capsid protein of type 2 porcine circovirus (PCV2) by using chimeric PCV1 and PCV2. J Virol 78(15):8135–8145

    Article  CAS  Google Scholar 

  10. Liu L, Suzuki T et al (2008) Efficient production of type 2 porcine circovirus-like particles by a recombinant baculovirus. Arch Virol 153(12):2291

    Article  CAS  Google Scholar 

  11. López-Vidal J, Gómez-Sebastián S et al (2015) Improved production efficiency of virus-like particles by the baculovirus expression vector system. PLoS ONE 10(10):e0140039

    Article  CAS  Google Scholar 

  12. Madson DM, Opriessnig T (2011) Effect of porcine circovirus type 2 (PCV2) infection on reproduction: disease, vertical transmission, diagnostics and vaccination. Anim Health Res Rev 12(1):47–65

    Article  CAS  Google Scholar 

  13. Mahe D, Blanchard P et al (2000) Differential recognition of ORF2 protein from type 1 and type 2 porcine circoviruses and identification of immunorelevant epitopes. J Gen Virol 81(7):1815–1824

    Article  CAS  Google Scholar 

  14. Masuda A, Lee JM et al (2018) Purification and characterization of immunogenic recombinant virus-like particles of porcine circovirus type 2 expressed in silkworm pupae. J Gen Virol 99(7):917–926

    Article  CAS  Google Scholar 

  15. Mo X, Li X et al (2019) Structural roles of PCV2 capsid protein N-terminus in PCV2 particle assembly and identification of PCV2 type-specific neutralizing epitope. PLoS Pathog 15(3):e1007562

    Article  CAS  Google Scholar 

  16. Segalés J, Kekarainen T et al (2013) The natural history of porcine circovirus type 2: from an inoffensive virus to a devastating swine disease? Vet Microbiol 165(1–2):13–20

    Article  CAS  Google Scholar 

  17. Shang S, Jin Y et al (2009) Fine mapping of antigenic epitopes on capsid proteins of porcine circovirus, and antigenic phenotype of porcine circovirus type 2. Mol Immunol 46(3):327–334

    Article  CAS  Google Scholar 

  18. Stamatatos L, Morris L et al (2009) Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine? Nat Med 15(8):866–870

    Article  CAS  Google Scholar 

  19. Szczepanek SM, Barrette RW et al (2012) Xenoepitope substitution avoids deceptive imprinting and broadens the immune response to foot-and-mouth disease virus. Clin Vaccine Immunol 19(4):461–467

    Article  CAS  Google Scholar 

  20. Thaa B, Sinhadri BC et al (2013) Signal peptide cleavage from GP5 of PRRSV: a minor fraction of molecules retains the decoy epitope, a presumed molecular cause for viral persistence. PLoS ONE 8(6):e65548

    Article  CAS  Google Scholar 

  21. Trible BR, Kerrigan M et al (2011) Antibody recognition of porcine circovirus type 2 capsid protein epitopes after vaccination, infection, and disease. Clin Vaccine Immunol 18(5):749–757

    Article  CAS  Google Scholar 

  22. Trible BR, Rowland RR (2012) Genetic variation of porcine circovirus type 2 (PCV2) and its relevance to vaccination, pathogenesis and diagnosis. Virus Res 164(1–2):68–77

    Article  CAS  Google Scholar 

  23. Trible BR, Suddith AW et al (2012) Recognition of the different structural forms of the capsid protein determines the outcome following infection with porcine circovirus type 2. J Virol 86(24):13508–13514

    Article  CAS  Google Scholar 

  24. Worsfold CS, Dardari R et al (2015) Assessment of neutralizing and non-neutralizing antibody responses against Porcine circovirus 2 in vaccinated and non-vaccinated farmed pigs. J Gen Virol 96(9):2743–2748

    Article  CAS  Google Scholar 

  25. Wu P, Lin W et al (2012) Characterization of porcine circovirus type 2 (PCV2) capsid particle assembly and its application to virus-like particle vaccine development. Appl Microbiol Biotechnol 95(6):1501–1507

    Article  CAS  Google Scholar 

  26. Xu X, Wang Z et al (2012) Baculovirus as a PRRSV and PCV2 bivalent vaccine vector: baculovirus virions displaying simultaneously GP5 glycoprotein of PRRSV and capsid protein of PCV2. J Virol Methods 179(2):359–366

    Article  CAS  Google Scholar 

  27. Yu C, Li X et al (2016) Replacing the decoy epitope of PCV2b capsid protein with a protective epitope enhances efficacy of PCV2b vaccine. Vaccine 34(50):6358–6366

    Article  CAS  Google Scholar 

  28. Yu S, Carpenter S et al (2005) Development of a reverse transcription-PCR assay to detect porcine circovirus type 2 transcription as a measure of replication. J Virol Methods 123(1):109–112

    Article  CAS  Google Scholar 

Download references

Acknowledgements

We would like to thank Mrs. Eunjin Hong (Innovac Co.) for technical assistance.

Funding

This study was funded by Small and Medium Business Administration (Grant no. S2785512).

Author information

Authors and Affiliations

  1. College of Veterinary Medicine, Institute of Veterinary Science, Kangwon National University, Chuncheon, 24341, Republic of Korea

    Kiju Kim, Minna Shin & Tae-Wook Hahn

Authors
  1. Kiju Kim
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Minna Shin
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Tae-Wook Hahn
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Tae-Wook Hahn.

Ethics declarations

Conflict of interest

The authors declare that they have no conflict of interest.

Additional information

Handling Editor: Ana Cristina Bratanich.

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Electronic supplementary material

Below is the link to the electronic supplementary material.

Supplementary file1 (JPG 310 kb)

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Kim, K., Shin, M. & Hahn, TW. Deletion of a decoy epitope in porcine circovirus 2 (PCV2) capsid protein affects the protective immune response in mice. Arch Virol 165, 2829–2835 (2020). https://doi.org/10.1007/s00705-020-04831-z

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00705-020-04831-z

Search

Navigation