Korean Journal of Veterinary Research (대한수의학회지)

The Korean Society of Veterinary Science (대한수의학회)
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Genetic variations in open reading frame 2 gene of porcine circovirus type 2 isolated in Korea during 2016-2017

  • Kim, Kiju (College of Veterinary Medicine & Institute of Veterinary Science, Kangwon National University) ;
  • Choi, Jong-Young (College of Veterinary Medicine & Institute of Veterinary Science, Kangwon National University) ;
  • Lyoo, Kwang-Soo (Korea Zoonosis Research Institute, Chonbuk National University) ;
  • Hahn, Tae-Wook (College of Veterinary Medicine & Institute of Veterinary Science, Kangwon National University)
  • Received : 2018.06.21
  • Accepted : 2018.07.18
  • Published : 2018.09.30
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Abstract

The capsid protein of porcine circovirus type 2 (PCV2) encoded by open reading frame 2 (ORF2) is important for neutralizing activity against PCV2 infection. This study investigated the heterogeneity of the ORF2 gene of PCV2 isolated in Korea during 2016-2017. The results revealed that PCV2d is currently the predominant genotype. Moreover, comparison of ORF2 from 17 PCV2 isolates revealed 88.3-100% homology at the nucleotide (deduced amino acid 86.3-100%) level. Interestingly, 61.5% (8/13) of the PCV2d isolates had glycine at position 210. These data provide a useful information for PCV2 epidemiology in Korea.

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References

  1. Allan G, Krakowka S, Ellis J, Charreyre C. Discovery and evolving history of two genetically related but phenotypically different viruses, porcine circoviruses 1 and 2. Virus Res 2012, 164, 4-9. https://doi.org/10.1016/j.virusres.2011.09.013
  2. Choi C, Chae C. In-situ hybridization for the detection of porcine circovirus in pigs with postweaning multisystemic wasting syndrome. J Comp Pathol 1999, 121, 265-270. https://doi.org/10.1053/jcpa.1999.0315
  3. Cooper CA, Gasteiger E, Packer NH. GlycoMod-a software tool for determining glycosylation compositions from mass spectrometric data. Proteomics 2001, 1, 340-349. https://doi.org/10.1002/1615-9861(200102)1:2<340::AID-PROT340>3.0.CO;2-B
  4. Huang LP, Lu YH, Wei YW, Guo LJ, Liu CM. Identification of one critical amino acid that determines a conformational neutralizing epitope in the capsid protein of porcine circovirus type 2. BMC Microbiol 2011, 11, 188. https://doi.org/10.1186/1471-2180-11-188
  5. Jin J, Park C, Cho SH, Chung J. The level of decoy epitope in PCV2 vaccine affects the neutralizing activity of sera in the immunized animals. Biochem Biophys Res Commun 2018, 496, 846-851. https://doi.org/10.1016/j.bbrc.2018.01.141
  6. Kedkovid R, Woonwong Y, Arunorat J, Sirisereewan C, Sangpratum N, Kesdangsakonwut S, Tummaruk P, Teankum K, Assavacheep P, Jittimanee S, Thanawongnuwech R. Porcine circovirus type 3 (PCV3) shedding in sow colostrum. Vet Microbiol 2018, 220, 12-17. https://doi.org/10.1016/j.vetmic.2018.04.032
  7. Kim D, Ha Y, Oh Y, Chae C. Prevalence of porcine circovirus types 2a and b in pigs with and without postweaning multi-systemic wasting syndrome. Vet J 2011, 188, 115-117. https://doi.org/10.1016/j.tvjl.2010.02.006
  8. Kwon T, Lee DU, Yoo SJ, Je SH, Shin JY, Lyoo YS. Genotypic diversity of porcine circovirus type 2 (PCV2) and genotype shift to PCV2d in Korean pig population. Virus Res 2017, 228, 24-29. https://doi.org/10.1016/j.virusres.2016.11.015
  9. Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, McWilliam H, Valentin F, Wallace IM, Wilm A, Lopez R, Thompson JD, Gibson TJ, Higgins DG. Clustal W and Clustal X version 2.0. Bioinformatics 2007, 23, 2947-2948. https://doi.org/10.1093/bioinformatics/btm404
  10. Misinzo G, Delputte PL, Meerts P, Lefebvre DJ, Nauwynck HJ. Porcine circovirus 2 uses heparan sulfate and chondroitin sulfate B glycosaminoglycans as receptors for its attachment to host cells. J Virol 2006, 80, 3487-3494. https://doi.org/10.1128/JVI.80.7.3487-3494.2006
  11. Olvera A, Cortey M, Segales J. Molecular evolution of porcine circovirus type 2 genomes: phylogeny and clonality. Virology 2007, 357, 175-185. https://doi.org/10.1016/j.virol.2006.07.047
  12. Opriessnig T, Xiao CT, Gerber PF, Halbur PG. Emergence of a novel mutant PCV2b variant associated with clinical PCVAD in two vaccinated pig farms in the U.S. concurrently infected with PPV2. Vet Microbiol 2013, 163, 177-183. https://doi.org/10.1016/j.vetmic.2012.12.019
  13. Ramos N, Mirazo S, Castro G, Arbiza J. First identification of porcine circovirus type 2b mutant in pigs from Uruguay. Infect Genet Evol 2015, 33, 320-323. https://doi.org/10.1016/j.meegid.2015.05.023
  14. Shang SB, Jin YL, Jiang X, Zhou JY, Zhang X, Xing G, He JL, Yan Y. Fine mapping of antigenic epitopes on capsid proteins of porcine circovirus, and antigenic phenotype of porcine circovirus type 2. Mol Immunol 2009, 46, 327-334. https://doi.org/10.1016/j.molimm.2008.10.028
  15. Tamura K, Stecher G, Peterson D, Filipski A, Kumar S. MEGA6: Molecular Evolutionary Genetics Analysis version 6.0. Mol Biol Evol 2013, 30, 2725-2729. https://doi.org/10.1093/molbev/mst197
  16. Tischer I, Gelderblom H, Vettermann W, Koch MA. A very small porcine virus with circular single-stranded DNA. Nature 1982, 295, 64-66. https://doi.org/10.1038/295064a0
  17. Trible BR, Kerrigan M, Crossland N, Potter M, Faaberg K, Hesse R, Rowland RRR. Antibody recognition of porcine circovirus type 2 capsid protein epitopes after vaccination, infection, and disease. Clin Vaccine Immunol 2011, 18, 749-757. https://doi.org/10.1128/CVI.00418-10
  18. Trible BR, Rowland RRR. Genetic variation of porcine circovirus type 2 (PCV2) and its relevance to vaccination, pathogenesis and diagnosis. Virus Res 2012, 164, 68-77. https://doi.org/10.1016/j.virusres.2011.11.018
  19. Trible BR, Suddith AW, Kerrigan MA, Cino-Ozuna AG, Hesse RA, Rowland RRR. Recognition of the different structural forms of the capsid protein determines the outcome following infection with porcine circovirus type 2. J Virol 2012, 86, 13508-13514. https://doi.org/10.1128/JVI.01763-12