Peptides mimicking viral proteins of porcine circovirus type 2 were profiled by the spectrum of mouse anti-PCV2 antibodies
Abstract Background Porcine circovirus 2 (PCV2) is a small, non-enveloped DNA virus causing swine lymphocyte depletion and severe impact on the swine industry. The aim of this study was to evaluate the antigenicity and immunogenicity of specific peptides, and seeking the potential candidate of PCV2...
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BMC
2017-05-01
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Series: | BMC Immunology |
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Online Access: | http://link.springer.com/article/10.1186/s12865-017-0211-2 |
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author | Ling-Chu Hung Cheng-Yao Yang Ivan-Chen Cheng |
author_facet | Ling-Chu Hung Cheng-Yao Yang Ivan-Chen Cheng |
author_sort | Ling-Chu Hung |
collection | DOAJ |
description | Abstract Background Porcine circovirus 2 (PCV2) is a small, non-enveloped DNA virus causing swine lymphocyte depletion and severe impact on the swine industry. The aim of this study was to evaluate the antigenicity and immunogenicity of specific peptides, and seeking the potential candidate of PCV2 peptide-based vaccine. It’s initiating from peptides reacting with PCV2-infected pig sera and peptide-immunized mouse sera. Results The data showed that the sera from PCV2-infected pigs could react with the N-terminal (C1), middle region (C2), and C-terminal peptide (C3) of PCV2 capsid protein (CP), ORF3 protein (N1), ORF6 protein (N2) and ORF9 protein (N3). This study demonstrated that anti-PCV2 mouse antisera could be generated by specific synthetic peptides (C3 and N2) and recognized PCV2 viral protein. We found that the tertiary or linear form C-terminal sequence (C3) of PCV2 capsid peptide only appeared a local distribution in the nucleus of PCV2-infected PK cells, virus-like particles of PCV2 major appeared a local distribution in the cytoplasm, and ORF 6 protein of PCV2 were shown unusually in cytoplasm. Furthermore, most residues of the C1 and the C3 were presented on the surface of PCV2 CP, in the view of 3-D structure of the CP. Our data demonstrated that PCV2-infected pigs had higher OD405 value of anti-C3 IgG on Day 1, Month 3 and Month 6 than in Month 1. These pigs had higher anti-C3 IgM level in Month 3 and Month 6 than on Day 1 (P < 0.01). Conclusions We demonstrated that the key peptide (C3) mimic the C-terminal of PCV2 capsid protein which were capable of inducing antibodies. The specific antibody against the C3 were confirmed as the serological marker in PCV2-infected pigs. |
first_indexed | 2024-12-10T16:17:50Z |
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language | English |
last_indexed | 2024-12-10T16:17:50Z |
publishDate | 2017-05-01 |
publisher | BMC |
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series | BMC Immunology |
spelling | doaj.art-22c736834a514bcc8abeca80b0e649dd2022-12-22T01:41:54ZengBMCBMC Immunology1471-21722017-05-0118111310.1186/s12865-017-0211-2Peptides mimicking viral proteins of porcine circovirus type 2 were profiled by the spectrum of mouse anti-PCV2 antibodiesLing-Chu Hung0Cheng-Yao Yang1Ivan-Chen Cheng2Animal Health Research Institute, Council of Agriculture, Executive YuanAgricultural Technology Research InstituteSchool of Veterinary Medicine, National Taiwan UniversityAbstract Background Porcine circovirus 2 (PCV2) is a small, non-enveloped DNA virus causing swine lymphocyte depletion and severe impact on the swine industry. The aim of this study was to evaluate the antigenicity and immunogenicity of specific peptides, and seeking the potential candidate of PCV2 peptide-based vaccine. It’s initiating from peptides reacting with PCV2-infected pig sera and peptide-immunized mouse sera. Results The data showed that the sera from PCV2-infected pigs could react with the N-terminal (C1), middle region (C2), and C-terminal peptide (C3) of PCV2 capsid protein (CP), ORF3 protein (N1), ORF6 protein (N2) and ORF9 protein (N3). This study demonstrated that anti-PCV2 mouse antisera could be generated by specific synthetic peptides (C3 and N2) and recognized PCV2 viral protein. We found that the tertiary or linear form C-terminal sequence (C3) of PCV2 capsid peptide only appeared a local distribution in the nucleus of PCV2-infected PK cells, virus-like particles of PCV2 major appeared a local distribution in the cytoplasm, and ORF 6 protein of PCV2 were shown unusually in cytoplasm. Furthermore, most residues of the C1 and the C3 were presented on the surface of PCV2 CP, in the view of 3-D structure of the CP. Our data demonstrated that PCV2-infected pigs had higher OD405 value of anti-C3 IgG on Day 1, Month 3 and Month 6 than in Month 1. These pigs had higher anti-C3 IgM level in Month 3 and Month 6 than on Day 1 (P < 0.01). Conclusions We demonstrated that the key peptide (C3) mimic the C-terminal of PCV2 capsid protein which were capable of inducing antibodies. The specific antibody against the C3 were confirmed as the serological marker in PCV2-infected pigs.http://link.springer.com/article/10.1186/s12865-017-0211-2Porcine circovirus type 2PeptideMimicOpen reading frame proteinsAntibody |
spellingShingle | Ling-Chu Hung Cheng-Yao Yang Ivan-Chen Cheng Peptides mimicking viral proteins of porcine circovirus type 2 were profiled by the spectrum of mouse anti-PCV2 antibodies BMC Immunology Porcine circovirus type 2 Peptide Mimic Open reading frame proteins Antibody |
title | Peptides mimicking viral proteins of porcine circovirus type 2 were profiled by the spectrum of mouse anti-PCV2 antibodies |
title_full | Peptides mimicking viral proteins of porcine circovirus type 2 were profiled by the spectrum of mouse anti-PCV2 antibodies |
title_fullStr | Peptides mimicking viral proteins of porcine circovirus type 2 were profiled by the spectrum of mouse anti-PCV2 antibodies |
title_full_unstemmed | Peptides mimicking viral proteins of porcine circovirus type 2 were profiled by the spectrum of mouse anti-PCV2 antibodies |
title_short | Peptides mimicking viral proteins of porcine circovirus type 2 were profiled by the spectrum of mouse anti-PCV2 antibodies |
title_sort | peptides mimicking viral proteins of porcine circovirus type 2 were profiled by the spectrum of mouse anti pcv2 antibodies |
topic | Porcine circovirus type 2 Peptide Mimic Open reading frame proteins Antibody |
url | http://link.springer.com/article/10.1186/s12865-017-0211-2 |
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