https://scholars.lib.ntu.edu.tw/handle/123456789/638108
標題: | Exploring the surface epitope and nuclear localization analysis of porcine circovirus type 3 capsid protein | 作者: | Chang, Chia Chun Wu, Ching Ying Ciou, Jhao Guan Wu, Ching Wei Wang, Yi Chen HUI-WEN CHANG Chien, Maw Sheng Huang, Chienjin |
關鍵字: | Capsid protein | Cytotoxicity | Monoclonal antibody | Nuclear localization | Porcine circovirus 3 | Virus-like particle | 公開日期: | 1-十二月-2023 | 卷: | 13 | 期: | 1 | 來源出版物: | AMB Express | 摘要: | Porcine circovirus 3 (PCV3) is a newly emerging virus associated with porcine dermatitis and nephropathy syndrome (PDNS) and reproductive disorders, impacting global pig populations. Porcine circoviruses contain two major open reading frames (ORFs), and the ORF2 encodes the viral capsid protein (Cap). Cap is the most antigenic structural protein and an ideal candidate for the development of vaccines and diagnostic reagents. This study generated a monoclonal antibody (MAb) specific to PCV3 Cap, MAb CCC160, for diagnosis and pathogenesis studies of this novel virus. The MAb specifically recognized PCV3-infected swine lymph node tissue in an immunohistochemical analysis confirming its clinical diagnostic potential. In addition, a novel linear B-cell epitope recognized by MAb CCC160 was identified at the amino acid region 120–134 of Cap. Nuclear localization analysis of PCV3 Cap revealed a potential nuclear localization signal (NLS) in the middle region (aa 131–143) in addition to the dominant N-terminal NLS that is already known. A cell viability assay further demonstrated that the cytotoxicity of PCV3 Cap is correlated with its nuclear localization, indicating a crucial role of Cap in the pathogenic mechanism of PCV3. A full-length construct of PCV3 Cap was successfully expressed using a baculovirus expression system and purified recombinant proteins self-assembled into virus-like particles (VLPs). The protein constitution of the VLPs was confirmed by MAb CCC160 recognition, indicating the correct conformation and specificity of VLP and exhibiting the linear epitope aa 120–134 on the VLP surface. These results provide insights for developing diagnostic tools and potential VLP vaccines for PCV3, revealing its pathogenesis and antigenic properties. |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85178961029&doi=10.1186%2fs13568-023-01652-6&partnerID=40&md5=d2cd126ed821982093ab9a0a24022c13 https://scholars.lib.ntu.edu.tw/handle/123456789/638108 |
ISSN: | 2191-0855 | DOI: | 10.1186/s13568-023-01652-6 |
顯示於: | 分子暨比較病理生物學研究所 |
在 IR 系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。