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|Title:||Structural insight into the type-specific epitope of porcine circovirus type 3||Authors:||Bi, M.
|Issue Date:||2020||Publisher:||Portland Press Ltd||Citation:||Bi, M., Li, X., Zhai, W., Yin, B., Tian, K., Mo, X. (2020). Structural insight into the type-specific epitope of porcine circovirus type 3. Bioscience Reports 40 (6) : BSR20201109. ScholarBank@NUS Repository. https://doi.org/10.1042/BSR20201109||Rights:||Attribution 4.0 International||Abstract:||The recently identified pathogenic Porcine circovirus type 3 (PCV3) may threaten to reduce the pig population dramatically worldwide. In our previous study, a PCV3-specific monoclonal antibody (mAb-1H11) was successfully applied in immune-histochemistry staining and ELISA, which specifically recognize PCV3 capsid protein in PCV3-positive pig tissues. In the present study, we expressed and purified the soluble sole capsid protein of PCV3. The purified capsid protein was capable of self-assembly into virus-like-particles (VLPs), which is validated by transmission electron microscopy and dynamic light scattering assays. Moreover, the epitope of mAb-1H11 was identified in the CD-loop region (a.a. 72-79) on the VLP surface, which is confirmed by PCV2-PCV3 epitope swapping assay. For the first time, we determined the cryo-EM structure of PCV3-VLP at 8.5 Å resolution that reveals the detailed structural information of PCV3-VLP. In our cryo-EM structure, PCV3-VLP is composed of 60 capsid protein subunits assembled with T = 1 icosahedral symmetry. Consistent to our bio-dot Western blot assay, the structural comparison between PCV3 and PCV2 revealed significant structural differences in the surface-exposed loops, including the CD-loop (a.a. 72-79) and the EF-loop (a.a. 109-131). Our work provides a structural framework for engineering future PCV3 vaccine and diagnosis kits development. © 2020 The Author(s).||Source Title:||Bioscience Reports||URI:||https://scholarbank.nus.edu.sg/handle/10635/196370||ISSN:||01448463||DOI:||10.1042/BSR20201109||Rights:||Attribution 4.0 International|
|Appears in Collections:||Staff Publications|
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