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Structure, Antigenic Properties, and Highly Efficient Assembly of PCV4 Capsid Protein
Porcine circovirus type 4 (PCV4), a recently reported circovirus, was first identified in pigs with clinical signs similar to porcine dermatitis nephropathy syndrome (PDNS), in Hunan province, China, in 2019. More knowledge regarding the assembly of capsid protein (Cap) into virus-like particles (VL...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8421537/ https://www.ncbi.nlm.nih.gov/pubmed/34504886 http://dx.doi.org/10.3389/fvets.2021.695466 |
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author | Wang, Dongliang Mai, Jinhui Lei, Bo Zhang, Yingjie Yang, Yi Wang, Naidong |
author_facet | Wang, Dongliang Mai, Jinhui Lei, Bo Zhang, Yingjie Yang, Yi Wang, Naidong |
author_sort | Wang, Dongliang |
collection | PubMed |
description | Porcine circovirus type 4 (PCV4), a recently reported circovirus, was first identified in pigs with clinical signs similar to porcine dermatitis nephropathy syndrome (PDNS), in Hunan province, China, in 2019. More knowledge regarding the assembly of capsid protein (Cap) into virus-like particles (VLPs), their structure and antigenic properties, are needed to provide new knowledge for diagnosis and further characterization of PCV4. In this study, high-level expression of PCV4 Cap was achieved in Escherichia coli with purified Cap self-assembling into VLPs (~20 nm) in vitro. Furthermore, these VLPs were internalized in vitro by PK15 and 3D4/21 cell lines. Significant structural differences between PCV4 and PCV2 capsids were demonstrated among loops (loop BC, CD, DE, EF, and GH), based on comparisons of 3D structures. In addition, five potential B cell epitopes identified in silico were mostly located in surface-exposed loops of PCV4 capsid. Cross-reaction between PCV4 and PCV2 or PCV3 conferred by humoral immune responses was deemed unlikely on the basis of ELISA and Western blotting for assessment of VLPs and using PCV4 or PCV2 VLPs. In conclusion, these studies provided new knowledge regarding PCV4 capsid surface patterns. It is noteworthy that the PCV4 VLPs prepared in our study have much potential for development of serological diagnostics for PCV4 and to further characterize this virus. |
format | Online Article Text |
id | pubmed-8421537 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-84215372021-09-08 Structure, Antigenic Properties, and Highly Efficient Assembly of PCV4 Capsid Protein Wang, Dongliang Mai, Jinhui Lei, Bo Zhang, Yingjie Yang, Yi Wang, Naidong Front Vet Sci Veterinary Science Porcine circovirus type 4 (PCV4), a recently reported circovirus, was first identified in pigs with clinical signs similar to porcine dermatitis nephropathy syndrome (PDNS), in Hunan province, China, in 2019. More knowledge regarding the assembly of capsid protein (Cap) into virus-like particles (VLPs), their structure and antigenic properties, are needed to provide new knowledge for diagnosis and further characterization of PCV4. In this study, high-level expression of PCV4 Cap was achieved in Escherichia coli with purified Cap self-assembling into VLPs (~20 nm) in vitro. Furthermore, these VLPs were internalized in vitro by PK15 and 3D4/21 cell lines. Significant structural differences between PCV4 and PCV2 capsids were demonstrated among loops (loop BC, CD, DE, EF, and GH), based on comparisons of 3D structures. In addition, five potential B cell epitopes identified in silico were mostly located in surface-exposed loops of PCV4 capsid. Cross-reaction between PCV4 and PCV2 or PCV3 conferred by humoral immune responses was deemed unlikely on the basis of ELISA and Western blotting for assessment of VLPs and using PCV4 or PCV2 VLPs. In conclusion, these studies provided new knowledge regarding PCV4 capsid surface patterns. It is noteworthy that the PCV4 VLPs prepared in our study have much potential for development of serological diagnostics for PCV4 and to further characterize this virus. Frontiers Media S.A. 2021-08-24 /pmc/articles/PMC8421537/ /pubmed/34504886 http://dx.doi.org/10.3389/fvets.2021.695466 Text en Copyright © 2021 Wang, Mai, Lei, Zhang, Yang and Wang. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Veterinary Science Wang, Dongliang Mai, Jinhui Lei, Bo Zhang, Yingjie Yang, Yi Wang, Naidong Structure, Antigenic Properties, and Highly Efficient Assembly of PCV4 Capsid Protein |
title | Structure, Antigenic Properties, and Highly Efficient Assembly of PCV4 Capsid Protein |
title_full | Structure, Antigenic Properties, and Highly Efficient Assembly of PCV4 Capsid Protein |
title_fullStr | Structure, Antigenic Properties, and Highly Efficient Assembly of PCV4 Capsid Protein |
title_full_unstemmed | Structure, Antigenic Properties, and Highly Efficient Assembly of PCV4 Capsid Protein |
title_short | Structure, Antigenic Properties, and Highly Efficient Assembly of PCV4 Capsid Protein |
title_sort | structure, antigenic properties, and highly efficient assembly of pcv4 capsid protein |
topic | Veterinary Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8421537/ https://www.ncbi.nlm.nih.gov/pubmed/34504886 http://dx.doi.org/10.3389/fvets.2021.695466 |
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