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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...

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Autores principales: Wang, Dongliang, Mai, Jinhui, Lei, Bo, Zhang, Yingjie, Yang, Yi, Wang, Naidong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
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.
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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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