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Interaction of porcine circovirus-like virus P1 capsid protein with host proteins
BACKGROUND: Porcine circovirus-like virus P1 is a relatively new kind of virus that is closely related to the post-weaning multisystemic wasting syndrome, congenital tremors, and abortions in swine. The molecular mechanisms of P1 virus infection and pathogenesis are fully unknown. To analyze P1 and...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8235626/ https://www.ncbi.nlm.nih.gov/pubmed/34174877 http://dx.doi.org/10.1186/s12917-021-02926-6 |
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author | Wen, Libin Zhu, Jiaping Zhang, Fengxi Xiao, Qi Xie, Jianping He, Kongwang |
author_facet | Wen, Libin Zhu, Jiaping Zhang, Fengxi Xiao, Qi Xie, Jianping He, Kongwang |
author_sort | Wen, Libin |
collection | PubMed |
description | BACKGROUND: Porcine circovirus-like virus P1 is a relatively new kind of virus that is closely related to the post-weaning multisystemic wasting syndrome, congenital tremors, and abortions in swine. The molecular mechanisms of P1 virus infection and pathogenesis are fully unknown. To analyze P1 and its host interactions, we used a yeast two-hybrid (Y2H) assay to identify cellular proteins interacting with the Cap of the P1 virus. In this study, the Cap of the P1 virus exhibited no self-activation and toxicity to yeast cells and was used as bait to screen the Y2H library prepared from the pancreas tissue. RESULTS: Five cellular proteins (EEP, Ral GDS, Bcl-2-L-12, CPS1, and one not identified) were found to interact with P1 Cap. The interaction between Cap and Ral GDS was confirmed by co-immunoprecipitation. CONCLUSIONS: Our data are likely to support the future investigation of the underlying mechanism of P1 infection and pathogenesis. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12917-021-02926-6. |
format | Online Article Text |
id | pubmed-8235626 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-82356262021-06-28 Interaction of porcine circovirus-like virus P1 capsid protein with host proteins Wen, Libin Zhu, Jiaping Zhang, Fengxi Xiao, Qi Xie, Jianping He, Kongwang BMC Vet Res Research BACKGROUND: Porcine circovirus-like virus P1 is a relatively new kind of virus that is closely related to the post-weaning multisystemic wasting syndrome, congenital tremors, and abortions in swine. The molecular mechanisms of P1 virus infection and pathogenesis are fully unknown. To analyze P1 and its host interactions, we used a yeast two-hybrid (Y2H) assay to identify cellular proteins interacting with the Cap of the P1 virus. In this study, the Cap of the P1 virus exhibited no self-activation and toxicity to yeast cells and was used as bait to screen the Y2H library prepared from the pancreas tissue. RESULTS: Five cellular proteins (EEP, Ral GDS, Bcl-2-L-12, CPS1, and one not identified) were found to interact with P1 Cap. The interaction between Cap and Ral GDS was confirmed by co-immunoprecipitation. CONCLUSIONS: Our data are likely to support the future investigation of the underlying mechanism of P1 infection and pathogenesis. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12917-021-02926-6. BioMed Central 2021-06-26 /pmc/articles/PMC8235626/ /pubmed/34174877 http://dx.doi.org/10.1186/s12917-021-02926-6 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Research Wen, Libin Zhu, Jiaping Zhang, Fengxi Xiao, Qi Xie, Jianping He, Kongwang Interaction of porcine circovirus-like virus P1 capsid protein with host proteins |
title | Interaction of porcine circovirus-like virus P1 capsid protein with host proteins |
title_full | Interaction of porcine circovirus-like virus P1 capsid protein with host proteins |
title_fullStr | Interaction of porcine circovirus-like virus P1 capsid protein with host proteins |
title_full_unstemmed | Interaction of porcine circovirus-like virus P1 capsid protein with host proteins |
title_short | Interaction of porcine circovirus-like virus P1 capsid protein with host proteins |
title_sort | interaction of porcine circovirus-like virus p1 capsid protein with host proteins |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8235626/ https://www.ncbi.nlm.nih.gov/pubmed/34174877 http://dx.doi.org/10.1186/s12917-021-02926-6 |
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