Interaction of porcine circovirus-like virus P1 capsid protein with host proteins

Abstract 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...

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Main Authors: Libin Wen, Jiaping Zhu, Fengxi Zhang, Qi Xiao, Jianping Xie, Kongwang He
Format: Article
Language:English
Published: BMC 2021-06-01
Series:BMC Veterinary Research
Subjects:
Cap
Online Access:https://doi.org/10.1186/s12917-021-02926-6
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spelling doaj-9211d7f8d85a4497a086dceb5e8451b72021-06-27T11:16:18ZengBMCBMC Veterinary Research1746-61482021-06-011711910.1186/s12917-021-02926-6Interaction of porcine circovirus-like virus P1 capsid protein with host proteinsLibin Wen0Jiaping Zhu1Fengxi Zhang2Qi Xiao3Jianping Xie4Kongwang He5Institute of Veterinary Medicine, Jiangsu Academy of Agricultural SciencesInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural SciencesInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural SciencesInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural SciencesInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural SciencesInstitute of Veterinary Medicine, Jiangsu Academy of Agricultural SciencesAbstract 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.https://doi.org/10.1186/s12917-021-02926-6Porcine circovirus-like virus P1yeast two-hybrid assayCapcellular proteinco-immunoprecipitation
collection DOAJ
language English
format Article
sources DOAJ
author Libin Wen
Jiaping Zhu
Fengxi Zhang
Qi Xiao
Jianping Xie
Kongwang He
spellingShingle Libin Wen
Jiaping Zhu
Fengxi Zhang
Qi Xiao
Jianping Xie
Kongwang He
Interaction of porcine circovirus-like virus P1 capsid protein with host proteins
BMC Veterinary Research
Porcine circovirus-like virus P1
yeast two-hybrid assay
Cap
cellular protein
co-immunoprecipitation
author_facet Libin Wen
Jiaping Zhu
Fengxi Zhang
Qi Xiao
Jianping Xie
Kongwang He
author_sort Libin Wen
title 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_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_sort interaction of porcine circovirus-like virus p1 capsid protein with host proteins
publisher BMC
series BMC Veterinary Research
issn 1746-6148
publishDate 2021-06-01
description Abstract 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.
topic Porcine circovirus-like virus P1
yeast two-hybrid assay
Cap
cellular protein
co-immunoprecipitation
url https://doi.org/10.1186/s12917-021-02926-6
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AT qixiao interactionofporcinecircoviruslikevirusp1capsidproteinwithhostproteins
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