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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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 |
work_keys_str_mv |
AT libinwen interactionofporcinecircoviruslikevirusp1capsidproteinwithhostproteins AT jiapingzhu interactionofporcinecircoviruslikevirusp1capsidproteinwithhostproteins AT fengxizhang interactionofporcinecircoviruslikevirusp1capsidproteinwithhostproteins AT qixiao interactionofporcinecircoviruslikevirusp1capsidproteinwithhostproteins AT jianpingxie interactionofporcinecircoviruslikevirusp1capsidproteinwithhostproteins AT kongwanghe interactionofporcinecircoviruslikevirusp1capsidproteinwithhostproteins |
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1721358028131794944 |