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A High-Throughput Method to Analyze the Interaction Proteins With p22 Protein of African Swine Fever Virus In Vitro
African swine fever virus (ASFV) has been identified as the agent of African swine fever, resulting in a mortality rate of nearly 100% in domestic pigs worldwide. Protein p22 encoded by gene KP177R has been reported to be localized at the inner envelope of the virus, while the function of p22 remain...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8450437/ https://www.ncbi.nlm.nih.gov/pubmed/34552974 http://dx.doi.org/10.3389/fvets.2021.719859 |
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author | Zhu, Xuejiao Fan, Baochao Zhou, Junming Wang, Dandan Fan, Huiying Li, Bin |
author_facet | Zhu, Xuejiao Fan, Baochao Zhou, Junming Wang, Dandan Fan, Huiying Li, Bin |
author_sort | Zhu, Xuejiao |
collection | PubMed |
description | African swine fever virus (ASFV) has been identified as the agent of African swine fever, resulting in a mortality rate of nearly 100% in domestic pigs worldwide. Protein p22 encoded by gene KP177R has been reported to be localized at the inner envelope of the virus, while the function of p22 remains unclear. In this study, p22 interacting proteins of the host were identified by a high-throughput method and analyzed by Gene ontology terms and Kyoto Encyclopedia of Gene and Genomes (KEGG) pathways; numerous cellular proteins in 293-T that interacted with p22 protein were identified. These interacting proteins were related to the biological processes of binding, cell structure, signal transduction, cell adhesion, etc. At the same time, the interacted proteins participated in several KEGG pathways like ribosome, spliceosome, etc. The key proteins in the protein–protein interaction network were closely related to actin filament organization and movement, resulting in affecting the process of phagocytosis and endocytosis. A large number of proteins that interacted with p22 were identified, providing a large database, which should be very useful to elucidate the function of p22 in the near future, laying the foundation for elucidating the mechanism of ASFV. |
format | Online Article Text |
id | pubmed-8450437 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-84504372021-09-21 A High-Throughput Method to Analyze the Interaction Proteins With p22 Protein of African Swine Fever Virus In Vitro Zhu, Xuejiao Fan, Baochao Zhou, Junming Wang, Dandan Fan, Huiying Li, Bin Front Vet Sci Veterinary Science African swine fever virus (ASFV) has been identified as the agent of African swine fever, resulting in a mortality rate of nearly 100% in domestic pigs worldwide. Protein p22 encoded by gene KP177R has been reported to be localized at the inner envelope of the virus, while the function of p22 remains unclear. In this study, p22 interacting proteins of the host were identified by a high-throughput method and analyzed by Gene ontology terms and Kyoto Encyclopedia of Gene and Genomes (KEGG) pathways; numerous cellular proteins in 293-T that interacted with p22 protein were identified. These interacting proteins were related to the biological processes of binding, cell structure, signal transduction, cell adhesion, etc. At the same time, the interacted proteins participated in several KEGG pathways like ribosome, spliceosome, etc. The key proteins in the protein–protein interaction network were closely related to actin filament organization and movement, resulting in affecting the process of phagocytosis and endocytosis. A large number of proteins that interacted with p22 were identified, providing a large database, which should be very useful to elucidate the function of p22 in the near future, laying the foundation for elucidating the mechanism of ASFV. Frontiers Media S.A. 2021-09-06 /pmc/articles/PMC8450437/ /pubmed/34552974 http://dx.doi.org/10.3389/fvets.2021.719859 Text en Copyright © 2021 Zhu, Fan, Zhou, Wang, Fan and Li. 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 Zhu, Xuejiao Fan, Baochao Zhou, Junming Wang, Dandan Fan, Huiying Li, Bin A High-Throughput Method to Analyze the Interaction Proteins With p22 Protein of African Swine Fever Virus In Vitro |
title | A High-Throughput Method to Analyze the Interaction Proteins With p22 Protein of African Swine Fever Virus In Vitro |
title_full | A High-Throughput Method to Analyze the Interaction Proteins With p22 Protein of African Swine Fever Virus In Vitro |
title_fullStr | A High-Throughput Method to Analyze the Interaction Proteins With p22 Protein of African Swine Fever Virus In Vitro |
title_full_unstemmed | A High-Throughput Method to Analyze the Interaction Proteins With p22 Protein of African Swine Fever Virus In Vitro |
title_short | A High-Throughput Method to Analyze the Interaction Proteins With p22 Protein of African Swine Fever Virus In Vitro |
title_sort | high-throughput method to analyze the interaction proteins with p22 protein of african swine fever virus in vitro |
topic | Veterinary Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8450437/ https://www.ncbi.nlm.nih.gov/pubmed/34552974 http://dx.doi.org/10.3389/fvets.2021.719859 |
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