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Protein Interactions Network of Porcine Circovirus Type 2 Capsid With Host Proteins

Virus-host interaction is a tug of war between pathogenesis and immunity, followed by either activating the host immune defense system to eliminate virus or manipulating host immune control mechanisms to survive and facilitate virus propagation. Comprehensive knowledge of interactions between host a...

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Autores principales: Zhou, Jianwei, Li, Hanying, Yu, Tianqi, Li, Jiarong, Dong, Weiren, Ojha, Nishant Kumar, Jin, Yulan, Gu, Jinyan, Zhou, Jiyong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7283462/
https://www.ncbi.nlm.nih.gov/pubmed/32582087
http://dx.doi.org/10.3389/fmicb.2020.01129
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author Zhou, Jianwei
Li, Hanying
Yu, Tianqi
Li, Jiarong
Dong, Weiren
Ojha, Nishant Kumar
Jin, Yulan
Gu, Jinyan
Zhou, Jiyong
author_facet Zhou, Jianwei
Li, Hanying
Yu, Tianqi
Li, Jiarong
Dong, Weiren
Ojha, Nishant Kumar
Jin, Yulan
Gu, Jinyan
Zhou, Jiyong
author_sort Zhou, Jianwei
collection PubMed
description Virus-host interaction is a tug of war between pathogenesis and immunity, followed by either activating the host immune defense system to eliminate virus or manipulating host immune control mechanisms to survive and facilitate virus propagation. Comprehensive knowledge of interactions between host and viral proteins might provide hints for developing novel antiviral strategies. To gain a more detailed knowledge of the interactions with porcine circovirus type 2 capsid protein, we employed a coimmunoprecipitation combined with liquid chromatography mass spectrometry (LC-MS) approach and 222 putative PCV2 Cap-interacting host proteins were identified in the infected porcine kidney (PK-15) cells. Further, a protein-protein interactions (PPIs) network was plotted, and the PCV2 Cap-interacting host proteins were potentially involved in protein binding, DNA transcription, metabolism and innate immune response based on the gene ontology annotation and Kyoto Encyclopedia of Genes and Genomes database enrichment. Verification in vitro assay demonstrated that eight cellular proteins, namely heterogeneous nuclear ribonucleoprotein C, nucleophosmin-1, DEAD-box RNA helicase 21, importin β3, eukaryotic translation initiation factor 4A2, snail family transcriptional repressor 2, MX dynamin like GTPase 2, and intermediate chain 1 interacted with PCV2 Cap. Thus, this work effectively provides useful protein-related information to facilitate further investigation of the underlying mechanism of PCV2 infection and pathogenesis.
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spelling pubmed-72834622020-06-23 Protein Interactions Network of Porcine Circovirus Type 2 Capsid With Host Proteins Zhou, Jianwei Li, Hanying Yu, Tianqi Li, Jiarong Dong, Weiren Ojha, Nishant Kumar Jin, Yulan Gu, Jinyan Zhou, Jiyong Front Microbiol Microbiology Virus-host interaction is a tug of war between pathogenesis and immunity, followed by either activating the host immune defense system to eliminate virus or manipulating host immune control mechanisms to survive and facilitate virus propagation. Comprehensive knowledge of interactions between host and viral proteins might provide hints for developing novel antiviral strategies. To gain a more detailed knowledge of the interactions with porcine circovirus type 2 capsid protein, we employed a coimmunoprecipitation combined with liquid chromatography mass spectrometry (LC-MS) approach and 222 putative PCV2 Cap-interacting host proteins were identified in the infected porcine kidney (PK-15) cells. Further, a protein-protein interactions (PPIs) network was plotted, and the PCV2 Cap-interacting host proteins were potentially involved in protein binding, DNA transcription, metabolism and innate immune response based on the gene ontology annotation and Kyoto Encyclopedia of Genes and Genomes database enrichment. Verification in vitro assay demonstrated that eight cellular proteins, namely heterogeneous nuclear ribonucleoprotein C, nucleophosmin-1, DEAD-box RNA helicase 21, importin β3, eukaryotic translation initiation factor 4A2, snail family transcriptional repressor 2, MX dynamin like GTPase 2, and intermediate chain 1 interacted with PCV2 Cap. Thus, this work effectively provides useful protein-related information to facilitate further investigation of the underlying mechanism of PCV2 infection and pathogenesis. Frontiers Media S.A. 2020-06-03 /pmc/articles/PMC7283462/ /pubmed/32582087 http://dx.doi.org/10.3389/fmicb.2020.01129 Text en Copyright © 2020 Zhou, Li, Yu, Li, Dong, Ojha, Jin, Gu and Zhou. http://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 Microbiology
Zhou, Jianwei
Li, Hanying
Yu, Tianqi
Li, Jiarong
Dong, Weiren
Ojha, Nishant Kumar
Jin, Yulan
Gu, Jinyan
Zhou, Jiyong
Protein Interactions Network of Porcine Circovirus Type 2 Capsid With Host Proteins
title Protein Interactions Network of Porcine Circovirus Type 2 Capsid With Host Proteins
title_full Protein Interactions Network of Porcine Circovirus Type 2 Capsid With Host Proteins
title_fullStr Protein Interactions Network of Porcine Circovirus Type 2 Capsid With Host Proteins
title_full_unstemmed Protein Interactions Network of Porcine Circovirus Type 2 Capsid With Host Proteins
title_short Protein Interactions Network of Porcine Circovirus Type 2 Capsid With Host Proteins
title_sort protein interactions network of porcine circovirus type 2 capsid with host proteins
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7283462/
https://www.ncbi.nlm.nih.gov/pubmed/32582087
http://dx.doi.org/10.3389/fmicb.2020.01129
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