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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Bibliographic Details
Published in:Frontiers in microbiology 2020-06, Vol.11, p.1129-1129
Main Authors: Zhou, Jianwei, Li, Hanying, Yu, Tianqi, Li, Jiarong, Dong, Weiren, Ojha, Nishant Kumar, Jin, Yulan, Gu, Jinyan, Zhou, Jiyong
Format: Article
Language:English
Subjects:
bioinformatics approach
GO and KEGG analyses
Microbiology
porcine circovirus type 2
protein interactions network
viral capsid
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Summary: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.
ISSN:1664-302X
1664-302X
DOI:10.3389/fmicb.2020.01129