Abstract
African swine fever virus (ASFV) is prevalent in many countries and is a contagious and lethal virus that infects pigs, posing a threat to the global pig industry and public health. The interaction between the virus and the host is key to unlocking the mystery behind viral pathogenesis. A comprehensive understanding of the viral and host protein interaction may provide clues for developing new antiviral strategies. Here, we show a network of ASFV MGF360-9L protein interactions in porcine kidney (PK-15) cells. Overall, 268 proteins that interact with MGF360-9L are identified using immunoprecipitation and liquid chromatography–mass spectrometry (LC-MS). Accordingly, gene ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses were conducted, and the protein–protein interaction (PPI) network was created. It was speculated that the cellular proteins interacting with MGF360-9L are involved in protein binding, metabolism, and the innate immune response. Proteasome subunit alpha type (PSMA3), 26S protease regulatory subunit 4 (PSMC1), autophagy and beclin 1 regulator 1 (AMBRA1), and DEAD-box helicase 20 (DDX20) could interact with MGF360-9L in vitro. PSMA3 and PSMC1 overexpression significantly promoted ASFV replication, and MGF360-9L maintained the transcriptional level of PSMA3 and PSMC1. Here, we show the interaction between ASFV MGF360-9L and cellular proteins and elucidate the virus–host interaction network, which effectively provides useful protein-related information that can enable further study of the potential mechanism and pathogenesis of ASFV infection.
Highlights
African swine fever (ASF) is a highly pathogenic infectious disease caused by the African swine fever virus (ASFV), the only member of the Afarviridae family
To identify the potential host protein binding to MGF360-9L, the 3 × FLAG tag MGF3609L plasmid and empty FLAG were transfected into PK-15 cells for co-immunoprecipitation and liquid chromatography–mass spectrometry (LC-MS) analysis
MGF360-9L-interacting host proteins were eluted with protein A/G sepharose and analyzed on SDS-PAGE followed by silver staining. β-actin was used as a loading control
Summary
African swine fever (ASF) is a highly pathogenic infectious disease caused by the African swine fever virus (ASFV), the only member of the Afarviridae family. As there are no effective and specific drugs or commercial vaccines at present, stringent prevention and control measures to conduct early laboratory diagnosis and culling of animals infected with ASFV and those with suspected infections are generally and internationally accepted. This has caused substantial economic losses in countries where outbreaks have occurred and posed a significant threat to global food safety and supply [5,6]. Despite researchers’ efforts, due to the large number of proteins encoded by ASFV, there are still many proteins whose functions are unknown
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