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Proteomics study reveals that ASFV g5Rp protein interacts with eukaryotic translation initiation factor 5A and may regulate host translation

ABSTRACT: African Swine fever virus (ASFV) decapacitase (g5Rp) hydrolyses the 5’ cap structure on cellular mRNA, facilitating the expression of viral genes in the early stages of ASFV infection. To investigate how g5Rp affects host translation would be beneficial for the prevention and control of ASFV infection and transmission. In this study, firstly we purified the g5Rp protein and investigated its protease activity, and secondly we performed a label-free quantitative proteomic assay to study the dynamic changes in the proteome of porcine alveolar macrophages (3D/421) overexpressing g5Rp. Analyzing 122 differentially expressed host cell proteins, we focused on the majority of ribosome-related upregulated protein expression in the protein family (eIF) belonging to the eukaryotic translation starter factor, notably downregulation of EIF2S1 and EIF5A. 7 proteins that may interact with g5Rp were further identified with IP-MS, and EIF5A and g5Rp were identified through CO-IP and PLA assays. Protein crystallization and structural analysis revealed that g5Rp, a dimer protein with Nudix domain, promotes ASFV replication by modulating translation in host cells. The present findings provide new insights into the mechanism of g5Rp involvement in host cell translation and lay the foundation for the prevention and control of ASFV.

INSTRUMENT(S):

ORGANISM(S): Sus Scrofa Domesticus (domestic Pig)

SUBMITTER: chunmei xu

LAB HEAD: xiaomin Zhao

PROVIDER: PXD046133 | Pride | 2025-11-30

REPOSITORIES: Pride

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			Action	DRS
	ASFV-1.raw	Raw
	ASFV-2.raw	Raw
	ASFV-3.raw	Raw
	Flag-g5Rp-1.raw	Raw
	Flag-g5Rp-2.raw	Raw

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