Proteomics

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Peste des petits ruminants virus nucleocapsid protein interacts with PACT and induces stress granule to promote viral replication

ABSTRACT: Stress granules (SGs) formation is a conserved cellular strategy to reduce stress-related damage regulating cell survival. A Mass spectrometry-based profiling of the interactome of PPRV N protein revealed that PPRV N interacted with PACT to regulate the assembly of SGs. N protein inhibited the interaction between PACT and a PKR inhibitor TRBP through binding to the M1 domain of PACT, which enhanced the interaction between PACT and PKR and thus promoted PKR activation and subsequent eIF2α phosphorylation as well as SGs formation. The regulatory function of N protein was strikingly abrogated in PACT-/- cells. PPRV infection-induced SGs through the PKR/eIF2α pathway are PACT-dependent. The loss of function assay indicated that PPRV-induced SGs were critical for PPRV replication. We concluded that the PPRV N protein manipulates the host PKR/eIF2α/SGs axis to favor virus replication.

ORGANISM(S): Homo Sapiens

SUBMITTER: Zixiang Zhu  

PROVIDER: PXD039104 | iProX | Tue Dec 27 00:00:00 GMT 2022

REPOSITORIES: iProX

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Peste Des Petits Ruminants Virus Nucleocapsid Protein Interacts with Protein Kinase R-Activating Protein and Induces Stress Granules To Promote Viral Replication.

Chen Shuying S   Yang Fan F   Cao Weijun W   Zhang Xiangle X   Liu Huisheng H   Zhang Keshan K   Liu Xiangtao X   Wang Jingyu J   Zheng Haixue H   Zhu Zixiang Z  

Journal of virology 20230118 2

The pathogenic mechanisms of peste des petits ruminants virus (PPRV) infection remain poorly understood, leaving peste des petits ruminants (PPR) control and eradication especially difficult. Here, we determined that PPRV nucleocapsid (N) protein triggers formation of stress granules (SGs) to benefit viral replication. A mass spectrometry-based profiling of the interactome of PPRV N protein revealed that PPRV N protein interacted with protein kinase R (PKR)-activating protein (PACT), and this in  ...[more]

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