Evidence map›Paper›PMID 41742195›Full record

ArticleVeterinary research2026

The CP312R protein of African swine fever virus inhibits host protein translation via the BiP/PERK/eIF2α pathway.

Jingwen Dai, Pingping Zhou, Yanjin Wang, Haojie Ren, Kehui Zhang, Meilin Li, Hailiang Ge, Hongwei Cao, Jiaqi Li, Hao Deng and 4 more

Abstract read
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In one paragraph

Article in Veterinary research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors.

Jingwen Dai *State Key Laboratory of Animal Disease Control and Prevention, National High-Containment Facilities for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, 678 Haping Road, Harbin, 150069, Heilongjiang, China.
Pingping Zhou *Harbin Medical University, Harbin, 150081, China.
Yanjin Wang *State Key Laboratory of Animal Disease Control and Prevention, National High-Containment Facilities for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, 678 Haping Road, Harbin, 150069, Heilongjiang, China.
Haojie RenInternational Joint Research Centre of National Animal Immunology, College of Veterinary Medicine, Henan Agricultural University, Zhengzhou, 450046, China.
Kehui ZhangState Key Laboratory of Animal Disease Control and Prevention, National High-Containment Facilities for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, 678 Haping Road, Harbin, 150069, Heilongjiang, China.
Meilin LiState Key Laboratory of Animal Disease Control and Prevention, National High-Containment Facilities for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, 678 Haping Road, Harbin, 150069, Heilongjiang, China.
Hailiang GeState Key Laboratory of Animal Disease Control and Prevention, National High-Containment Facilities for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, 678 Haping Road, Harbin, 150069, Heilongjiang, China.
Hongwei CaoState Key Laboratory of Animal Disease Control and Prevention, National High-Containment Facilities for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, 678 Haping Road, Harbin, 150069, Heilongjiang, China.
Jiaqi LiState Key Laboratory of Animal Disease Control and Prevention, National High-Containment Facilities for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, 678 Haping Road, Harbin, 150069, Heilongjiang, China.
Hao DengState Key Laboratory of Animal Disease Control and Prevention, National High-Containment Facilities for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, 678 Haping Road, Harbin, 150069, Heilongjiang, China.
Wen-Rui HeInternational Joint Research Centre of National Animal Immunology, College of Veterinary Medicine, Henan Agricultural University, Zhengzhou, 450046, China.
Lian-Feng LiState Key Laboratory of Animal Disease Control and Prevention, National High-Containment Facilities for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, 678 Haping Road, Harbin, 150069, Heilongjiang, China. lilianfeng@caas.cn.
Su LiState Key Laboratory of Animal Disease Control and Prevention, National High-Containment Facilities for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, 678 Haping Road, Harbin, 150069, Heilongjiang, China. lisu@caas.cn.
Hua-Ji QiuState Key Laboratory of Animal Disease Control and Prevention, National High-Containment Facilities for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, 678 Haping Road, Harbin, 150069, Heilongjiang, China. qiuhuaji@caas.cn.

Funding

Heilongjiang Provincial Natural Science Foundation of China TD2023C007National Key Research and Development Program of China 2021YFD1800104National Natural Science Foundation of China 32372983National Natural Science Foundation of China 32473002
6 · The paper itself

Abstract

African swine fever is a highly contagious, febrile, hemorrhagic, and often fatal disease of domestic pigs and wild boar, caused by African swine fever virus (ASFV). ASFV has evolved multiple strategies to suppress host antiviral responses, including the regulation of host translation shutoff for immune evasion. However, the intricate mechanisms of translation shutoff regulated by viral proteins remain largely unexplored. A previous study has shown that pCP312R-a structural protein of ASFV with 312 amino acids (aa)-inhibits host protein translation by binding to the ribosomal protein S27A (RPS27A). Here, we demonstrated that the RNA polymerase-like domain (aa 59-163) of pCP312R was essential for inhibiting protein synthesis. However, the RNA polymerase-like domain of pCP312R did not interact with RPS27A, implying the existence of a novel inhibitory mechanism. In this study, we showed that pCP312R specifically inhibited cellular protein synthesis at the stage of translation. Notably, overexpression of pCP312R reduced the expression of heavy-chain-binding protein (BiP). Furthermore, pCP312R induced the protein translation shutoff by promoting the phosphorylation of PKR-like endoplasmic reticulum kinase (PERK) and eukaryotic initiation factor 2α (eIF2α). Taken together, our study reveals that ASFV pCP312R inhibits cellular protein synthesis via the BiP/PERK/eIF2α pathway.

Indexed as

African Swine FeverAfrican Swine Fever VirusProtein BiosynthesisViral ProteinsAnimalseIF-2 KinaseEukaryotic Initiation Factor-2Integrated Stress ResponseSignal TransductionSwineeIF-2 KinaseEukaryotic Initiation Factor-2Viral ProteinsAfrican swine fever virusCP312R proteineukaryotic initiation factor 2αheavy-chain-binding proteinPKR-like endoplasmic reticulum kinaseshutoff

Identifiers

PMID41742195
PMCPMC13040927

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.