MARCH8 promotes the proteasomal degradation of foot-and-mouth disease virus VP1, VP2, and VP3 to negatively regulate viral replication.

Mengge Yin, Xiangmin Li, Min Zhang, Qiongqiong Zhao, Haoyuan Wang, Huiyan Zhang, Zengjun Lu, Ping Qian

Abstract read

In one paragraph

Article in Veterinary research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact

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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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

Genome-wide CRISPR screen identifies RNF24 as a critical host factor for foot-and-mouth disease virus entry.Frontiers in cell and developmental biology · 2026
Article

4 · The record

Corrections and comments

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

8 authors.

Mengge YinNational Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan, 430070, Hubei, China.

Xiangmin LiNational Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan, 430070, Hubei, China.

Min ZhangNational Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan, 430070, Hubei, China.

Qiongqiong ZhaoNational Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan, 430070, Hubei, China.

Haoyuan WangNational Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan, 430070, Hubei, China.

Huiyan ZhangState Key Laboratory for Animal Disease Control and Prevention, National Foot-and-Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, Gansu, China.

Zengjun LuState Key Laboratory for Animal Disease Control and Prevention, National Foot-and-Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, Gansu, China. luzengjun@caas.cn.

Ping QianNational Key Laboratory of Agricultural Microbiology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan, 430070, Hubei, China. qianp@mail.hzau.edu.cn.ORCID http://orcid.org/0000-0002-4059-5358

Funding

National Key R&D Program of China 2021YFD1800300National Natural Science Foundation of China 32072841

6 · The paper itself

Abstract

The host cell membrane-associated RING-CH8 protein (MARCH8) functions as an antiviral host factor by targeting viral envelope glycoproteins. Foot-and-mouth disease virus (FMDV) is a non-enveloped, positive-sense, single-stranded RNA virus. The potential impact of MARCH8 on FMDV replication remains uncertain. Here, we found that the overexpression of MARCH8 significantly inhibited FMDV replication in a dose-dependent manner. Conversely, the knockdown of MARCH8 facilitated FMDV replication. Specifically, MARCH8 interacted with VP1, VP2, and VP3, mediating their degradation in a proteasome-dependent manner. MARCH8 catalyzed the K33-linked polyubiquitination of VP1, VP2, and VP3. Moreover, the Lys210 residue of VP1, the Lys63 residue of VP2, and the Lys118 residue of VP3 were identified as critical target sites for MARCH8-mediated degradation. Overall, we conclude that MARCH8 is an intrinsic antiviral factor against FMDV.

Indexed as

Capsid ProteinsFoot-and-Mouth Disease VirusProteasome Endopeptidase ComplexUbiquitin-Protein LigasesVirus ReplicationAnimalsFoot-and-Mouth DiseaseProteolysisCapsid ProteinsProteasome Endopeptidase ComplexUbiquitin-Protein LigasesVP1 protein, Foot-and-mouth disease virusVP2 protein, Foot-and-mouth disease virusVP3 protein, Foot-and-mouth disease virusfoot-and-mouth disease virusK33-linked polyubiquitinationMembrane-associated RING-CH8 proteinproteasomal degradationrestriction factor

Identifiers

PMID40307900

DOI10.1186/s13567-025-01521-z

PMCPMC12044826

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LicenceCC BY

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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.