Evidence map›Paper›PMID 32967959›Full record

ArticleJournal of virology2020

Cytoplasmic Cargo Receptor p62 Inhibits Avibirnavirus Replication by Mediating Autophagic Degradation of Viral Protein VP2.

Yahui Li, Boli Hu, Gang Ji, Yina Zhang, Chenyang Xu, Jing Lei, Chan Ding, Jiyong Zhou

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.8field-weighted citation impact, top 10% of its field
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

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

18 citing papers in PubMed, 24 citations in OpenAlex.

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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 at 3 institutions in 1 country.

Yahui LiInstitute of Immunology and College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, China.
Boli HuInstitute of Immunology and College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, China bolihu@njau.edu.cn jyzhou@zju.edu.cn.
Gang JiInstitute of Immunology and College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, China.
Yina ZhangMOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University, Hangzhou, China.
Chenyang XuInstitute of Immunology and College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, China.
Jing LeiInstitute of Immunology and College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, China.
Chan DingShanghai Veterinary Research Institute, CAAS, Shanghai, China.
Jiyong ZhouMOA Key Laboratory of Animal Virology, Center for Veterinary Sciences, Zhejiang University, Hangzhou, China bolihu@njau.edu.cn jyzhou@zju.edu.cn.ORCID 0000-0002-8852-1227
Nanjing Agricultural University · CNZhejiang University · CNShanghai Veterinary Research Institute · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Selective autophagy regulates the degradation of cytoplasmic cargos, such as damaged organelles, invading pathogens, and aggregated proteins. Furthermore, autophagy is capable of degrading avibirnavirus, but the mechanism responsible for this process is unclear. Here, we show that autophagy cargo receptor p62 regulates the degradation of the avibirnavirus capsid protein VP2. Binding of p62 to VP2 enhances autophagic induction and promotes autophagic degradation of viral protein VP2. Further study showed that the interaction of p62 with viral protein VP2 is dependent on ubiquitination at the K411 site of VP2 and the ubiquitin-associated domain of p62. Mutation analysis showed that the K411R mutation of viral protein VP2 prohibits its p62-mediated degradation. Consistent with this finding, p62 lacking the ubiquitin-associated domain or the LC3-interacting region no longer promoted the degradation of VP2. Virus production revealed that the knockout of p62 but not the overexpression of p62 promotes the replication of avibirnavirus. Collectively, our findings suggest that p62 mediates selective autophagic degradation of avibirnavirus protein VP2 in a ubiquitin-dependent manner and is an inhibitor of avibirnavirus replication.

Indexed as

AnimalsAutophagyAvibirnavirusBirnaviridae InfectionsCapsid ProteinsChickensCytosolGene Knockout TechniquesHEK293 CellsHumansRNA-Binding ProteinsUbiquitinViral ProteinsVirus ReplicationCapsid ProteinsP62 protein, humanRNA-Binding ProteinsUbiquitinViral Proteinsautophagyavibirnaviruscargo receptorp62VP2

Identifiers

PMID32967959
PMCPMC7925189
OpenAlexW3089039440

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.