Evidence map›Paper›PMID 30852271›Full record

ArticleVirology2019

N-Linked glycosylation of the membrane protein ectodomain regulates infectious bronchitis virus-induced ER stress response, apoptosis and pathogenesis.

Jia Qi Liang, Shouguo Fang, Quan Yuan, Mei Huang, Rui Ai Chen, To Sing Fung, Ding Xiang Liu

Abstract read
In one paragraph

Article in Virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Perturbation of the host cell CaCell death & disease · 2023
    Article
  5. Review
  6. Article
  7. Role forScience advances · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Characterization of the SARS-CoV-2 E Protein: Sequence, Structure, Viroporin, and Inhibitors.Protein science : a publication of the Protein Society · 2021
    Review
  14. Animal Coronaviruses Induced Apoptosis.Life (Basel, Switzerland) · 2021
    Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. 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

7 authors at 3 institutions in 1 country.

Jia Qi LiangSouth China Agricultural University, Guangdong Province Key Laboratory Microbial Signals & Disease Co, and Integrative Microbiology Research Centre, Guangzhou 510642, Guangdong, People's Republic of China.
Shouguo FangAgricultural School, Yangtze University, 266 Jingmilu, Jingzhou City, Hubei Province 434025, People's Republic of China.
Quan YuanSouth China Agricultural University, Guangdong Province Key Laboratory Microbial Signals & Disease Co, and Integrative Microbiology Research Centre, Guangzhou 510642, Guangdong, People's Republic of China.
Mei HuangZhaoqing Institute of Biotechnology Co., Ltd., Zhaoqing 526238, Guangdong, People's Republic of China.
Rui Ai ChenCollege of Veterinary Medicine, South China Agricultural University, Guangzhou 510642, People's Republic of China; Zhaoqing DaHuaNong Biology Medicine Co., Ltd., Zhaoqing 526238, Guangdong, People's Republic of China.
To Sing FungSouth China Agricultural University, Guangdong Province Key Laboratory Microbial Signals & Disease Co, and Integrative Microbiology Research Centre, Guangzhou 510642, Guangdong, People's Republic of China. Electronic address: tosingfung@qq.com.
Ding Xiang LiuSouth China Agricultural University, Guangdong Province Key Laboratory Microbial Signals & Disease Co, and Integrative Microbiology Research Centre, Guangzhou 510642, Guangdong, People's Republic of China. Electronic address: dxliu0001@163.com.
South China Agricultural University · CNYangtze University · CNZhaoqing University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coronavirus membrane (M) protein is the most abundant structural protein playing a critical role in virion assembly. Previous studies show that the N-terminal ectodomain of M protein is modified by glycosylation, but its precise functions are yet to be thoroughly investigated. In this study, we confirm that N-linked glycosylation occurs at two predicted sites in the M protein ectodomain of infectious bronchitis coronavirus (IBV). Dual mutations at the two sites (N3D/N6D) did not affect particle assembly, virus-like particle formation and viral replication in culture cells. However, activation of the ER stress response was significantly reduced in cells infected with rN3D/N6D, correlated with a lower level of apoptosis and reduced production of pro-inflammatory cytokines. Taken together, this study demonstrates that although not essential for replication, glycosylation in the IBV M protein ectodomain plays important roles in activating ER stress, apoptosis and proinflammatory response, and may contribute to the pathogenesis of IBV.

Indexed as

ApoptosisEndoplasmic Reticulum StressCoronavirus InfectionsCoronavirus M ProteinsCytokinesGlycosylationHumansInfectious bronchitis virusProtein DomainsViral Matrix ProteinsCoronavirus M ProteinsCytokinesM protein, Avian infectious bronchitis virusViral Matrix ProteinsApoptosisCoronavirusER stressGlycosylationParticle assemblyPro-inflammatory responseViral pathogenesis

Identifiers

PMID30852271
PMCPMC7112112
OpenAlexW2915449685

What OpenQuestion holds

Textmetadata
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.