Evidence map›Paper›PMID 36591809›Full record

ReviewEmerging microbes & infections2023

Host antiviral factors hijack furin to block SARS-CoV-2, ebola virus, and HIV-1 glycoproteins cleavage.

Changqing Yu, Guosheng Wang, Qiang Liu, Jingbo Zhai, Mengzhou Xue, Qiang Li, Yuanhua Xian, Chunfu Zheng

Open access · goldAbstract readReview
In one paragraph

Review in Emerging microbes & infections, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

11 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 8 institutions in 3 countries.

Changqing YuSchool of Advanced Agricultural Sciences, Yibin Vocational and Technical College, Yibin, People's Republic of China.
Guosheng WangDepartment of Pulmonary and Critical Care Medicine, Shanghai East Hospital, Tongji University School of Medicine, Shanghai, People's Republic of China.
Qiang LiuNanchong Key Laboratory of Disease Prevention, Control and Detection in Livestock and Poultry, Nanchong Vocational and Technical College, Nanchong, People's Republic of China.
Jingbo ZhaiKey Laboratory of Zoonose Prevention and Control at Universities of Inner Mongolia Autonomous Region, Medical College, Inner Mongolia Minzu University, Tongliao, People's Republic of China.
Mengzhou XueDepartment of Cerebrovascular Diseases, The Second Affiliated Hospital of Zhengzhou University, Zhengzhou, People's Republic of China.
Qiang LiDepartment of Pulmonary and Critical Care Medicine, Shanghai East Hospital, Tongji University School of Medicine, Shanghai, People's Republic of China.
Yuanhua XianSchool of Advanced Agricultural Sciences, Yibin Vocational and Technical College, Yibin, People's Republic of China.
Chunfu ZhengInstitute of Animal Health, Guangdong Academy of Agricultural Sciences, Key Laboratory of Livestock Disease Prevention of Guangdong Province, Scientific Observation and Experiment Station of Veterinary Drugs and Diagnostic Techniques of Guangdong Province, Ministry of Agriculture and Rural Affairs, Guangzhou, People's Republic of China.
Ministry of Agriculture and Rural Affairs · CNMongolian National University · MNNanchong Central Hospital · CNSecond Affiliated Hospital of Zhengzhou University · CNShanghai East Hospital · CNTongji University · CNYibin University · CNYibin Vocational and Technical College

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Viral envelope glycoproteins are crucial for viral infections. In the process of enveloped viruses budding and release from the producer cells, viral envelope glycoproteins are presented on the viral membrane surface as spikes, promoting the virus's next-round infection of target cells. However, the host cells evolve counteracting mechanisms in the long-term virus-host co-evolutionary processes. For instance, the host cell antiviral factors could potently suppress viral replication by targeting their envelope glycoproteins through multiple channels, including their intracellular synthesis, glycosylation modification, assembly into virions, and binding to target cell receptors. Recently, a group of studies discovered that some host antiviral proteins specifically recognized host proprotein convertase (PC) furin and blocked its cleavage of viral envelope glycoproteins, thus impairing viral infectivity. Here, in this review, we briefly summarize several such host antiviral factors and analyze their roles in reducing furin cleavage of viral envelope glycoproteins, aiming at providing insights for future antiviral studies.

Indexed as

COVID-19EbolavirusHemorrhagic Fever, EbolaHIV-1Virus DiseasesAntiviral AgentsFurinGlycoproteinsHumansSARS-CoV-2Viral Envelope ProteinsAntiviral AgentsFurinGlycoproteinsViral Envelope ProteinsAntiviral factorscleavagefurinSARS-CoV-2viral glycoprotein

Identifiers

PMID36591809
PMCPMC9897805
OpenAlexW4313398575

What Socratic 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 Socratic graph.