Evidence map›Paper›PMID 39128851›Full record

ArticleAutophagy2024

AP3B1 facilitates PDIA3/ERP57 function to regulate rabies virus glycoprotein selective degradation and viral entry.

Yuelan Zhang, Xinyi Zhang, Xue Yang, Linyue Lv, Qinyang Wang, Shaowei Zeng, Zhuyou Zhang, Martin Dorf, Shitao Li, Ling Zhao and 1 more

Abstract read
In one paragraph

Article in Autophagy, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
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

11 authors.

Yuelan ZhangDepartment of Rheumatology and Immunology, State Key Laboratory of Virology, Zhongnan Hospital, Wuhan University, Wuhan, China.
Xinyi ZhangDepartment of Rheumatology and Immunology, State Key Laboratory of Virology, Zhongnan Hospital, Wuhan University, Wuhan, China.
Xue YangDepartment of Rheumatology and Immunology, State Key Laboratory of Virology, Zhongnan Hospital, Wuhan University, Wuhan, China.
Linyue LvDepartment of Rheumatology and Immunology, State Key Laboratory of Virology, Zhongnan Hospital, Wuhan University, Wuhan, China.
Qinyang WangDepartment of Rheumatology and Immunology, State Key Laboratory of Virology, Zhongnan Hospital, Wuhan University, Wuhan, China.
Shaowei ZengDepartment of Rheumatology and Immunology, State Key Laboratory of Virology, Zhongnan Hospital, Wuhan University, Wuhan, China.
Zhuyou ZhangDepartment of Rheumatology and Immunology, State Key Laboratory of Virology, Zhongnan Hospital, Wuhan University, Wuhan, China.
Martin DorfDepartment of Microbiology & Immunobiology, Harvard Medical School, Boston, MA, USA.
Shitao LiDepartment of Microbiology and Immunology, Tulane University, New Orleans, LA, USA.
Ling ZhaoState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, China.
Bishi FuDepartment of Rheumatology and Immunology, State Key Laboratory of Virology, Zhongnan Hospital, Wuhan University, Wuhan, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rabies virus causes an estimated 59,000 annual fatalities worldwide and promising therapeutic treatments are necessary to develop. In this study, affinity tag-purification mass spectrometry was employed to delineate RABV glycoprotein and host protein interactions, and PDIA3/ERP57 was identified as a potential inhibitor of RABV infection. PDIA3 restricted RABV infection with follow mechanisms: PDIA3 mediated the degradation of RABV G protein by targeting lysine 332 via the selective macroautophagy/autophagy pathway; The PDIA3 interactor, AP3B1 (adaptor related protein complex 3 subunit beta 1) was indispensable in PDIA3-triggered selective degradation of the G protein; Furthermore, PDIA3 competitively bound with NCAM1/NCAM (neural cell adhesion molecule 1) to block RABV G, hindering viral entry into host cells. PDIA3 190-199 aa residues bound to the RABV G protein were necessary and sufficient to defend against RABV. These results demonstrated the therapeutic potential of biologics that target PDIA3 or utilize PDIA3 190-199 aa peptide to treat clinical rabies.

Indexed as

GlycoproteinsProtein Disulfide-IsomerasesRabies virusVirus InternalizationAnimalsAutophagyHEK293 CellsHumansMiceProteolysisRabiesGlycoproteinsPDIA3 protein, humanPdia3 protein, mouseProtein Disulfide-IsomerasesAP3B1PDIA3rabies virusselective autophagytherapeutic peptideviral entry

Identifiers

PMID39128851
PMCPMC11587837

What OpenQuestion holds

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Registered trials

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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.