Evidence map›Paper›PMID 40259479›Full record

ArticleAutophagy2025

ATG9 inhibits

Chen Chen, Guoxu Liu, Kehan Xu, Aibao Chen, Ziyang Cheng, Xueping Yan, Ting Zhang, Yan Sun, Tian Yu, Jiayao Wang and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Autophagy, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

15 authors.

Chen ChenResearch Center for Immunological Diseases, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Guoxu LiuDepartment of Immunology, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Kehan XuDepartment of Microbiology, Anhui Province Key Laboratory of Zoonoses, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Aibao ChenDepartment of Cell Biology, School of Life Sciences, Anhui Medical University, Hefei, China.
Ziyang ChengDepartment of Immunology, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Xueping YanDepartment of Immunology, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Ting ZhangDivision of Pulmonary and Critical Care Medicine, Mayo Clinic, Rochester, USA.
Yan SunDepartment of Immunology, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Tian YuDepartment of Immunology, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Jiayao WangDepartment of Immunology, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Shuangshuang LuoDepartment of Microbiology, Anhui Province Key Laboratory of Zoonoses, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Weiting ZhouDepartment of Microbiology, Anhui Province Key Laboratory of Zoonoses, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Shengqun DengDepartment of Pathogen Biology, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Yan LiuDepartment of Microbiology, Anhui Province Key Laboratory of Zoonoses, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.
Yanan YangResearch Center for Immunological Diseases, School of Basic Medical Sciences, Anhui Medical University, Hefei, China.ORCID 0009-0000-2717-7453

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ickettsiae are tick-borne pathogens that infect human hosts through poorly characterized mechanisms. Herein, we report that ATG9 (autophagy related 9) plays a previously unrecognized role in inhibiting Rickettsia binding to the host cell surface. Unexpectedly, this new function of ATG9 is likely independent of macroautophagy/autophagy. Instead, ATG9 acts as a host defending factor by binding to XRCC6/KU70, a receptor of the Rickettsia outer-membrane protein rOmpB. Both ATG9 and rOmpB bind to the DNA-binding domain of XRCC6, suggesting a competitive role for ATG9 occupying the binding site of rOmpB to abrogate Rickettsia binding. Furthermore, we show that rapamycin transcriptionally activates ATG9 and inhibits rOmpB-mediated infection in a mouse model. Collectively, our study reveals a novel innate mechanism regulating Rickettsia infection and suggests that agonists of ATG9 May be useful for developing therapeutic strategies for the intervention of rickettsial diseases.

Indexed as

Autophagy-Related ProteinsBacterial Outer Membrane ProteinsCell MembraneKu AutoantigenMembrane ProteinsRickettsiaAnimalsAutophagyHumansMiceProtein BindingRickettsia InfectionsSirolimusVesicular Transport ProteinsAtg9A protein, mouseAutophagy-Related ProteinsBacterial Outer Membrane ProteinsKu AutoantigenMembrane ProteinsSirolimusVesicular Transport ProteinsXrcc6 protein, humanAutophagy-related genehost defenseinfectious diseaserickettsiarOmpBtick-borne pathogen

Identifiers

PMID40259479
PMCPMC12459360

What Socratic 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 Socratic graph.