Evidence map›Paper›PMID 34196914›Full record

ArticleVirologica Sinica2021

ANXA2 Facilitates Enterovirus 71 Infection by Interacting with 3D Polymerase and PI4KB to Assist the Assembly of Replication Organelles.

Qiuhan Zhang, Siliang Li, Ping Lei, Zixian Li, Feifei Chen, Qi Chen, Yulu Wang, Jiami Gong, Qi Tang, Xinjin Liu and 2 more

Open access · greenAbstract read
In one paragraph

Article in Virologica Sinica, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

16 citing papers in PubMed, 35 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

12 authors at 1 institution in 1 country.

Qiuhan Zhang *State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Siliang Li *State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Ping LeiState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Zixian LiState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Feifei ChenState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Qi ChenState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Yulu WangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Jiami GongState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Qi TangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Xinjin LiuState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Ke LanState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China. klan@whu.edu.cn.ORCID http://orcid.org/0000-0002-0384-8598
Shuwen WuState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China. shuwenwu@whu.edu.cn.ORCID http://orcid.org/0000-0002-8112-3429
Wuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Similar to that of other enteroviruses, the replication of enterovirus 71 (EV71) occurs on rearranged membranous structures called replication organelles (ROs). Phosphatidylinositol 4-kinase III (PI4KB), which is required by enteroviruses for RO formation, yields phosphatidylinositol-4-phosphate (PI4P) on ROs. PI4P then binds and induces conformational changes in the RNA-dependent RNA polymerase (RdRp) to modulate RdRp activity. Here, we targeted 3D polymerase, the core enzyme of EV71 ROs, and found that the host factor Annexin A2 (ANXA2) can interact with 3D polymerase and promote the replication of EV71. Then, an experiment showed that the annexin domain of ANXA2, which possesses membrane-binding capacity, mediates the interaction of ANXA2 with EV71 3D polymerase. Further research showed that ANXA2 is localized on ROs and interacts with PI4KB. Overexpression of ANXA2 stimulated the formation of PI4P, and the level of PI4P was decreased in ANXA2-knockout cells. Furthermore, ANXA2, PI4KB, and 3D were shown to be localized to the viral RNA replication site, where they form a higher-order protein complex, and the presence of ANXA2 promoted the PI4KB-3D interaction. Altogether, our data provide new insight into the role of ANXA2 in facilitating formation of the EV71 RNA replication complex.

Indexed as

Annexin A2Enterovirus A, Human1-Phosphatidylinositol 4-KinaseOrganellesVirus Replication1-Phosphatidylinositol 4-KinaseAnnexin A23D polymeraseAnnexin A2 (ANXA2)Enterovirus 71 (EV71)Phosphatidylinositol 4-kinase III (PI4KB)

Identifiers

PMID34196914
PMCPMC8692544
OpenAlexW3175745846

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.