Evidence map›Paper›PMID 40434106›Full record

ArticleJournal of virology2025

Autographa californica multiple nucleopolyhedrovirus Ac51 interacts with Ac66 and facilitates its nuclear localization to promote the nuclear egress of nucleocapsids.

Jianxiang Qiu, Guo-Sheng Zhu, Jiaxin Liu, Longkuan Feng, Zefen Pang, Dandong Zhu, Kanghong Chen, Xiukui Yan, Ao Li, Chuming You and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of virology, 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

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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

11 authors.

Jianxiang Qiu *Biosafety Laboratory, The Affiliated Guangdong Second Provincial General Hospital of Jinan University, Guangzhou, Guangdong, China.ORCID 0000-0003-3426-5050
Guo-Sheng Zhu *Biosafety Laboratory, The Affiliated Guangdong Second Provincial General Hospital of Jinan University, Guangzhou, Guangdong, China.
Jiaxin LiuBiosafety Laboratory, The Affiliated Guangdong Second Provincial General Hospital of Jinan University, Guangzhou, Guangdong, China.
Longkuan FengBiosafety Laboratory, The Affiliated Guangdong Second Provincial General Hospital of Jinan University, Guangzhou, Guangdong, China.
Zefen PangBiosafety Laboratory, The Affiliated Guangdong Second Provincial General Hospital of Jinan University, Guangzhou, Guangdong, China.
Dandong ZhuBiosafety Laboratory, The Affiliated Guangdong Second Provincial General Hospital of Jinan University, Guangzhou, Guangdong, China.
Kanghong ChenBiosafety Laboratory, The Affiliated Guangdong Second Provincial General Hospital of Jinan University, Guangzhou, Guangdong, China.
Xiukui YanBiosafety Laboratory, The Affiliated Guangdong Second Provincial General Hospital of Jinan University, Guangzhou, Guangdong, China.
Ao LiSchool of Life Sciences and Medicine, Shandong University of Technology, Zibo, Shandong, China.
Chuming YouBiosafety Laboratory, The Affiliated Guangdong Second Provincial General Hospital of Jinan University, Guangzhou, Guangdong, China.ORCID 0000-0001-9348-2149
Zhixin FangBiosafety Laboratory, The Affiliated Guangdong Second Provincial General Hospital of Jinan University, Guangzhou, Guangdong, China.ORCID 0000-0003-2105-5599

Funding

National Natural Science Foundation of China 32000110,31701845Science and Technology Planning Project of Guangzhou 202201011464,2024A03J0923,202102020745,202201020482Talent Project of Guangdong Second Provincial General Hospital 2024F001
6 · The paper itself

Abstract

Autographa californica multiple nucleopolyhedrovirus is a large DNA virus that replicates within host nuclei. The mechanism underlying the nuclear egress of viral nucleocapsids is not fully understood. We previously identified Ac51 as a key player in facilitating efficient nuclear egress of nucleocapsids for the release of budded viruses (BVs). This protein joins Ac66 and EXON0 as the third identified protein with a similar function. In this study, we evaluated the functional importance of conserved domains of Ac51 during virus replication and found that the coiled-coil (CC) motif of Ac51 was crucial for the protein's accumulation and BV production. Our study further revealed a strong interaction and colocalization between Ac51 and Ac66. Deletion of

Indexed as

Cell NucleusNucleocapsidNucleocapsid ProteinsNucleopolyhedrovirusesViral ProteinsActive Transport, Cell NucleusAnimalsProtein BindingSf9 CellsSpodopteraVirus ReleaseVirus ReplicationNucleocapsid ProteinsViral ProteinsAc51Ac66AcMNPVnucleocapsid egress

Identifiers

PMID40434106
PMCPMC12172431

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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.