Evidence map›Paper›PMID 34504014›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Structural changes in bacteriophage T7 upon receptor-induced genome ejection.

Wenyuan Chen, Hao Xiao, Li Wang, Xurong Wang, Zhixue Tan, Zhen Han, Xiaowu Li, Fan Yang, Zhonghua Liu, Jingdong Song and 2 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
6.9field-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

40 citing papers in PubMed, 66 citations in OpenAlex.

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  15. Cryo-EM structure of cyanopodophage A4 reveals a pentameric pre-ejectosome in the double-stabilized capsid.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  16. Journal of virology · 2025
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  20. Moo19 and B2: Structures ofScience advances · 2024
    Article
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 4 institutions in 1 country.

Wenyuan ChenKey Laboratory for Matter Microstructure and Function of Hunan Province, Key Laboratory of Low-dimensional Quantum Structures and Quantum Control, School of Physics and Electronics, Hunan Normal University, Changsha 410082, China.ORCID 0000-0002-9449-8596
Hao XiaoKey Laboratory for Matter Microstructure and Function of Hunan Province, Key Laboratory of Low-dimensional Quantum Structures and Quantum Control, School of Physics and Electronics, Hunan Normal University, Changsha 410082, China.ORCID 0000-0003-2461-494X
Li WangState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Xurong WangKey Laboratory for Matter Microstructure and Function of Hunan Province, Key Laboratory of Low-dimensional Quantum Structures and Quantum Control, School of Physics and Electronics, Hunan Normal University, Changsha 410082, China.
Zhixue TanKey Laboratory for Matter Microstructure and Function of Hunan Province, Key Laboratory of Low-dimensional Quantum Structures and Quantum Control, School of Physics and Electronics, Hunan Normal University, Changsha 410082, China.ORCID 0000-0002-7793-6494
Zhen HanKey Laboratory for Matter Microstructure and Function of Hunan Province, Key Laboratory of Low-dimensional Quantum Structures and Quantum Control, School of Physics and Electronics, Hunan Normal University, Changsha 410082, China.ORCID 0000-0003-0082-5291
Xiaowu LiSchool of Electronics and Information Engineering, Hunan University of Science and Engineering, Yongzhou 425199, China.
Fan YangKey Laboratory for Matter Microstructure and Function of Hunan Province, Key Laboratory of Low-dimensional Quantum Structures and Quantum Control, School of Physics and Electronics, Hunan Normal University, Changsha 410082, China.
Zhonghua LiuThe National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha 410082, China.ORCID 0000-0001-8497-6702
Jingdong SongState Key Laboratory of Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China; lingpengcheng@mail.tsinghua.edu.cn hrliu@hunnu.edu.cn songjd@ivdc.chinacdc.cn.ORCID 0000-0001-8808-1981
Hongrong LiuKey Laboratory for Matter Microstructure and Function of Hunan Province, Key Laboratory of Low-dimensional Quantum Structures and Quantum Control, School of Physics and Electronics, Hunan Normal University, Changsha 410082, China; lingpengcheng@mail.tsinghua.edu.cn hrliu@hunnu.edu.cn songjd@ivdc.chinacdc.cn.ORCID 0000-0001-6247-5464
Lingpeng ChengKey Laboratory for Matter Microstructure and Function of Hunan Province, Key Laboratory of Low-dimensional Quantum Structures and Quantum Control, School of Physics and Electronics, Hunan Normal University, Changsha 410082, China; lingpengcheng@mail.tsinghua.edu.cn hrliu@hunnu.edu.cn songjd@ivdc.chinacdc.cn.ORCID 0000-0002-9148-0550
Hunan Normal University · CNChinese Academy of Sciences · CNHunan University of Science and Engineering · CNNational Institute for Viral Disease Control and Prevention · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many tailed bacteriophages assemble ejection proteins and a portal-tail complex at a unique vertex of the capsid. The ejection proteins form a transenvelope channel extending the portal-tail channel for the delivery of genomic DNA in cell infection. Here, we report the structure of the mature bacteriophage T7, including the ejection proteins, as well as the structures of the full and empty T7 particles in complex with their cell receptor lipopolysaccharide. Our near-atomic-resolution reconstruction shows that the ejection proteins in the mature T7 assemble into a core, which comprises a fourfold gene product 16 (gp16) ring, an eightfold gp15 ring, and a putative eightfold gp14 ring. The gp15 and gp16 are mainly composed of helix bundles, and gp16 harbors a lytic transglycosylase domain for degrading the bacterial peptidoglycan layer. When interacting with the lipopolysaccharide, the T7 tail nozzle opens. Six copies of gp14 anchor to the tail nozzle, extending the nozzle across the lipopolysaccharide lipid bilayer. The structures of gp15 and gp16 in the mature T7 suggest that they should undergo remarkable conformational changes to form the transenvelope channel. Hydrophobic α-helices were observed in gp16 but not in gp15, suggesting that gp15 forms the channel in the hydrophilic periplasm and gp16 forms the channel in the cytoplasmic membrane.

Indexed as

Bacteriophage T7CapsidCapsid ProteinsCell MembraneCryoelectron MicroscopyDNA, ViralLipid BilayersModels, MolecularPeriplasmStructure-Activity RelationshipTransduction, GeneticViral ProteinsCapsid ProteinsDNA, ViralLipid BilayersViral Proteinsbacteriophagesejection proteinsgenome deliverylipopolysaccharide

Identifiers

PMID34504014
PMCPMC8449382
OpenAlexW3205562355

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.