Evidence map›Paper›PMID 37833330›Full record

ArticleNature communications2023

Cryo-EM structure of cyanophage P-SCSP1u offers insights into DNA gating and evolution of T7-like viruses.

Lanlan Cai, Hang Liu, Wen Zhang, Shiwei Xiao, Qinglu Zeng, Shangyu Dang

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. 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
    Article
  8. Article
  9. Ejectosome ofPNAS nexus · 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

6 authors.

Lanlan Cai *Department of Ocean Science, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.ORCID http://orcid.org/0000-0002-1084-2848
Hang Liu *Division of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.ORCID http://orcid.org/0000-0002-6176-3963
Wen ZhangDivision of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.
Shiwei XiaoDepartment of Ocean Science, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.
Qinglu ZengDepartment of Ocean Science, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China. zeng@ust.hk.ORCID http://orcid.org/0000-0002-5616-7155
Shangyu DangDivision of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China. sdang@ust.hk.ORCID http://orcid.org/0000-0001-9141-1865

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyanophages, together with their host cyanobacteria, play important roles in marine biogeochemical cycles and control of marine food webs. The recently identified MPP-C (Marine Picocyanobacteria Podovirus clade C) cyanophages, belonging to the T7-like podoviruses, contain the smallest genomes among cyanopodoviruses and exhibit distinct infection kinetics. However, understanding of the MPP-C cyanophage infection process is hindered by the lack of high-resolution structural information. Here, we report the cryo-EM structure of the cyanophage P-SCSP1u, a representative member of the MPP-C phages, in its native form at near-atomic resolution, which reveals the assembly mechanism of the capsid and molecular interaction of the portal-tail complex. Structural comparison of the capsid proteins of P-SCSP1u and other podoviruses with known structures provides insights into the evolution of T7-like viruses. Furthermore, our study provides the near-atomic resolution structure of portal-tail complex for T7-like viruses. On the basis of previously reported structures of phage T7, we identify an additional valve and gate to explain the DNA gating mechanism for the T7-like viruses.

Indexed as

BacteriophagesPodoviridaeCryoelectron MicroscopyDNAGenome, ViralPhylogenyDNA

Identifiers

PMID37833330
PMCPMC10575957

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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.