ArticleNature communications2026
Cryo-EM structures of bacteriophage T4 portal-neck assembly intermediates reveal a viral genome retention mechanism.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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.
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.
Who cites it
2 citing papers in PubMed.
- Something old, something new? Herpesvirus genome packaging examined in light of lessons from the tailed bacteriophages.Journal of virology · 2026Review
- In situ structures of the portal-neck-tail complex of bacteriophage T4 inform a viral genome positioning mechanism.Nature communications · 2026Article
Corrections and comments
- Update of
Authors and funding
13 authors.
Funding
Abstract
Bacteriophage T4 has long served as an extraordinary model for tailed phages. During virion assembly, the viral DNA genome is tightly packed into the head, to which tail attaches via a portal-neck connector. Keeping this highly pressurized head leak-proof during these transactions is a challenge, yet the mechanisms remain poorly understood. Here we show that T4 seals its DNA-filled capsid using a double "genome-gate" mechanism. By reconstituting portal (gp20)-neck (gp13/gp14) assembly intermediates in vitro and determining their structures, we find that the gp14 hexamer forms a primary gate that closes the portal-neck opening. This gate is reinforced by a second gate formed by the host protein Hfq, which is hijacked by the virus as an accessory structural component. Hfq also stabilizes neck assembly and prevents its mis-assembly with portal. These studies define a viral genome retention mechanism in which a pre-assembled gp13/gp14/Hfq neck complex seals the pressurized, genome-filled capsid during virion maturation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.