ArticleNature communications2024
Capsid structure of bacteriophage ΦKZ provides insights into assembly and stabilization of jumbo phages.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Article
- The biology of jumbo phages.Nature communications · 2026Review
- Structural atlas of the intact jumbo phage phiKZ.Nature communications · 2026Article
- Genomic analysis of jumbo coliphage fEgEco12.Archives of virology · 2026Article
- Bridging the Structural Gap: A Methodological Review of Cryo-Electron Microscopy for Underrepresented Viruses.Viruses · 2026Review
- Structure of defense against restriction proteins DarA and Hdf in phage P1 reveals a new molecular mechanism during phage assembly, infection and DNA ejection.PLoS pathogens · 2026Article
- Bacteriophage genome-wide transposon mutagenesis.bioRxiv : the preprint server for biology · 2025Article
- Controlling nanocage assembly, towards developing a one-health "plug & play" platform for targeted therapy.Chemical communications (Cambridge, England) · 2025Review
- Novel Giant Phages vB_AerVM_332-Vera and vB_AerVM_332-Igor and Siphophage vB_AerVS_332-Yulya Infecting the SameViruses · 2025Article
Corrections and comments
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Jumbo phages are a group of tailed bacteriophages with large genomes and capsids. As a prototype of jumbo phage, ΦKZ infects Pseudomonas aeruginosa, a multi-drug-resistant (MDR) opportunistic pathogen leading to acute or chronic infection in immunocompromised individuals. It holds potential to be used as an antimicrobial agent and as a model for uncovering basic phage biology. Although previous low-resolution structural studies have indicated that jumbo phages may have more complicated capsid structures than smaller phages such as HK97, the detailed structures and the assembly mechanism of their capsids remain largely unknown. Here, we report a 3.5-Å-resolution cryo-EM structure of the ΦKZ capsid. The structure unveiled ten minor capsid proteins, with some decorating the outer surface of the capsid and the others forming a complex network attached to the capsid's inner surface. This network seems to play roles in driving capsid assembly and capsid stabilization. Similar mechanisms of capsid assembly and stabilization are probably employed by many other jumbo viruses.
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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 Socratic graph.