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9GYI

Cryo-EM structure of the capsid-forming phage-inducible chromosomal island (cf-PICI) EcCI2

Summary for 9GYI
Entry DOI10.2210/pdb9gyi/pdb
EMDB information51699
DescriptorMajor head protein (1 entity in total)
Functional Keywordspici, cf-pici, bacteriophage, capsid, phage-inducible chromosomal island, virus like particle
Biological sourceEscherichia coli O157:H7 str. EDL933
Total number of polymer chains4
Total formula weight172701.72
Authors
Patkowski, J.B.,Penades, J.R.,Costa, T.R.D. (deposition date: 2024-10-02, release date: 2025-09-10, Last modification date: 2025-11-26)
Primary citationHe, L.,Patkowski, J.B.,Wang, J.,Miguel-Romero, L.,Aylett, C.H.S.,Fillol-Salom, A.,Costa, T.R.D.,Penades, J.R.
Chimeric infective particles expand species boundaries in phage-inducible chromosomal island mobilization.
Cell, 188:6636-6653.e17, 2025
Cited by
PubMed Abstract: Some mobile genetic elements spread among unrelated bacterial species through unknown mechanisms. Recently, we discovered that identical capsid-forming phage-inducible chromosomal islands (cf-PICIs), a new family of phage satellites, are present across multiple species and genera, raising questions about their widespread dissemination. Here, we have identified and characterized a new biological entity enabling this transfer. Unlike other satellites, cf-PICIs produce their own capsids and package their DNA, relying solely on phage tails for transfer. cf-PICIs release non-infective, tailless capsids containing their DNA into the environment. These subcellular entities then interact with phage tails from various species, forming chimeric particles that inject DNA into different bacterial species depending on the tail present. Additionally, we elucidated the structure of the tailless cf-PICIs and the mechanism behind their unique capsid formation. Our findings illuminate the mechanisms used by satellites to spread in nature, contributing to bacterial evolution and the emergence of new pathogens.
PubMed: 40930093
DOI: 10.1016/j.cell.2025.08.019
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.24 Å)
Structure validation

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