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. 2025 Jun 5;33(6):1063-1073.e2.
doi: 10.1016/j.str.2025.03.007. Epub 2025 Apr 1.

Structure of the Staphylococcus aureus bacteriophage 80α neck shows details of the DNA, tail completion protein, and tape measure protein

James L Kizziah  1 , Amarshi Mukherjee  1 , Laura K Parker  1 , Terje Dokland  2
Affiliations

Structure of the Staphylococcus aureus bacteriophage 80α neck shows details of the DNA, tail completion protein, and tape measure protein

James L Kizziah et al. Structure. .

Abstract

The Staphylococcus aureus pathogenicity islands (SaPIs), including SaPI1, are a type of mobile genetic elements (MGEs) that are mobilized at high frequency by "helper" bacteriophages, such as 80α, leading to packaging of the SaPI genomes into virions made from helper-encoded structural proteins. 80α and SaPI1 virions consist of an icosahedral head connected via a portal vertex to a long, non-contractile tail. A connector or "neck" forms the interface between the tail and the head. Here, we have determined the high-resolution structure of the neck section of SaPI1 virions, including the dodecameric portal and head-tail-connector proteins, and the hexameric head-tail joining, tail terminator and major tail proteins. We also resolved the DNA, the tail completion protein (TCP), and the tape measure protein (TMP) inside the tail, features that have not previously been observed at high resolution. Our study provides insights into the assembly and infection process in this important group of MGEs.

Keywords: 3D reconstruction; DNA packaging; Staphylococcus aureus pathogenicity island 1; bacteriophage tail; connector; cryo-electron microscopy; ejection; portal protein; virus structure.

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Conflict of interest statement

Declaration of interests The authors declare no competing interests.

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