Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery.
The mechanisms by which most double-stranded DNA viruses package and release their genomic DNA are not fully understood. Single particle cryo-electron microscopy and asymmetric 3D reconstruction reveal the organization of the complete bacteriophage P22 virion, including the protein channel through which DNA is first packaged and later ejected. This channel is formed by a dodecamer of portal proteins and sealed by a tail hub consisting of two stacked barrels capped by a protein needle. Six trimeric tailspikes attached around this tail hub are kinked, suggesting a functional hinge that may be used to trigger DNA release. Inside the capsid, the portal's central channel is plugged by densities interpreted as pilot/injection proteins. A short rod-like density near these proteins may be the terminal segment of the dsDNA genome. The coaxially packed DNA genome is encapsidated by the icosahedral shell. This complete structure unifies various biochemical, genetic, and crystallographic data of its components from the past several decades.
Chang
Juan
J
Graduate Program in Structural and Computational Biology and Molecular Biophysics, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.
Weigele
Peter
P
King
Jonathan
J
Chiu
Wah
W
Jiang
Wen
W
D017100:Bacteriophage P22 / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D002213:Capsid / Q000737:chemistry*; D020285:Cryoelectron Microscopy; D042003:DNA Packaging; D004279:DNA, Viral / Q000378:metabolism*; D014764:Viral Proteins / Q000737:chemistry
D004279:DNA, Viral; D014764:Viral Proteins