Visualization of protein-RNA interactions in cytoplasmic polyhedrosis virus.
Unlike the multiple-shelled organization of other Reoviridae members, cytoplasmic polyhedrosis virus (CPV) has a single-shelled capsid. The three-dimensional structures of full and empty CPV by electron cryomicroscopy show identical outer shells but differ inside. The outer surface reveals a T=1 icosahedral shell decorated with spikes at its icosahedral vertices. The internal space of the empty CPV is unoccupied except for 12 mushroom-shaped densities attributed to the transcriptional enzyme complexes. The ordered double-stranded RNA inside the full capsid forms spherical shells spaced 25 A apart. The RNA-protein interactions suggest a mechanism for RNA transcription and release.
Zhang
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Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas, USA.
Zhang
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J
Yu
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Lu
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Zhang
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Jakana
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Chen
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Zhang
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Zhou
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ZH
D000818:Animals; D012831:Bombyx / Q000821:virology; D020285:Cryoelectron Microscopy; D012330:RNA, Double-Stranded / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D012087:Reoviridae / Q000648:ultrastructure*; D014764:Viral Proteins / Q000378:metabolism*; D014771:Virion / Q000648:ultrastructure
D012330:RNA, Double-Stranded; D012367:RNA, Viral; D014764:Viral Proteins