Visualization of Protein-RNA Interactions in Cytoplasmic Polyhedrosis Virus

Author:

Zhang H.1,Zhang J.2,Yu X.2,Lu X.2,Zhang Q.2,Jakana J.3,Chen D. H.14,Zhang X.4,Zhou Z. H.1

Affiliation:

1. Department of Pathology and Laboratory Medicine, University of Texas—Houston Medical School,1 and

2. State Key Lab for Biocontrol, Institute of Entomology, Zhongshan University, Guangzhou 510275,2 and

3. Department of Biochemistry, Baylor College of Medicine,3 Houston, Texas, and

4. Beijing Laboratory of Electron Microscopy, Institute of Physics, Chinese Academy of Sciences, Beijing 100080,4 China

Abstract

ABSTRACT 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 Å apart. The RNA-protein interactions suggest a mechanism for RNA transcription and release.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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