Ribonucleoprotein-like structures from coronavirus particles.
The structure of the ribonucleoprotein (RNP) complex of three coronaviruses was investigated. A single-stranded helix of diam. 14 to 16 nm and up to 320 nm in length was released from disrupted particles of human coronavirus strain 229E and mouse hepatitis virus strain 3 after incubation in mild conditions. The helical complexes appeared to be composed of globular subunits with long axes of 5 to 7 nm surrounding a hollow core of diam. 3 to 4 nm. The complexes were shown to be sensitive to both pancreatic RNase and to pronase. No undegraded internal component was obtained from disrupted avian infectious bronchitis virus particles. We conclude that these structures are RNP complexes. The similarity between these RNPs and those of other large lipid containing RNA viruses is discussed.
D003332:Coronaviridae / Q000648:ultrastructure*; D006801:Humans; D001351:Infectious bronchitis virus / Q000648:ultrastructure; D006517:Murine hepatitis virus / Q000648:ultrastructure; D011402:Pronase / Q000378:metabolism; D012367:RNA, Viral / Q000032:analysis*; D012260:Ribonucleases / Q000378:metabolism; D014764:Viral Proteins / Q000032:analysis*
D012367:RNA, Viral; D014764:Viral Proteins; D012260:Ribonucleases; D011402:Pronase