Search

Closteroviruses possess exceptionally long filamentous virus particles that mediate protection and active transport of the genomic RNA within infected plants. These virions are composed of a long 'body' and short 'tail' whose principal components are the major and minor capsid proteins, respectively. Here we use biochemical, genetic, and ultrastructural analyses to dissect the molecular composition and architecture of particles of beet yellows virus, a closterovirus. We demonstrate that the virion tails encapsidate the 5'-terminal, [approximately equal to] 650-nt-long, part of the viral RNA. In addition to the minor capsid protein, the viral Hsp70-homolog, 64-kDa protein, and 20-kDa protein are also incorporated into the virion tail. Atomic force microscopy of virions revealed that the tail possesses a striking, segmented morphology with the tip segment probably being built of 20-kDa protein. The unexpectedly complex structure of closterovirus virions has important mechanistic and functional implications that may also apply to other virus families. atomic force microscopy | closterovirus | RNA encapsidation | virion structure | virus transport

Transport of plant viruses from cell to cell typically involves one or more vital proteins that supply specific cell-to-cell movement functions. Long-distance transport of viruses through the vascular system is a less well understood process with requirements different from those of cell-to-cell movement. Usually vital coat protein (CP) is required for long-distance movement, but groundnut rosette umbravirus (GRV) does not code for a CP. However, this virus moves efficiently from cell to cell and long distance. We demonstrate here that the protein encoded by ORF3 of GRV can functionally replace the CP of tobacco mosaic virus (TMV) for long-distance movement. In spite of low levels of virus RNA accumulation in infected cells, chimeric TMV with a replacement of the CP gene by GRV ORF3 was able to move rapidly through the phloem. Moreover, this chimeric virus complemented long-distance movement of another CP-deficient TMV derivative expressing the gene encoding the green fluorescent protein. Thus, the GRV ORF3-encoded protein represents a class of trans-acting long-distance movement factors that can facilitate trafficking of an unrelated viral RNA.