Aa. Agranovsky et al., RATTLESNAKE STRUCTURE OF A FILAMENTOUS PLANT RNA VIRUS BUILT OF 2 CAPSID PROTEINS, Proceedings of the National Academy of Sciences of the United Statesof America, 92(7), 1995, pp. 2470-2473
Elongated particles of simple RNA viruses of plants are composed of an
RNA molecule coated with numerous identical capsid protein subunits t
o form a regular helical structure, of which tobacco mosaic virus is t
he archetype. Filamentous particles of the closterovirus beet yellows
virus (BYV) reportedly contain approximate to 4000 identical 22-kDa (p
it) capsid protein subunits. The BYV genome encodes a 24-kDa protein (
p24) that is structurally related to the p22. We searched for the p24
in BYV particles by using immunoelectron microscopy with specific anti
bodies against the recombinant p24 protein and its N-terminal peptide,
A 75-nm segment at one end of the 1370-nm filamentous viral particle
was found to be consistently labeled with both types of antibodies, th
us indicating that p24 is indeed the second capsid protein and that th
e closterovirus particle, unlike those of other plant viruses with hel
ical symmetry, has a ''rattlesnake'' rather than uniform structure.