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. 1995 Mar 28;92(7):2470–2473. doi: 10.1073/pnas.92.7.2470

"Rattlesnake" structure of a filamentous plant RNA virus built of two capsid proteins.

A A Agranovsky 1, D E Lesemann 1, E Maiss 1, R Hull 1, J G Atabekov 1
PMCID: PMC42239  PMID: 7708667

Abstract

Elongated particles of simple RNA viruses of plants are composed of an RNA molecule coated with numerous identical capsid protein subunits to form a regular helical structure, of which tobacco mosaic virus is the archetype. Filamentous particles of the closterovirus beet yellow virus (BYV) reportedly contain approximately 4000 identical 22-kDa (p22) 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 antibodies 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, thus indicating that p24 is indeed the second capsid protein and that the closterovirus particle, unlike those of other plant viruses with helical symmetry, has a "rattlesnake" rather than uniform structure.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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