The structure of Turnip mosaic virus, an important plant virus with a wide host range, has been solved

Plant viruses with an elongated and flexuous architecture are problematic candidates for a detailed structural characterization, since the flexuous nature of their capsids prevents crystallization, and consequently an analysis by X-ray crystallography. However, the latest methodological advances are allowing less-resolving techniques, such as cryo-electron microscopy, to reach resolution parameters almost comparable to the most advanced ones.


Thanks to cryo-electron microscopy, in-depth studies of Turnip mosaic virus, a potyvirus, virions and VLPs (virus-like particles lacking nucleic acids) have been carried out. It was possible to establish the location of different domains of the coat protein, their interactions with other subunits in the assembly, as well as the interaction with ribonucleic acid and how its absence affects intersubunit interactions and the viral particle assembled structure.

This new study allows a better understanding of the assembly, so now the functionalization of these particles, either by genetic fusion or chemical conjugation, can have an empirical basis, making these viral nanoparticles more efficacious in different biotechnological fields.


Original Paper:

Cuesta, R., Yuste-Calvo, C., Gil-Cartón, D., Sánchez, F., Ponz, F., Valle, M. 2019. Structure of Turnip mosaic virus and its viral-like particles. Scientific Reports 9, 1–6. DOI: 10.1038/s41598-019-51823-4