Activities

High resolution cryoEM structure of flexible filamentous plant viruses

 

Seminar

High resolution cryoEM structure of flexible filamentous plant viruses

Mikel Valle, PhD

High resolution cryoEM structure of flexible filamentous plant viruses Viruses with flexuous filamentous particles include plant pathogens that cause large economic losses in crops. These viruses contain several hundreds of coat protein (CP) copies arranged in helical fashion protecting a single stranded (+)ssRNA and display a common overall design. Their flexible nature has been a burden for crystallographic studies, and their structure has remained elusive. The latest developments in cryo-electron microscopy (cryoEM) have provided "cheaper" atomic resolution potential. We have characterized the structure of two flexuous plant viruses at ~4.0 Å resolution by cryoEM. The derived atomic models have revealed their structural homology and a universally conserved RNA biding site, a potential target for antiviral phytosanitary compounds. Surprisingly, the described fold for their CPs is also similar to the one displayed by nucleoproteins of animal viruses such as influenza.