Intrinsic Disorder in Viral Proteins Genome-Linked
Author Information
Author(s): Hébrard Eugénie, Bessin Yannick, Michon Thierry, Longhi Sonia, Uversky Vladimir N, Delalande François, Van Dorsselaer Alain, Romero Pedro, Walter Jocelyne, Declerk Nathalie, Fargette Denis
Primary Institution: UMR 1097 Résistance des Plantes aux Bio-agresseurs, IRD, CIRAD, Université de Montpellier II
Hypothesis
Intrinsic disorder is a common feature of VPgs in various viral species.
Conclusion
The study shows that both RYMV and LMV VPgs contain intrinsically disordered regions, suggesting that intrinsic disorder is a common characteristic of VPgs across different viral genera.
Supporting Evidence
- RYMV and LMV VPgs were shown to be predominantly or partly unstructured in solution.
- Disordered regions were predicted in all VPg sequences regardless of the viral genus or family.
- Experimental evidence supports the presence of intrinsically disordered regions in RYMV and LMV VPgs.
Takeaway
Some proteins in viruses, called VPgs, are like spaghetti—long and tangled instead of neatly folded. This helps them do important jobs in the virus's life cycle.
Methodology
Bacterial expression, purification, and biochemical characterization of VPgs from RYMV and LMV were performed, along with disorder predictions using various computational tools.
Limitations
The study's disorder predictions may not accurately reflect the actual disordered regions due to the diverse nature of VPg sequences.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website