0
0The paper outlines a structural study of the HBx protein, an essential regulatory component of the Hepatitis B virus linked to the development of liver cancer. Using NMR spectroscopy and AlphaFold predictions, researchers discovered that the HBx1–120 isoform is naturally disordered but folds locally when it hijacks human host proteins like Bcl-xL and Spindlin1. The study specifically identifies a rare inter-molecular zinc finger that allows HBx to bind tightly to Spindlin1, effectively blocking its ability to interact with methylated histone tails. By concealing these epigenetic docking sites, the virus subverts transcriptional control to promote its own replication. Ultimately, this research establishes a new experimental framework for understanding how viral intrinsically disordered proteins utilize multivalent interactions to manipulate cellular environments.
References:
Clavier A, Shida T, Droemer MA, Gómez-Evain S, von Hammerstein F, Holzinger J, Leuthold MM, Douat C, Schütz AK. HBV HBx protein masks epigenetic reader Spindlin1 via an inter-molecular zinc finger to subvert transcriptional control. Nat Commun. 2026 May 25;17(1):4687. doi: 10.1038/s41467-026-72986-5. PMID: 42185260; PMCID: PMC13213052.
