In vitro reconstitution shows how HIV-1 Gag assemblies on membranes can package the RNA genome in the presence of a vast excess of competing cellular RNAs, and that selectivity and immature lattice assembly are deeply intertwined with one another.
Nucleation, elasticity theory, and simulations were combined to construct a general phase diagram that elucidates the conditions for successful viral assembly and the key factors to prevent it.
A pliable hydrophobic interface in the HIV-1 Rev protein enables assembly of diverse oligomeric structures, guided by the RRE scaffold present in HIV-1 mRNAs.
A structural comparison of different states of the protein responsible for encapsidation of the viral RNA genome provides mechanistic insights into this process.
A combination of X-ray crystallography, molecular dynamics and small angle X-ray scattering shows that the transcription antiterminator M2-1 is a structurally dynamic homotetramer that undergoes large concerted conformational changes upon binding its target RNA.
Exploiting virus-encoded ion channels as drug targets drove a multi-faceted approach to deriving potent small molecules targeting HCV p7, simultaneously providing new insights into its fundamental biology.
Structural and functional studies reveal how Newcastle disease virus nucleocapsid protects its viral genome through a self-capping mechanism, which is important for new antiviral drug design.
