The structure of phage L's Dec demonstrates a new fold within this family of proteins, and shows modulation of capsid binding occurs through two sites, with site 1 being preferred.

Interactions were visualized between the nuclear egress complex from herpes simplex virus and a capsid protein that could promote nucleocytoplasmic translocation of the capsid in infected cells.

Duck Hepatitis B core protein forms capsids with a slowly folding extension domain which folding competence is important for viral replication.

Small molecule antivirals that drive assembly of HBV capsid protein can also bind to pre-assembled capsids causing them to change morphology or even break, suggesting a complex transduction of binding effects across the capsid.

Conformational flexibility in HIV-1 capsid, provided by cyclophilin A binding, facilitates evasion of capsid-targeting restriction factor MxB, while allowing sequence change to facilitate cytotoxic T-cell evasion.

Higher-order assembly enables and links pathogen recognition and downstream steps in the TRIM5-mediated anti-HIV response.

Atomic structures suggest a novel mechanism for the regulation of mRNA transcription and capping in dsRNA viruses.

Disassembly of the HIV-1 capsid is a catastrophic process, whereby initiation and propagation can be controlled independently by molecules that bind to different features of the capsid lattice.

Enterovirus A71 adaptation to bind heparan sulfate as receptor comes with compensation that destabilizes its virus capsid.

Efficient nuclear transport of very large biomolecules, relevant for viral transport, scales non-linearly with size and its kinetics can be explained by a simple two-parameter energetic model.