A combination of detailed sampling and mathematical modeling suggests that the response of immune cells to reactivation of herpes simplex virus 2 is extremely rapid and effective within microscopic areas of genital skin.

Novel cell-free biochemical experiments show that the host GTPase MxB can restrict the infection of alphaherpesviruses by disassembling the sturdy viral capsids so that they can no longer protect the viral genomes.

Internal DNA pressure of tens of atmospheres inside a herpesvirus capsid powers ejection of the viral genome into a cell nucleus, causing infection.

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.

A restriction factor induced by interferons blocks the replication of herpesviruses by disassembling the capsid proteins surrounding their genome.

A conserved viral protein complex that promotes membrane wrapping of nascent herpesvirus particles shows structural similarity to cellular membrane-remodelling proteins, suggesting functional mimicry.

Characterization of PML subnuclear structures during human cytomegalovirus infection demonstrates that prolonged interferon and DNA damage signaling can induce giant PML nuclear bodies which sequentially entrap both nucleic acids and viral proteins as a cytoprotective mechanism.

CRISPR genome editing technology can efficiently introduce mutations into lytic and latent HSV genomes to block lytic replication and reactivation of latent herpes simplex virus genome though differential mechanisms.

Transient DNA interactions by DNA-binding proteins are utilized by herpes simple virus as an alternative route to generate membraneless compartments in the nucleus without invoking phase separation.

A combination of imaging techniques reveals how herpes simplex virus type 1 assembles within infected cells, highlighting the roles of essential viral proteins in viral assembly and exit.