Molecular mechanisms reveal that human cytomegalovirus has evolved to deploy two individual glycoproteins working in synergy to efficiently evade antibody-mediated immunity mediated by Fc-gamma receptors.

Inactivation of KAP1 by mTOR-mediated phosphorylation releases human cytomegalovirus from latency, and has the potential to be used as a therapy to purge the virus from transplant organs.

The human cytomegalovirus (HCMV) interactome systematically characterises high-confidence viral-viral and viral-host protein interactions in HCMV-infected cells, facilitating multiple novel insights into HCMV and herpesviral function.

Single-cell and bulk expression analyses reveal that HCMV latent infection drives cells towards a weaker immune-responsive state, which is important for its expression and reactivation.

Analysis of human cytomegalovirus-encoded glycoprotein US10 targeting human leucocyte antigen class I molecules reveals a multimodal strategy, resulting in a geno- and allotypic-dependent effects.

Distinct binding of viral proteins to the same region on the nucleosome surface can result in contrasting changes to higher-order chromatin structure in the host cell.

The HCMV virion envelope is derived from the host exosome membrane, and exosome machinery and export pathways facilitate virion egress.

Organoids developed from matched human placental tissue define differences in antiviral signaling between cell types comprising the maternal-fetal interface.

The human cytomegalovirus US12 gene family work co-operatively to degrade large numbers of immune ligands and prevent recognition by natural killer cells.

Ribosome production is unexpectedly integrated into innate cell-intrinsic responses that regulate double strand DNA-sensing and inflammatory cytokine induction in infected and uninfected cells.