HSV-1 employs UL56 to antagonize expression and function of cGAMP channels

We report that infection with multiple human viruses depletes some of these cGAMP conduits. This includes herpes simplex virus 1 (HSV-1) that targets SLC46A2, P2X7, and the VRAC subunits LRRC8A and LRRC8C for degradation. The HSV-1 protein UL56 is necessary and sufficient for these effects that are mediated at least partially by proteasomal turnover. UL56 thereby inhibits cGAMP uptake via VRAC, SLC46A2, and P2X7. Taken together, HSV-1 antagonizes intercellular cGAMP transfer. We propose that this limits innate immunity by reducing cell-to-cell communication via the immunotransmitter cGAMP.PMID:38652659 | DOI:10.1016/j.celrep.2024.114122

Source: Herpes - April 23, 2024 Category: Infectious Diseases Authors: Henry T W Blest Alexander Redmond Jed Avissar Jake Barker Anne Bridgeman Gerissa Fowler Lise Chauveau Jonny Hertzog Iolanda Vendrell Roman Fischer Marie B Iversen Lichen Jing David M Koelle S øren R Paludan Benedikt M Kessler Colin M Crump Jan Rehwinkel Source Type: research