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Significance In addition to the well-characterized main nuclear latency-associated nuclear antigen (LANA) protein of Kaposi sarcoma herpesvirus (KSHV), cytoplasmic LANA isoforms are known to exist, but their function has thus far been unknown. Here we show that N-terminally truncated cytoplasmic isoforms of LANA play a role in antagonizing the innate response triggered, by means of cGMP-AMP synthase (cGAS) and stimulator of interferon genes (STING), during the reactivation of KSHV from latency. By directly interacting with cGAS, cytoplasmic LANA variants inhibit the cGAS-STING–dependent induction of interferon and thereby promote the reactivation of KSHV from latency. These findings extend the roles of a γ-herpesvirus latent protein into the lytic replication cycle.

Cytoplasmic isoforms of Kaposi sarcoma herpesvirus LANA recruit and antagonize the innate immune DNA sensor cGAS