{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T08:28:56Z","timestamp":1793176136057,"version":"4.5.0"},"reference-count":82,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2025,11,25]],"date-time":"2025-11-25T00:00:00Z","timestamp":1764028800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2025,11,25]],"date-time":"2025-11-25T00:00:00Z","timestamp":1764028800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI127335"],"award-info":[{"award-number":["AI127335"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["P51 OD 011092"],"award-info":[{"award-number":["P51 OD 011092"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R37 AI21640"],"award-info":[{"award-number":["R37 AI21640"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["T32 AI170496-01A1"],"award-info":[{"award-number":["T32 AI170496-01A1"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2025,11,25]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title\/>\n                    <jats:p>\n                      Human cytomegalovirus (HCMV) is a ubiquitous pathogen that persists throughout the lifetime of the host due to the establishment of latency. HCMV encodes four putative G protein-coupled receptors (GPCRs): US27, US28, UL33, and UL78. A definitive role for UL78 in HCMV infection has yet to be elucidated. Utilizing an\n                      <jats:italic toggle=\"yes\">in vitro<\/jats:italic>\n                      CD34\n                      <jats:sup>+<\/jats:sup>\n                      hematopoietic progenitor cell (HPC) model, we demonstrate that a recombinant virus lacking UL78 protein expression fails to efficiently reactivate from latent infection. Furthermore, we show that UL78 preferentially couples to the G\u03b1\n                      <jats:sub>i<\/jats:sub>\n                      family of G proteins and that a recombinant HCMV containing mutations in the UL78 G protein-coupling DRL motif also fails to reactivate from latent infection. Together, our findings indicate that G\u03b1\n                      <jats:sub>i<\/jats:sub>\n                      coupling is important for UL78 function during reactivation in latently infected CD34\n                      <jats:sup>+<\/jats:sup>\n                      HPCs. To better understand the role of UL78, we conducted proteomic analyses in HCMV-UL78-TurboID-infected fibroblasts and CD34\n                      <jats:sup>+<\/jats:sup>\n                      HPCs undergoing reactivation from latency. Congruent with our coupling data, we found that G\u03b1\n                      <jats:sub>i<\/jats:sub>\n                      was the only heterotrimeric G\u03b1 protein in proximity to UL78. Pathway analysis of the UL78 interactome revealed that proteins associated with membrane trafficking, signaling, and the nuclear pore complex were enriched in both cell types. In addition, the UL78 interactome contained viral proteins with nuclear localization including viral transcription and DNA replication machinery. Nuclear localization of UL78 was validated using cell fractionation, immunofluorescence microscopy, and proteomic analysis of isolated nuclei. Together, our results provide novel insights into the localization and function of UL78, previously unknown to contribute to reactivation from latent infection.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>IMPORTANCE<\/jats:title>\n                    <jats:p>\n                      Human cytomegalovirus (HCMV) remains one of the most widespread viral infections globally. Primary HCMV infection is typically asymptomatic and leads to the establishment of latency in myeloid lineage cells, where the virus persists for the host\u2019s lifetime. Reactivation of latent HCMV can cause severe complications, particularly in immunocompromised individuals, such as transplant recipients and people living with HIV. Several factors influence the transition from latent to lytic infection, including signal transduction through the viral G protein-coupled receptors: US27, US28, UL33, and UL78. Using an advanced\n                      <jats:italic toggle=\"yes\">in vitro<\/jats:italic>\n                      model, we show that recombinant viruses lacking UL78 fail to efficiently reactivate from latent infection. Moreover, we show that UL78 preferentially couples to the G\u03b1\n                      <jats:sub>i<\/jats:sub>\n                      family of G proteins via a conserved DRL motif, and this coupling is required for efficient reactivation. These results were confirmed by proximity-dependent labeling experiments, where we identified G\u03b1\n                      <jats:sub>i<\/jats:sub>\n                      and several other proteins involved in trafficking, signaling, transcription, and nuclear localization. Nuclear localization of UL78 was confirmed by cell fractionation, immunofluorescence microscopy, and proximity-dependent labeling in isolated nuclei. Collectively, our results uncover a novel role for UL78 in reactivation from latency and shed new light on its localization and function.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/jvi.01402-25","type":"journal-article","created":{"date-parts":[[2025,10,8]],"date-time":"2025-10-08T13:04:28Z","timestamp":1759928668000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":3,"title":["Human cytomegalovirus UL78 is a nuclear-localized GPCR necessary for efficient reactivation from latent infection in CD34\n                    <sup>+<\/sup>\n                    hematopoietic progenitor cells"],"prefix":"10.1128","volume":"99","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3611-3715","authenticated-orcid":false,"given":"Samuel","family":"Medica","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00d4pqn65","id-type":"ROR","asserted-by":"publisher"}],"name":"Vaccine & 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