{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T15:39:19Z","timestamp":1782833959744,"version":"3.54.5"},"update-to":[{"DOI":"10.1371\/journal.ppat.1013487","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2025,9,12]],"date-time":"2025-09-12T00:00:00Z","timestamp":1757635200000}}],"reference-count":73,"publisher":"Public Library of Science (PLoS)","issue":"9","license":[{"start":{"date-parts":[[2025,9,8]],"date-time":"2025-09-08T00:00:00Z","timestamp":1757289600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001711","name":"Schweizerischer Nationalfonds zur F\u00c3\u00b6rderung der Wissenschaftlichen Forschung","doi-asserted-by":"publisher","award":["310030_214957"],"award-info":[{"award-number":["310030_214957"]}],"id":[{"id":"10.13039\/501100001711","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008475","name":"Hartmann M\u00c3\u00bcller-Stiftung f\u00c3\u00bcr Medizinische Forschung","doi-asserted-by":"publisher","award":["2378"],"award-info":[{"award-number":["2378"]}],"id":[{"id":"10.13039\/501100008475","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>SUMO-modified Tripartite Motif Protein 28 (TRIM28; KAP1) plays a crucial role in repressing endogenous retroelement (ERE) transcription. We previously provided evidence that loss of SUMO-modified TRIM28 triggered by influenza A virus (IAV) infection promotes activation of host antiviral immunity via a mechanism involving derepression of EREs and production of immunostimulatory RNAs. While the IAV NS1 protein might limit consequences of such activation via its dsRNA-binding activity, we hypothesized that other human pathogenic viruses could have evolved more direct strategies to counteract this potential ERE-based defense system. Here, we reveal that V proteins from diverse paramyxoviruses, including Measles, Mumps, Parainfluenza, and Nipah\/Hendra viruses, can all engage with TRIM28. Notably, the efficiency of engagement varies markedly between virus species, a phenotype that can be linked to specific residues within the C-terminal domain of V proteins. Further mapping showed that V proteins target both the TRIM28 Coiled-Coil domain and the TRIM28 PHD-Bromodomain, which contains the functionally-relevant TRIM28 SUMO-modification sites necessary for ERE repression. In this context, while paramyxovirus infection triggers canonical stress-associated phosphorylation of TRIM28, loss of SUMO-modified TRIM28 does not occur, and minimal induction of the TRIM28-dependent ERE RNA, HERVK14C, is observed. Furthermore, pre-infection with Parainfluenza virus type 2, which encodes a V protein that efficiently engages with TRIM28, limits subsequent IAV-triggered loss of SUMO-modified TRIM28 and upregulation of HERVK14C RNA. These findings dissect the interplay between paramyxoviruses and TRIM28, providing support for the concept of a TRIM28-regulated ERE-based antiviral defense system by uncovering a potential viral antagonistic measure.<\/jats:p>","DOI":"10.1371\/journal.ppat.1013487","type":"journal-article","created":{"date-parts":[[2025,9,8]],"date-time":"2025-09-08T17:56:12Z","timestamp":1757354172000},"page":"e1013487","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":2,"title":["TRIM28 is a target for paramyxovirus V 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