{
  "abstract": "Herpesviruses are a large group of double-stranded-DNA viruses that replicate their genomes in the nucleus, forming large replication compartments during lytic infection. Herpesviruses are known to modulate host DNA replication and DNA damage-repair proteins to promote their replication. Ubiquitination is a cellular process that can alter protein stability, localization, and availability, including that of multiple proteins involved in genome maintenance. Ubiquitin-specific proteases (USPs) are a class of deubiquitinating enzymes (DUBs) that counter this process by removing ubiquitin chains, thus acting as another level of regulation. Proteins from each of the three herpesvirus subfamilies (alpha-, beta-, and gammaherpesviruses) have been reported to interact with at least one host USP, and USP7 in particular is reported as a target in representatives of all three subfamilies. In this review, we give an up-to-date summary of herpesviruses–USPs interactions, with special emphasis on DNA replication, and how these interactions could shape infection outcomes. We also examine published proteomic datasets for herpesvirus-driven host-proteome modulation and offer a framework for future directions to prioritize potentially important, understudied USPs. Lastly, we visit herpesvirus-encoded DUBs and highlight their roles in viral replication by remodeling ubiquitin signaling, discussing viral DUBs and virus–USP interfaces as proposed antiviral targets.",
  "abstract_shown": true,
  "affiliations": [
    "Department of Molecular Medicine, Mayo Clinic, Rochester, MN 55905, USA"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 3,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Mohamed Maarouf",
      "orcid": "0000-0002-1762-5387"
    },
    {
      "affs": [
        0
      ],
      "name": "Christopher S. Peterson"
    },
    {
      "affs": [
        0
      ],
      "name": "Kareem N. Mohni",
      "orcid": "0000-0001-6112-8022"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/59mqjr8yycrgs.bib",
  "cited_by": 0,
  "doi": "10.3390/ijms27219631",
  "fulltext_url": null,
  "id": "59mqjr8yycrgs",
  "issns": [
    "1422-0067"
  ],
  "landing_url": "https://www.mdpi.com/1422-0067/27/21/9631",
  "language": null,
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1312|Ubiquitin and proteasome pathways"
    ]
  ],
  "openalex": "W7224116923",
  "pdf_url": null,
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-28",
  "publisher": "MDPI AG",
  "ris": "https://research.draconitic.com/paper/59mqjr8yycrgs.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:57Z",
      "native_id": "10.3390/ijms27219631",
      "source": "crossref",
      "url": "https://www.mdpi.com/1422-0067/27/21/9631"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Ubiquitin and proteasome pathways",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Host Ubiquitin-Specific Proteases Regulate All Stages of Herpesvirus Infection",
  "title_text": "Host Ubiquitin-Specific Proteases Regulate All Stages of Herpesvirus Infection",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:18:57Z",
  "url": "https://research.draconitic.com/paper/59mqjr8yycrgs",
  "venue": "International Journal of Molecular Sciences",
  "versions": []
}