Natural history of eukaryotic DNA viruses with double jelly- roll major capsid proteins

• 成果类型: Article
• 署名作者: Krupovic, Mart; Kuhn, Jens H.; Fischer, Matthias G.; V. Koonin, Eugene; Redrejo, Modesto
• 署名单位: Pasteur Network; Universite Paris Cite; Institut Pasteur Paris; National Institutes of Health (NIH) - USA; NIH National Institute of Allergy & Infectious Diseases (NIAID); Max Planck Society; National Institutes of Health (NIH) - USA; NIH National Library of Medicine (NLM)
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-11864
• DOI: 10.1073/pnas.2405771121
• 发表日期: 2024-06-04
• 关键词: mobile genetic elements; cysteine proteases; terminal protein; FAMILY; genome; polymerases; transpovirons; transposons; EVOLUTION; sequence

摘要

The phylum Preplasmiviricota (kingdom Bamfordvirae , realm Varidnaviria ) is a broad assemblage of diverse viruses with comparatively short double - stranded DNA genomes (<50 kbp) that produce icosahedral capsids built from double jelly - roll major capsid proteins. Preplasmiviricots infect hosts from all cellular domains, testifying to their ancient origin, and, in particular, are associated with six of the seven supergroups of eukaryotes. Preplasmiviricots comprise four major groups of viruses, namely, polintons, polinton - like viruses (PLVs), virophages, and adenovirids. We used protein structure modeling and analysis to show that protein - primed DNA polymerases (pPolBs) of polintons, virophages, and cytoplasmic linear plasmids encompass an N - terminal domain homologous to the terminal proteins (TPs) of prokaryotic PRD1 - like tectivirids and eukaryotic adenovirids that are involved in protein - primed replication initiation, followed by a viral ovarian tumor-like cysteine deubiquitinylase (vOTU) domain. The vOTU domain is likely responsible for the cleavage of the TP from the large pPolB polypeptide and is inactivated in adenovirids, in which TP is a separate protein. Many PLVs and transpovirons encode a distinct derivative of polinton - like pPolB that retains the TP, vOTU, and pPolB polymerization palm domains but lacks the exonuclease domain and instead contains a superfamily 1 helicase domain. Analysis of the presence/ absence and inactivation of the vOTU domains and replacement of pPolB with other DNA polymerases in eukaryotic preplasmiviricots enabled us to outline a complete scenario for their origin and evolution.