---
res:
  bibo_abstract:
  - Poxviruses are large pleomorphic double-stranded DNA viruses that include well
    known members such as variola virus, the causative agent of smallpox, Mpox virus,
    as well as Vaccinia virus (VACV), which serves as a vaccination strain for formerly
    mentioned viruses. VACV is a valuable model for studying large pleomorphic DNA
    viruses in general and poxviruses specifically, as many features, such as core
    morphology and structural proteins, are well conserved within this family. Despite
    decades of research, our understanding of the structural components and proteins
    that comprise the poxvirus core in mature virions remains limited. Although major
    core proteins were identified via indirect experimental evidence, the core's complexity,
    with its large size, structure and number of involved proteins, has hindered efforts
    to achieve high-resolution insights and to define the roles of the individual
    proteins. The specific protein composition of the core's individual layers, including
    the palisade layer and the inner core wall, has remained unclear. In this study,
    we have merged multiple approaches, including single particle cryo electron microscopy
    of purified virus cores, cryo-electron tomography and subtomogram averaging of
    mature virions and molecular modeling to elucidate the structural determinants
    of the VACV core. Due to the lack of experimentally derived structures, either
    in situ or reconstituted in vitro, we used Alphafold to predict models of the
    putative major core protein candidates, A10, 23k, A3, A4, and L4. Our results
    show that the VACV core is composed of several layers with varying local symmetries,
    forming more intricate interactions than observed previously. This allowed us
    to identify several molecular building blocks forming the viral core lattice.
    In particular, we identified trimers of protein A10 as a major core structure
    that forms the palisade layer of the viral core. Additionally, we revealed that
    six petals of a flower shaped core pore within the core wall are composed of A10
    trimers. Furthermore, we obtained a cryo-EM density for the inner core wall that
    could potentially accommodate an A3 dimer. Integrating descriptions of protein
    interactions from previous studies enabled us to provide a detailed structural
    model of the poxvirus core wall, and our findings indicate that the interactions
    within A10 trimers are likely consistent across orthopox- and parapoxviruses.
    This combined application of cryo-SPA and cryo-ET can help overcome obstacles
    in studying complex virus structures in the future, including their key assembly
    proteins, interactions, and the formation into a core lattice. Our work provides
    important fundamental new insights into poxvirus core architecture, also considering
    the recent re-emergence of poxviruses.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Julia
      foaf_name: Datler, Julia
      foaf_surname: Datler
      foaf_workInfoHomepage: http://www.librecat.org/personId=3B12E2E6-F248-11E8-B48F-1D18A9856A87
    orcid: 0000-0002-3616-8580
  bibo_doi: 10.15479/at:ista:18766
  dct_date: 2024^xs_gYear
  dct_isPartOf:
  - http://id.crossref.org/issn/2663-337X
  - http://id.crossref.org/issn/978-3-99078-049-7
  dct_language: eng
  dct_publisher: Institute of Science and Technology Austria@
  dct_subject:
  - cryo-EM
  - cryo-ET
  - cryo-SPA
  - Structural Virology
  - Poxvirus
  - Vaccinia Virus
  - Structural Biology
  dct_title: Elucidating the structural determinants of the poxvirus core using multi-modal
    cryo-EM@
...