Elucidating the structural determinants of the poxvirus core using multi-modal cryo-EM (Record no. 768069)

MARC details
000 -LEADER
fixed length control field 03840ntm a22003737a 4500
003 - CONTROL NUMBER IDENTIFIER
control field AT-ISTA
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250915132911.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 250915s2024 au ||||| m||| 00| 0 eng d
040 ## - CATALOGING SOURCE
Transcribing agency ISTA
100 ## - MAIN ENTRY--PERSONAL NAME
Personal name Datler, Julia
9 (RLIN) 1084230
245 ## - TITLE STATEMENT
Title Elucidating the structural determinants of the poxvirus core using multi-modal cryo-EM
260 ## - PUBLICATION, DISTRIBUTION, ETC. (IMPRINT)
Name of publisher, distributor, etc. Institute of Science and Technology Austria
Date of publication, distribution, etc. 2024
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General note Thesis
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Formatted contents note Abstract
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Formatted contents note Acknowledgements
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Formatted contents note About the Author
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Formatted contents note List of Publications
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Formatted contents note List of Contributors
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Formatted contents note Table of Contents
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Formatted contents note List of Figures
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Formatted contents note List of Tables
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Formatted contents note List of Abbreviations
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Formatted contents note 1 Introduction
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Formatted contents note 2 Aims and Objectives
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Formatted contents note 3 Material and Methods
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Formatted contents note 4 Results
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Formatted contents note 5 Discussion
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Formatted contents note References
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Formatted contents note A Appendix 1
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Formatted contents note B Appendix 2
520 ## - SUMMARY, ETC.
Summary, etc. 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.
856 ## - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://doi.org/10.15479/at:ista:18766">https://doi.org/10.15479/at:ista:18766</a>
942 ## - ADDED ENTRY ELEMENTS (KOHA)
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  Not Lost Dewey Decimal Classification     Library Library 15/09/2025   Quiet Room AT-ISTA#003320 16/09/2025 15/09/2025 Book

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