Cryo-EM Characterization of Extremophile Viruses with Dynamic Structures

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Cryo-EM Characterization of Extremophile Viruses with Dynamic Structures

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Author(s): Daniel Gutierrez-Del-Rio ¹ , Rafael Ayala ¹ , Hanna Oksanen ² , Matthias Wolf ¹ ^,

Publication date (Electronic): 21 January 2025

Conference name: 13th Asia Pacific Microscopy Congress 2025 (APMC13)

Conference date: 2-7 Febuary 2025

Keywords: virology, virus-inspired materials, dynamic structures, single particle analysis

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Abstract

Archaea, identified as a distinct domain of life in the 1970s, possess unique biological traits that enable them to thrive in extreme environments which denature most biomolecules and proteins. Archaeal viruses (AVs) display many unique morphotypes not found in bacteria or eukaryote viruses. These viral structures have evolved to protect and deliver the viral genome in the harsh environments where archaea thrive [ 1]. The study of AVs is critical to exploiting the biotechnological potential of archaea, but also for the development of virus-inspired nanomaterials.

This study focuses on a detailed structural analysis and high-resolution cryogenic electron microscopy (cryo-EM) reconstructions of the halo-archaeal virus Salterprovirus His1 (His1).

His1, an enveloped virus found in hypersaline environments, infects Halobacterium hispanica and is distinguished by its lemon-like shape, unique tail structure, and a distinctive transformation into hollow nanotubes when exposed to high-temperatures [ 2].

A near-atomic resolution reconstruction and protein mapping of His1 remains to be achieved, with particular interest in the transformation dynamics and its role in the infection mechanism ( Fig.1) [ 3]. Reconstructing the initial, intermediate, and final forms at high-resolution is crucial for understanding their exceptional molecular stability.

Fig. 1.

Heat-induced tube transformation of Salterprovirus His1.

Here, we present 3D reconstructions of the initial (lemon) and final (tube, Fig.2) forms at the highest resolution obtained to date. This preliminary data reveals distinct structural phases, motivating further detailed investigation. Beyond its basic virology interest, this self-assembling, self-replicating nanotube system shows promise as a programmable material [ 4].

Fig. 2.

a) Cryo-EM micrography of Salterprovirus His1 in both lemon and tubular forms. b) 3D reconstruction of His1’s tubular form. c) Detail of major capsid protein (MCP).

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Publication date (Electronic): 21 January 2025

Electronic Location Identifier: e316

Affiliations

[1 ]Molecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology, Okinawa, Japan

[2 ]Biological and Environmental Sciences Department, University of Helsinki, Helsinki, Finland

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*Corresponding author: Matthias.Wolf@ 123456oist.jp

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Daniel Gutierrez-Del-Rio https://orcid.org/0000-0002-4592-9345

Rafael Ayala https://orcid.org/0000-0002-9332-4623

Hanna Oksanen https://orcid.org/0000-0003-3047-8294

Matthias Wolf https://orcid.org/0000-0001-8480-0918

Article

DOI: 10.14293/APMC13-2025-0316

SO-VID: 73dfd9eb-2a8a-42fa-a99d-35b0033ad167

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Published under Creative Commons Attribution 4.0 International ( CC BY 4.0). Users are allowed to share (copy and redistribute the material in any medium or format) and adapt (remix, transform, and build upon the material for any purpose, even commercially), as long as the authors and the publisher are explicitly identified and properly acknowledged as the original source.

Conference name: 13th Asia Pacific Microscopy Congress 2025

Conference acronym: APMC13

Conference number: 13

Conference location: Brisbane, Australia

Conference date: 2-7 Febuary 2025

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References

M Krupovic, et al. Virus Res 244 (2018), p. 181-193. DOI:10.1016/j.virusres.2017.11.025
C Hong, et al. PNAS 112 (2015), p. 2449-2454. DOI: 10.1073/pnas.1425008112
F Wang, et al. Cell 185 (2022), p. 1297-1307.e11 DOI: 10.1016/j.cell.2022.02.019
A M Wen, N F Steinmetz, Chem Soc Rev 45 (2016), p. 4074-4126. DOI: 10.1039/C5CS00287G

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[1] M Krupovic, et al. Virus Res 244 (2018), p. 181-193. DOI:10.1016/j.virusres.2017.11.025

[2] C Hong, et al. PNAS 112 (2015), p. 2449-2454. DOI: 10.1073/pnas.1425008112

[3] F Wang, et al. Cell 185 (2022), p. 1297-1307.e11 DOI: 10.1016/j.cell.2022.02.019

[4] A M Wen, N F Steinmetz, Chem Soc Rev 45 (2016), p. 4074-4126. DOI: 10.1039/C5CS00287G

Cryo-EM Characterization of Extremophile Viruses with Dynamic Structures

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