Structural Insights into Common and Host-Specific Receptor-Binding Mechanisms in Algal Picorna-like Viruses
(2022) In Viruses 14(11).- Abstract
Marnaviridae viruses are abundant algal viruses that regulate the dynamics of algal blooms in aquatic environments. They employ a narrow host range because they merely lyse their algal host species. This host-specific lysis is thought to correspond to the unique receptor-binding mechanism of the Marnaviridae viruses. Here, we present the atomic structures of the full and empty capsids of Chaetoceros socialis forma radians RNA virus 1 built-in 3.0 Å and 3.1 Å cryo-electron microscopy maps. The empty capsid structure and the structural variability provide insights into its assembly and uncoating intermediates. In conjunction with the previously reported atomic model of the Chaetoceros tenuissimus RNA virus type II capsid, we have... (More)
Marnaviridae viruses are abundant algal viruses that regulate the dynamics of algal blooms in aquatic environments. They employ a narrow host range because they merely lyse their algal host species. This host-specific lysis is thought to correspond to the unique receptor-binding mechanism of the Marnaviridae viruses. Here, we present the atomic structures of the full and empty capsids of Chaetoceros socialis forma radians RNA virus 1 built-in 3.0 Å and 3.1 Å cryo-electron microscopy maps. The empty capsid structure and the structural variability provide insights into its assembly and uncoating intermediates. In conjunction with the previously reported atomic model of the Chaetoceros tenuissimus RNA virus type II capsid, we have identified the common and diverse structural features of the VP1 surface between the Marnaviridae viruses. We have also tested the potential usage of AlphaFold2 for structural prediction of the VP1s and a subsequent structural phylogeny for classifying Marnaviridae viruses by their hosts. These findings will be crucial for inferring the host-specific receptor-binding mechanism in Marnaviridae viruses.
(Less)
- author
- Wang, Han
; Munke, Anna
LU
; Li, Siqi ; Tomaru, Yuji and Okamoto, Kenta
- publishing date
- 2022-11
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- algal bloom, algal virus, icosahedral viruses, Marnaviridae, ssRNA viruses, diatom virus, virus, capsid structure, cryo-EM, cryo-electron microscopy
- in
- Viruses
- volume
- 14
- issue
- 11
- article number
- 2369
- publisher
- MDPI AG
- external identifiers
-
- pmid:36366467
- scopus:85141632923
- ISSN
- 1999-4915
- DOI
- 10.3390/v14112369
- language
- English
- LU publication?
- no
- additional info
- Publisher Copyright: © 2022 by the authors.
- id
- 0daefbea-3d46-49ff-83fd-a7ff952a7d1e
- date added to LUP
- 2025-04-15 22:33:20
- date last changed
- 2025-06-25 10:57:07
@article{0daefbea-3d46-49ff-83fd-a7ff952a7d1e, abstract = {{<p>Marnaviridae viruses are abundant algal viruses that regulate the dynamics of algal blooms in aquatic environments. They employ a narrow host range because they merely lyse their algal host species. This host-specific lysis is thought to correspond to the unique receptor-binding mechanism of the Marnaviridae viruses. Here, we present the atomic structures of the full and empty capsids of Chaetoceros socialis forma radians RNA virus 1 built-in 3.0 Å and 3.1 Å cryo-electron microscopy maps. The empty capsid structure and the structural variability provide insights into its assembly and uncoating intermediates. In conjunction with the previously reported atomic model of the Chaetoceros tenuissimus RNA virus type II capsid, we have identified the common and diverse structural features of the VP1 surface between the Marnaviridae viruses. We have also tested the potential usage of AlphaFold2 for structural prediction of the VP1s and a subsequent structural phylogeny for classifying Marnaviridae viruses by their hosts. These findings will be crucial for inferring the host-specific receptor-binding mechanism in Marnaviridae viruses.</p>}}, author = {{Wang, Han and Munke, Anna and Li, Siqi and Tomaru, Yuji and Okamoto, Kenta}}, issn = {{1999-4915}}, keywords = {{algal bloom; algal virus; icosahedral viruses; Marnaviridae; ssRNA viruses; diatom virus; virus; capsid structure; cryo-EM; cryo-electron microscopy}}, language = {{eng}}, number = {{11}}, publisher = {{MDPI AG}}, series = {{Viruses}}, title = {{Structural Insights into Common and Host-Specific Receptor-Binding Mechanisms in Algal Picorna-like Viruses}}, url = {{http://dx.doi.org/10.3390/v14112369}}, doi = {{10.3390/v14112369}}, volume = {{14}}, year = {{2022}}, }