An Assembly Intermediate Structure of Rice Dwarf Virus Reveals a Hierarchical Outer Capsid Shell Assembly Mechanism

Nakamichi, Yusuke; Miyazaki, Naoyuki; Tsutsumi, Kenta; Higashiura, Akifumi; Narita, Hiroko; Murata, Kazuyoshi; Nakagawa, Atsushi

doi:10.1016/j.str.2018.10.029

Cited by 5 publications

(2 citation statements)

References 42 publications

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“…The CrP of RnMBV1 can be associated with the protrusion protein/fiber of the toti-like viruses that are likely involved in its egress and/or entry (23,24). The CrP also reminds us about the assembly of the outer shell for the transmission in sedoreoviruses, whose intermediates only comprise outer capsid proteins at 3-fold axes (45). Therefore, the CrPs might also serve as a factor together with the aforementioned protrusion domain in MCPs for facilitating virus-to-host transmissions.…”

Section: Resultsmentioning

confidence: 99%

Capsid structure of a metazoan fungal dsRNA megabirnavirus reveals its uniquely acquired structures

Wang

Salaipeth

Miyazaki

et al. 2022

Preprint

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Rosellinia necatrix megabirnavirus 1-W779 (RnMBV1) is a non-enveloped icosahedral double-stranded (ds)RNA virus that infects the ascomycete fungus Rosellinia. necatrix, a causative agent that induces a lethal plant disease white root rot. Herein, we have first resolved the atomic structure of the RnMBV1 capsid at 3.2 Å resolution using cryo-electron microscopy (cryo-EM) single-particle analysis. Contrary to the other structurally associated viral capsid proteins, the RnMBV1 capsid protein structure exhibits an extra-long C-terminal arm and a surface protrusion domain. In addition, the previously unrecognized crown proteins are identified in a symmetry-expanded cryo-EM model and are present over the 3-fold axes. These exclusive structural features of the RnMBV1 capsid could have been acquired for playing essential roles in transmission, genome packaging, and/or particle assembly of the megabirnaviruses. Our findings, therefore, will reinforce the understanding of how the structural and molecular machineries of the megabirnaviruses influence the virulence of the disease-related ascomycete fungus.

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Section: Resultsmentioning

confidence: 99%

Capsid structure of a metazoan fungal dsRNA megabirnavirus reveals its uniquely acquired structures

Wang

Salaipeth

Miyazaki

et al. 2022

Preprint

Self Cite

View full text Add to dashboard Cite

show abstract

“…CrP also reminds us about the assembly of the outer shell for the transmission in sedoreoviruses, whose intermediates only comprise outer capsid proteins at 3-fold axes [46]. However, there is no sequence or structure similarity between the RnMBV1 CrPs and these surface proteins.…”

Section: Plos Pathogensmentioning

confidence: 99%

Capsid structure of a fungal dsRNA megabirnavirus reveals its previously unidentified surface architecture

et al. 2023

Self Cite

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Rosellinia necatrix megabirnavirus 1-W779 (RnMBV1) is a non-enveloped icosahedral double-stranded (ds)RNA virus that infects the ascomycete fungus Rosellinia necatrix, a causative agent that induces a lethal plant disease white root rot. Herein, we have first resolved the atomic structure of the RnMBV1 capsid at 3.2 Å resolution using cryo-electron microscopy (cryo-EM) single-particle analysis. Compared with other non-enveloped icosahedral dsRNA viruses, the RnMBV1 capsid protein structure exhibits an extra-long C-terminal arm and a surface protrusion domain. In addition, the previously unrecognized crown proteins are identified in a symmetry-expanded cryo-EM model and are present over the 3-fold axes. These exclusive structural features of the RnMBV1 capsid could have been acquired for playing essential roles in transmission and/or particle assembly of the megabirnaviruses. Our findings, therefore, will reinforce the understanding of how the structural and molecular machineries of the megabirnaviruses influence the virulence of the disease-related ascomycete fungus.

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Polymorphic Self‐Assembly with Procedural Flexibility for Monodisperse Quaternary Protein Structures of DegQ Enzymes

Jeon,

Han,

et al. 2024

Advanced Materials

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As large molecular tertiary structures, some proteins can act as small robots that find, bind, and chaperone target protein clients, showing the potential to serve as smart building blocks in self‐assembly fields. Instead of using such intrinsic functions, most self‐assembly methodologies for proteins aim for de novo‐designed structures with accurate geometric assemblies, which could limit procedural flexibility. Here, we present a strategy enabling polymorphic clustering of quaternary proteins, exhibiting simplicity and flexibility of self‐assembling paths for proteins in forming monodisperse quaternary cage particles. We propose that the enzyme protomer DegQ, previously solved at low resolution, may potentially be usable as a threefold symmetric building block, which can form polyhedral cages incorporated by the chaperone action of DegQ in the presence of protein clients. To obtain highly monodisperse cage particles, we utilize soft, and hence, less resistive client proteins, which can program the inherent chaperone activity of DegQ to efficient formations of polymorphic cages, depending on the size of clients. By reconstructing the atomic resolution cryo‐EM DegQ structures using obtained 12‐ and 24‐meric clusters, we validate the polymorphic clustering of DegQ enzymes in terms of soft and rigid domains, which would provide effective routes for protein self‐assemblies with procedural flexibility.This article is protected by copyright. All rights reserved

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An Assembly Intermediate Structure of Rice Dwarf Virus Reveals a Hierarchical Outer Capsid Shell Assembly Mechanism

Cited by 5 publications

References 42 publications

Capsid structure of a metazoan fungal dsRNA megabirnavirus reveals its uniquely acquired structures

Capsid structure of a metazoan fungal dsRNA megabirnavirus reveals its uniquely acquired structures

Capsid structure of a fungal dsRNA megabirnavirus reveals its previously unidentified surface architecture

Polymorphic Self‐Assembly with Procedural Flexibility for Monodisperse Quaternary Protein Structures of DegQ Enzymes

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