Crystal Structures of a Piscine Betanodavirus : Mechanisms of Capsid Assembly and Viral Infection

Chen, Nai-Chi; Yoshimura, Masato; Guan, Hong-Hsiang; Wang, Ting-Yu; Misumi, Yuko; Lin, Chien-Chih; Chuankhayan, Phimonphan; Nakagawa, Atushi; Chan, Sunney I.; Tsukihara, Tomitake; Chen, Tzong-Yueh; Chen, Chun-Jung

doi:https://doi.org/10.1371/journal.ppat.1005203

Crystal Structures of a Piscine Betanodavirus : Mechanisms of Capsid Assembly and Viral Infection

Chen, Nai-Chi; Yoshimura, Masato; Guan, Hong-Hsiang et al.

PLOS Pathogens, 2015, 11(10), 1005203

Number of Access:1,260（2025-09-29 10:04 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/73666

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Title	Crystal Structures of a Piscine Betanodavirus : Mechanisms of Capsid Assembly and Viral Infection
Creator	CreatorName Chen, Nai-Chi
	CreatorName Yoshimura, Masato
	CreatorName Guan, Hong-Hsiang
	CreatorName Wang, Ting-Yu
	CreatorName Misumi, Yuko
	CreatorName Lin, Chien-Chih
	CreatorName Chuankhayan, Phimonphan
	NRID 1000020188890 1000020188890 ORCID 0000-0002-1700-7861 0000-0002-1700-7861 researchmap permalink atsushi_nakagawa atsushi_nakagawa Scopus Author ID 7202934909 7202934909 CreatorName Nakagawa, Atushi
	CreatorName Chan, Sunney I.
	NRID 1000000032277 1000000032277 CreatorName Tsukihara, Tomitake
	CreatorName Chen, Tzong-Yueh
	CreatorName Chen, Chun-Jung
Description	Chen NC, Yoshimura M, Guan HH, Wang TY, Misumi Y, et al. (2015) Crystal Structures of a Piscine Betanodavirus : Mechanisms of Capsid Assembly and Viral Infection. PLOS Pathogens 11(10): e1005203. https://doi.org/10.1371/journal.ppat.1005203
Abstract	Betanodaviruses cause massive mortality in marine fish species with viral nervous necrosis. The structure of a T = 3 Grouper nervous necrosis virus-like particle (GNNV-LP) is determined by the ab initio method with non-crystallographic symmetry averaging at 3.6 Å resolution. Each capsid protein (CP) shows three major domains: (i) the N-terminal arm, an intersubunit extension at the inner surface; (ii) the shell domain (S-domain), a jelly-roll structure; and (iii) the protrusion domain (P-domain) formed by three-fold trimeric protrusions. In addition, we have determined structures of the T = 1 subviral particles (SVPs) of (i) the delta-Pdomain mutant (residues 35−217) at 3.1 Å resolution; and (ii) the N-ARM deletion mutant (residues 35−338) at 7 Å resolution; and (iii) the structure of the individual P-domain (residues 214−338) at 1.2 Å resolution. The P-domain reveals a novel DxD motif asymmetrically coordinating two Ca^<2+> ions, and seems to play a prominent role in the calcium-mediated trimerization of the GNNV CPs during the initial capsid assembly process. The flexible N-ARM (N-terminal arginine-rich motif) appears to serve as a molecular switch for T = 1 or T = 3 assembly. Finally, we find that polyethylene glycol, which is incorporated into the Pdomain during the crystallization process, enhances GNNV infection. The present structural studies together with the biological assays enhance our understanding of the role of the Pdomain of GNNV in the capsid assembly and viral infection by this betanodavirus.
Publisher	PLOS
Source Title	PLOS Pathogens
Volume (Issue)	11(10)
Page	1005203
Date of Issued	2015-10
Language	English
Handle URL	https://hdl.handle.net/11094/73666
PISSN	15537366
eISSN	15537374
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1371/journal.ppat.1005203
Relation.isIdenticalTo	PMID 26491970
Access Rights	open access
CopyRight	© 2015 Chen NC et al. This article is licensed under a Creative Commons Attribution 4.0 International License.
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	PLOS Pathogens. 2015, 11(10), p. 1005203
DC.title	Crystal Structures of a Piscine Betanodavirus : Mechanisms of Capsid Assembly and Viral Infection
DC.creator	Chen, Nai-Chi
	Yoshimura, Masato
	Guan, Hong-Hsiang
	Wang, Ting-Yu
	Misumi, Yuko
	Lin, Chien-Chih
	Chuankhayan, Phimonphan
	Nakagawa, Atushi
	Chan, Sunney I.
	Tsukihara, Tomitake
	Chen, Tzong-Yueh
	Chen, Chun-Jung
DC.publisher	PLOS
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2015-10
DC.identifier	https://doi.org/10.1371/journal.ppat.1005203
DC.description	Chen NC, Yoshimura M, Guan HH, Wang TY, Misumi Y, et al. (2015) Crystal Structures of a Piscine Betanodavirus : Mechanisms of Capsid Assembly and Viral Infection. PLOS Pathogens 11(10): e1005203. https://doi.org/10.1371/journal.ppat.1005203
DCTERMS.abstract	Betanodaviruses cause massive mortality in marine fish species with viral nervous necrosis. The structure of a T = 3 Grouper nervous necrosis virus-like particle (GNNV-LP) is determined by the ab initio method with non-crystallographic symmetry averaging at 3.6 Å resolution. Each capsid protein (CP) shows three major domains: (i) the N-terminal arm, an intersubunit extension at the inner surface; (ii) the shell domain (S-domain), a jelly-roll structure; and (iii) the protrusion domain (P-domain) formed by three-fold trimeric protrusions. In addition, we have determined structures of the T = 1 subviral particles (SVPs) of (i) the delta-Pdomain mutant (residues 35−217) at 3.1 Å resolution; and (ii) the N-ARM deletion mutant (residues 35−338) at 7 Å resolution; and (iii) the structure of the individual P-domain (residues 214−338) at 1.2 Å resolution. The P-domain reveals a novel DxD motif asymmetrically coordinating two Ca^<2+> ions, and seems to play a prominent role in the calcium-mediated trimerization of the GNNV CPs during the initial capsid assembly process. The flexible N-ARM (N-terminal arginine-rich motif) appears to serve as a molecular switch for T = 1 or T = 3 assembly. Finally, we find that polyethylene glycol, which is incorporated into the Pdomain during the crystallization process, enhances GNNV infection. The present structural studies together with the biological assays enhance our understanding of the role of the Pdomain of GNNV in the capsid assembly and viral infection by this betanodavirus.
DC.rights	© 2015 Chen NC et al. This article is licensed under a Creative Commons Attribution 4.0 International License.
DC.format	73666
citation_title	Crystal Structures of a Piscine Betanodavirus : Mechanisms of Capsid Assembly and Viral Infection
citation_author	Chen, Nai-Chi
	Yoshimura, Masato
	Guan, Hong-Hsiang
	Wang, Ting-Yu
	Misumi, Yuko
	Lin, Chien-Chih
	Chuankhayan, Phimonphan
	Nakagawa, Atushi
	Chan, Sunney I.
	Tsukihara, Tomitake
	Chen, Tzong-Yueh
	Chen, Chun-Jung
citation_publisher	PLOS
citation_language	English
citation_date	2015-10
citation_journal_title	PLOS Pathogens
citation_volume	11
citation_issue	10
citation_firstpage	1005203
citation_doi	https://doi.org/10.1371/journal.ppat.1005203
citation_pmid	26491970
citation_public_url	https://hdl.handle.net/11094/73666

Crystal Structures of a Piscine Betanodavirus : Mechanisms of Capsid Assembly and Viral Infection

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