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

アクセス数:1,195件（2025-07-13 03:11 集計）

固定URL: https://hdl.handle.net/11094/73666

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タイトル	Crystal Structures of a Piscine Betanodavirus : Mechanisms of Capsid Assembly and Viral Infection
著者	著者名 Chen, Nai-Chi
	著者名 Yoshimura, Masato
	著者名 Guan, Hong-Hsiang
	著者名 Wang, Ting-Yu
	著者名 Misumi, Yuko
	著者名 Lin, Chien-Chih
	著者名 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 著者名 Nakagawa, Atushi
	著者名 Chan, Sunney I.
	NRID 1000000032277 1000000032277 著者名 Tsukihara, Tomitake
	著者名 Chen, Tzong-Yueh
	著者名 Chen, Chun-Jung
内容	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
抄録	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.
出版者	PLOS
収録物名	PLOS Pathogens
巻(号)	11(10)
ページ	1005203
刊行年月	2015-10
言語	英語
ハンドルURL	https://hdl.handle.net/11094/73666
PISSN	15537366
eISSN	15537374
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1371/journal.ppat.1005203
関連情報 (isIdenticalTo)	PMID 26491970
アクセス権	open access
権利情報	© 2015 Chen NC et al. This article is licensed under a Creative Commons Attribution 4.0 International License.
出版タイプ	Version of Record
カテゴリ	学術雑誌論文 Journal Article

資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
DCMI資源タイプ	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	英語
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	英語
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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