Evidence map›Paper›PMID 26491970›Full record

ArticlePLoS pathogens2015

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

Nai-Chi Chen, Masato Yoshimura, Hong-Hsiang Guan, Ting-Yu Wang, Yuko Misumi, Chien-Chih Lin, Phimonphan Chuankhayan, Atsushi Nakagawa, Sunney I Chan, Tomitake Tsukihara and 2 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
7.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

62 citing papers in PubMed, 143 citations in OpenAlex.

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2 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 3 countries.

Nai-Chi ChenInstitute of Biotechnology, National Cheng Kung University, Tainan, Taiwan; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, Taiwan.
Masato YoshimuraLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, Taiwan.
Hong-Hsiang GuanLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, Taiwan.
Ting-Yu WangInstitute of Biotechnology, National Cheng Kung University, Tainan, Taiwan.
Yuko MisumiInstitute for Protein Research, Osaka University, Suita, Osaka, Japan.
Chien-Chih LinLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, Taiwan.
Phimonphan ChuankhayanLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, Taiwan.
Atsushi NakagawaInstitute for Protein Research, Osaka University, Suita, Osaka, Japan.
Sunney I ChanInstitute of Chemistry, Academia Sinica, Taipei, Taiwan; Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California, United State of America.
Tomitake TsukiharaInstitute for Protein Research, Osaka University, Suita, Osaka, Japan; Picobiology Institute, Graduate School of Life Science, University of Hyogo, Kamigori, Hyogo, Japan.
Tzong-Yueh ChenInstitute of Biotechnology, National Cheng Kung University, Tainan, Taiwan.
Chun-Jung ChenInstitute of Biotechnology, National Cheng Kung University, Tainan, Taiwan; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, Taiwan; Department of Physics, National Tsing Hua University, Hsinchu, Taiwan; Center for Bioscience and Biotechnology, National Cheng Kung University, Tainan, Taiwan.
National Synchrotron Radiation Research Center · TWNational Cheng Kung University · TWCalifornia Institute of Technology · USOsaka University · JPProtein Research Foundation · JPUniversity of Hyogo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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 inter-subunit 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-P-domain 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 Ca2+ 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 P-domain during the crystallization process, enhances GNNV infection. The present structural studies together with the biological assays enhance our understanding of the role of the P-domain of GNNV in the capsid assembly and viral infection by this betanodavirus.

Indexed as

Virus AssemblyCalciumCapsid ProteinsCrystallography, X-RayNodaviridaePolyethylene GlycolsProtein Structure, TertiaryVirionCalciumCapsid ProteinsPolyethylene Glycols

Identifiers

PMID26491970
PMCPMC4619592
OpenAlexW2164391034

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.