Evidence map›Paper›PMID 21917973›Full record

ArticleJournal of virology2011

The interaction between bamboo mosaic virus replication protein and coat protein is critical for virus movement in plant hosts.

Cheng-Cheng Lee, Yuan-Ning Ho, Rei-Hsing Hu, Yu-Ting Yen, Zheng-Cheng Wang, Ya-Chien Lee, Yau-Heiu Hsu, Menghsiao Meng

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
6.6field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  9. Systematic Characterization of the Group 2 House Dust Mite Allergen inFrontiers in cellular and infection microbiology · 2021
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  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Host Factors in the Infection Cycle ofFrontiers in microbiology · 2017
    Review
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

8 authors at 1 institution in 1 country.

Cheng-Cheng LeeGraduate Institute of Biotechnology, National Chung Hsing University, 250 Kuo-Kuang Rd., Taichung, Taiwan 40227, Republic of China.
Yuan-Ning Ho
Rei-Hsing Hu
Yu-Ting Yen
Zheng-Cheng Wang
Ya-Chien Lee
Yau-Heiu Hsu
Menghsiao Meng
National Chung Hsing University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bamboo mosaic virus (BaMV) is a positive-sense RNA virus belonging to the genus Potexvirus. Open reading frame 1 (ORF1) encodes the viral replication protein that consists of a capping enzyme domain, a helicase-like domain (HLD), and an RNA-dependent RNA polymerase domain from the N to C terminus. ORF5 encodes the viral coat protein (CP) required for genome encapsidation and the virus movement in plants. In this study, application of a yeast-two hybrid assay detected an interaction between the viral HLD and CP. However, the interaction did not affect the NTPase activity of the HLD. To identify the critical amino acids of CP interacting with the HLD, a random mutational library of CP was created using error-prone PCR, and the mutations adversely affecting the interaction were screened by a bacterial two-hybrid system. As a result, the mutations A209G and N210S in CP were found to weaken the interaction. To determine the significance of the interaction, the mutations were introduced into a BaMV infectious clone, and the mutational effects on viral replication, movement, and genome encapsidation were investigated. There was no effect on accumulations of BaMV CP and genomic RNAs within protoplasts; however, the virus cell-to-cell movement in plants was restricted. Sequence alignment revealed that A209 of BaMV CP is conserved in many potexviruses. Mutation of the corresponding residue in Foxtail mosaic virus CP also reduced the viral HLD-CP interaction and restricted the virus movement, suggesting that interaction between CP and a widely conserved HLD in the potexviral replication protein is crucial for viral trafficking through plasmodesmata.

Indexed as

Protein Interaction MappingAmino Acid SequenceCapsid ProteinsDNA Mutational AnalysisMolecular Sequence DataMutant ProteinsPlant DiseasesPotexvirusRNA-Dependent RNA PolymeraseSequence AlignmentTwo-Hybrid System TechniquesCapsid ProteinsMutant ProteinsRNA-Dependent RNA Polymerase

Identifiers

PMID21917973
PMCPMC3209275
OpenAlexW2102389525

What OpenQuestion holds

Textmetadata
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.