Evidence map›Paper›PMID 17715215›Full record

ArticleJournal of virology2007

Capsid protein-mediated recruitment of host DnaJ-like proteins is required for Potato virus Y infection in tobacco plants.

Daniel Hofius, Annette T Maier, Christof Dietrich, Isabel Jungkunz, Frederik Börnke, Edgar Maiss, Uwe Sonnewald

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
7.8field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 139 citations in OpenAlex.

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  17. Occurrence ofVirusdisease · 2022
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  19. The RyThe New phytologist · 2022
    Article
  20. Article

3 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

7 authors at 5 institutions in 2 countries.

Daniel HofiusCopenhagen Biocenter, University of Copenhagen, Ole Maaloes Vej 5, DK-2200 Copenhagen N, Denmark. hofius@my.molbio.ku.dk
Annette T Maier
Christof Dietrich
Isabel Jungkunz
Frederik Börnke
Edgar Maiss
Uwe Sonnewald
Friedrich-Alexander-Universität Erlangen-Nürnberg · DELeibniz Institute DSMZ – German Collection of Microorganisms and Cell Cultures · DELeibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung (IPK) · DELeibniz University Hannover · DEUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The capsid protein (CP) of potyviruses is required for various steps during plant infection, such as virion assembly, cell-to-cell movement, and long-distance transport. This suggests a series of compatible interactions with putative host factors which, however, are largely unknown. By using the yeast two-hybrid system the CP from Potato virus Y (PVY) was found to interact with a novel subset of DnaJ-like proteins from tobacco, designated NtCPIPs. Mutational analysis identified the CP core region, previously shown to be essential for virion formation and plasmodesmal trafficking, as the interacting domain. The ability of NtCPIP1 and NtCPIP2a to associate with PVY CP could be confirmed in vitro and was additionally verified in planta by bimolecular fluorescence complementation. The biological significance of the interaction was assayed by PVY infection of agroinfiltrated leaves and transgenic tobacco plants that expressed either full-length or J-domain-deficient variants of NtCPIPs. Transient expression of truncated dominant-interfering NtCPIP2a but not of the functional protein resulted in strongly reduced accumulation of PVY in the inoculated leaf. Consistently, stable overexpression of J-domain-deficient variants of NtCPIP1 and NtCPIP2a dramatically increased the virus resistance of various transgenic lines, indicating a critical role of functional NtCPIPs during PVY infection. The negative effect of impaired NtCPIP function on viral pathogenicity seemed to be the consequence of delayed cell-to-cell movement, as visualized by microprojectile bombardment with green fluorescent protein-tagged PVY. Therefore, we propose that NtCPIPs act as important susceptibility factors during PVY infection, possibly by recruiting heat shock protein 70 chaperones for viral assembly and/or cellular spread.

Indexed as

Amino Acid SequenceCapsidCapsid ProteinsDNA Mutational AnalysisGene DeletionHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular Sequence DataMutationNicotianaPlants, Genetically ModifiedPotyvirusProtein Structure, TertiarySequence Homology, Amino AcidTwo-Hybrid System TechniquesCapsid ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock Proteins

Identifiers

PMID17715215
PMCPMC2168797
OpenAlexW2134596856

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.