Evidence map›Paper›PMID 18480444›Full record

ArticleJournal of virology2008

Mutational analysis of plant cap-binding protein eIF4E reveals key amino acids involved in biochemical functions and potyvirus infection.

Sylvie German-Retana, Jocelyne Walter, Bénédicte Doublet, Geneviève Roudet-Tavert, Valérie Nicaise, Cécile Lecampion, Marie-Christine Houvenaghel, Christophe Robaglia, Thierry Michon, Olivier Le Gall

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
6.9field-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

36 citing papers in PubMed, 75 citations in OpenAlex.

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  15. Structural studies of the eIF4E-VPg complex reveal a direct competition for capped RNA: Implications for translation.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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

10 authors at 4 institutions in 2 countries.

Sylvie German-RetanaInteractions Plante-Virus, UMR GDPP 1090, INRA Université de Bordeaux 2, BP 81, F-33883 Villenave d'Ornon Cedex, France. german@bordeaux.inra.fr
Jocelyne Walter
Bénédicte Doublet
Geneviève Roudet-Tavert
Valérie Nicaise
Cécile Lecampion
Marie-Christine Houvenaghel
Christophe Robaglia
Thierry Michon
Olivier Le Gall
Université de Bordeaux · FRAix-Marseille Université · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRJohn Innes Centre · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The eukaryotic translation initiation factor 4E (eIF4E) (the cap-binding protein) is involved in natural resistance against several potyviruses in plants. In lettuce, the recessive resistance genes mo1(1) and mo1(2) against Lettuce mosaic virus (LMV) are alleles coding for forms of eIF4E unable, or less effective, to support virus accumulation. A recombinant LMV expressing the eIF4E of a susceptible lettuce variety from its genome was able to produce symptoms in mo1(1) or mo1(2) varieties. In order to identify the eIF4E amino acid residues necessary for viral infection, we constructed recombinant LMV expressing eIF4E with point mutations affecting various amino acids and compared the abilities of these eIF4E mutants to complement LMV infection in resistant plants. Three types of mutations were produced in order to affect different biochemical functions of eIF4E: cap binding, eIF4G binding, and putative interaction with other virus or host proteins. Several mutations severely reduced the ability of eIF4E to complement LMV accumulation in a resistant host and impeded essential eIF4E functions in yeast. However, the ability of eIF4E to bind a cap analogue or to fully interact with eIF4G appeared unlinked to LMV infection. In addition to providing a functional mutational map of a plant eIF4E, this suggests that the role of eIF4E in the LMV cycle might be distinct from its physiological function in cellular mRNA translation.

Indexed as

Immunity, InnateAmino Acid SequenceAmino Acid SubstitutionDNA Mutational AnalysisEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GGenetic Complementation TestLactucaModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutation, MissensePlant DiseasesPlant ProteinsPoint MutationPotyvirusEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GPlant ProteinsRNA Caps

Identifiers

PMID18480444
PMCPMC2493313
OpenAlexW2101357267

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.