Evidence map›Paper›PMID 20442276›Full record

ArticlePlant physiology2010

Binding properties of the N-acetylglucosamine and high-mannose N-glycan PP2-A1 phloem lectin in Arabidopsis.

Julie Beneteau, Denis Renard, Laurent Marché, Elise Douville, Laurence Lavenant, Yvan Rahbé, Didier Dupont, Françoise Vilaine, Sylvie Dinant

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
10.8field-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

44 citing papers in PubMed, 99 citations in OpenAlex.

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  15. The Characterization of theInternational journal of molecular sciences · 2022
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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

9 authors at 4 institutions in 1 country.

Julie BeneteauUR1268 Unité de Recherches Biopolymères Interactions Assemblages, INRA, F-44300 Nantes, France.
Denis Renard
Laurent Marché
Elise Douville
Laurence Lavenant
Yvan Rahbé
Didier Dupont
Françoise Vilaine
Sylvie Dinant
Institut Jean-Pierre Bourgin · FRAgroParisTech · FRBiopolymères Interactions Assemblages · FRBiologie Fonctionnelle Insectes et Interactions · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phloem Protein2 (PP2) is a component of the phloem protein bodies found in sieve elements. We describe here the lectin properties of the Arabidopsis (Arabidopsis thaliana) PP2-A1. Using a recombinant protein produced in Escherichia coli, we demonstrated binding to N-acetylglucosamine oligomers. Glycan array screening showed that PP2-A1 also bound to high-mannose N-glycans and 9-acyl-N-acetylneuraminic sialic acid. Fluorescence spectroscopy-based titration experiments revealed that PP2-A1 had two classes of binding site for N,N',N''-triacetylchitotriose, a low-affinity site and a high-affinity site, promoting the formation of protein dimers. A search for structural similarities revealed that PP2-A1 aligned with the Cbm4 and Cbm22-2 carbohydrate-binding modules, leading to the prediction of a beta-strand structure for its conserved domain. We investigated whether PP2-A1 interacted with phloem sap glycoproteins by first characterizing abundant Arabidopsis phloem sap proteins by liquid chromatography-tandem mass spectrometry. Then we demonstrated that PP2-A1 bound to several phloem sap proteins and that this binding was not completely abolished by glycosidase treatment. As many plant lectins have insecticidal activity, we also assessed the effect of PP2-A1 on weight gain and survival in aphids. Unlike other mannose-binding lectins, when added to an artificial diet, recombinant PP2-A1 had no insecticidal properties against Acyrthosiphon pisum and Myzus persicae. However, at mid-range concentrations, the protein affected weight gain in insect nymphs. These results indicate the presence in PP2-A1 of several carbohydrate-binding sites, with potentially different functions in the trafficking of endogenous proteins or in interactions with phloem-feeding insects.

Indexed as

AcetylglucosamineAmino Acid SequenceAnimalsAphidsArabidopsisArabidopsis ProteinsBinding SitesCarbohydrate SequenceChitinChromatography, AffinityHistidineMannoseMolecular Sequence DataN-Acetylneuraminic AcidOligopeptidesPlant ExudatesAcetylglucosamineArabidopsis ProteinsChitinHis-His-His-His-His-HisHistidineMannoseN-Acetylneuraminic AcidOligopeptidesphloem lectinPlant ExudatesPlant LectinsPolysaccharidesPP2-A1 protein, ArabidopsisRecombinant Fusion Proteins

Identifiers

PMID20442276
PMCPMC2899916
OpenAlexW2049453454

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.