Evidence map›Paper›PMID 24130823›Full record

ArticlePloS one2013

Maize root lectins mediate the interaction with Herbaspirillum seropedicae via N-acetyl glucosamine residues of lipopolysaccharides.

Eduardo Balsanelli, Thalita Regina Tuleski, Valter Antonio de Baura, Marshall Geoffrey Yates, Leda Satie Chubatsu, Fabio de Oliveira Pedrosa, Emanuel Maltempi de Souza, Rose Adele Monteiro

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

19 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Dual RNA-seq of maize andFrontiers in plant science · 2024
    Article
  4. Biotization ofFrontiers in plant science · 2023
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Transcriptional Responses ofFrontiers in microbiology · 2021
    Article
  10. Article
  11. Review
  12. Review
  13. Defining the Genetic Basis of Plant⁻Endophytic Bacteria Interactions.International journal of molecular sciences · 2019
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Lipopolysaccharides in diazotrophic bacteria.Frontiers in cellular and infection microbiology · 2014
    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.

Eduardo BalsanelliDepartment of Biochemistry and Molecular Biology, Universidade Federal do Paraná, Curitiba, Paraná, Brazil.
Thalita Regina Tuleski
Valter Antonio de Baura
Marshall Geoffrey Yates
Leda Satie Chubatsu
Fabio de Oliveira Pedrosa
Emanuel Maltempi de Souza
Rose Adele Monteiro
Universidade Federal do Paraná · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herbaspirillum seropedicae is a plant growth-promoting diazotrophic betaproteobacterium which associates with important crops, such as maize, wheat, rice and sugar-cane. We have previously reported that intact lipopolysaccharide (LPS) is required for H. seropedicae attachment and endophytic colonization of maize roots. In this study, we present evidence that the LPS biosynthesis gene waaL (codes for the O-antigen ligase) is induced during rhizosphere colonization by H. seropedicae. Furthermore a waaL mutant strain lacking the O-antigen portion of the LPS is severely impaired in colonization. Since N-acetyl glucosamine inhibits H. seropedicae attachment to maize roots, lectin-like proteins from maize roots (MRLs) were isolated and mass spectrometry (MS) analysis showed that MRL-1 and MRL-2 correspond to maize proteins with a jacalin-like lectin domain, while MRL-3 contains a B-chain lectin domain. These proteins showed agglutination activity against wild type H. seropedicae, but failed to agglutinate the waaL mutant strain. The agglutination reaction was severely diminished in the presence of N-acetyl glucosamine. Moreover addition of the MRL proteins as competitors in H. seropedicae attachment assays decreased 80-fold the adhesion of the wild type to maize roots. The results suggest that N-acetyl glucosamine residues of the LPS O-antigen bind to maize root lectins, an essential step for efficient bacterial attachment and colonization.

Indexed as

AcetylglucosamineHost-Pathogen InteractionsBacterial AdhesionBacterial ProteinsGene Expression Regulation, BacterialHerbaspirillumMutagenesisO AntigensPlant LectinsPlant RootsZea maysAcetylglucosamineBacterial ProteinsO AntigensPlant Lectins

Identifiers

PMID24130823
PMCPMC3793968
OpenAlexW2088804996

What OpenQuestion holds

Textmetadata
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.