Evidence map›Paper›PMID 19521795›Full record

ArticleMolecular biotechnology2009

cDNA cloning and functional expression of the alpha-D-galactose-binding lectin frutalin in Escherichia coli.

Carla Oliveira, Sofia Costa, José A Teixeira, Lucília Domingues

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Molecular biotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Expression of Lectins in Heterologous Systems.International journal of molecular sciences · 2018
    Review
  3. Article
  4. Frutapin, a lectin fromBioscience reports · 2017
    Article
  5. Anti-Neuroblastoma Properties of a Recombinant Sunflower Lectin.International journal of molecular sciences · 2017
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Lectins: production and practical applications.Applied microbiology and biotechnology · 2011
    Review
  15. Article
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

4 authors at 2 institutions in 1 country.

Carla OliveiraIBB-Institute for Biotechnology and Bioengineering, Centre of Biological Engineering, Universidade do Minho, Campus de Gualtar, 4710-057, Braga, Portugal.
Sofia Costa
José A Teixeira
Lucília Domingues
Institute for Biotechnology and Bioengineering · PTUniversity of Minho · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

cDNA clones encoding frutalin, the alpha-D-galactose-binding lectin expressed in breadfruit seeds (Artocarpus incisa), were isolated and sequenced. The deduced amino acid sequences indicated that frutalin may be encoded by a family of genes. The NCBI database searches revealed that the frutalin sequence is highly homologous with jacalin and mornigaG sequences. Frutalin cDNA was re-amplified and cloned into the commercial expression vector pET-25b(+) for frutalin production in Escherichia coli. An experimental factorial design was employed to maximise the soluble expression of the recombinant lectin. The results indicated that temperature, time of induction, concentration of IPTG and the interaction between the concentration of IPTG and the time of induction had the most significant effects on the soluble expression level of recombinant frutalin. The optimal culture conditions were as follows: induction with 1 mM IPTG at 22 degrees C for 20 h, yielding 16 mg/l of soluble recombinant frutalin. SDS-PAGE and Western blot analysis revealed that recombinant frutalin was successfully expressed by bacteria with the expected molecular weight (17 kDa). These analyses also showed that recombinant frutalin was mainly produced as insoluble protein. Recombinant frutalin produced by bacteria revealed agglutination properties and carbohydrate-binding specificity similar to the native breadfruit lectin.

Indexed as

Amino Acid SequenceArtocarpusCarbohydratesChromatography, GelCloning, MolecularData Interpretation, StatisticalDNA, ComplementaryEscherichia coliHemagglutination TestsIsopropyl ThiogalactosideMolecular Sequence DataPlant LectinsRecombinant ProteinsSequence AlignmentSolubilityTemperatureCarbohydratesDNA, ComplementaryIsopropyl ThiogalactosidePlant LectinsRecombinant Proteins

Identifiers

PMID19521795
OpenAlexW2135371359

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.