Evidence map›Paper›PMID 31511534›Full record

ArticleScientific reports2019

E40, a novel microbial protease efficiently detoxifying gluten proteins, for the dietary management of gluten intolerance.

Linda Cavaletti, Anna Taravella, Lucia Carrano, Giacomo Carenzi, Alessandro Sigurtà, Nicola Solinas, Salvatore De Caro, Luigia Di Stasio, Stefania Picascia, Mariavittoria Laezza and 3 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.9field-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

30 citing papers in PubMed, 57 citations in OpenAlex.

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  14. Iranian journal of biotechnology · 2023
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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

13 authors at 2 institutions in 1 country.

Linda CavalettiFondazione Istituto Insubrico di Ricerca per la Vita (FIIRV), Gerenzano, Varese, Italy.
Anna TaravellaFondazione Istituto Insubrico di Ricerca per la Vita (FIIRV), Gerenzano, Varese, Italy.
Lucia CarranoFondazione Istituto Insubrico di Ricerca per la Vita (FIIRV), Gerenzano, Varese, Italy.
Giacomo CarenziFondazione Istituto Insubrico di Ricerca per la Vita (FIIRV), Gerenzano, Varese, Italy.
Alessandro SigurtàFondazione Istituto Insubrico di Ricerca per la Vita (FIIRV), Gerenzano, Varese, Italy.
Nicola SolinasFondazione Istituto Insubrico di Ricerca per la Vita (FIIRV), Gerenzano, Varese, Italy.
Salvatore De CaroInstitute of Food Sciences, National Research Council, Avellino, Italy.
Luigia Di StasioInstitute of Food Sciences, National Research Council, Avellino, Italy.
Stefania PicasciaInstitute of Biochemistry and Cell Biology, National Research Council, Naples, Italy.
Mariavittoria LaezzaInstitute of Biochemistry and Cell Biology, National Research Council, Naples, Italy.
Riccardo TronconeDepartment of Translational Medical Science (Section of Pediatrics), and European Laboratory for the Investigation of Food-Induced Diseases, University "Federico II", Naples, Italy.
Carmen GianfraniInstitute of Biochemistry and Cell Biology, National Research Council, Naples, Italy. c.gianfrani@ibp.cnr.it.
Gianfranco MamoneInstitute of Food Sciences, National Research Council, Avellino, Italy.
National Research Council · ITInstitute of Food Science · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gluten proteins are the causative agent of Celiac Disease (CD), a life-long food intolerance characterized by an autoimmune enteropathy. Inadvertent gluten exposure is frequent even in celiac patients complying with a gluten-free diet, and the supplementation of exogenous gluten-digestive enzymes (glutenases) is indeed a promising approach to reduce the risk of dietary gluten boost. Here we describe Endopeptidase 40, a novel glutenase discovered as secreted protein from the soil actinomycete Actinoallomurus A8, and its recombinant active form produced by Streptomyces lividans TK24. E40 is resistant to pepsin and trypsin, and active in the acidic pH range 3 to 6. E40 efficiently degrades the most immunogenic 33-mer as well as the whole gliadin proteins, as demonstrated by SDS-PAGE, HPLC, LC-MS/MS, and ELISA. T lymphocytes from duodenal biopsies of celiac patients showed a strongly reduced or absent release of IFN-γ when exposed to gluten digested with E40. Data in gastrointestinal simulated conditions suggest that no toxic peptides are freed during gluten digestion by E40 into the stomach to enter the small intestine, thus counteracting the intestinal inflammatory cascade to occur in CD patients. E40 is proposed as a novel candidate in Oral Enzymatic Therapy for the dietary management of gluten toxicity.

Indexed as

ActinobacteriaBacterial ProteinsCeliac DiseaseChromatography, LiquidEndopeptidasesEnzyme-Linked Immunosorbent AssayFood IntoleranceGliadinGlutensHumansIntestine, SmallTandem Mass SpectrometryBacterial ProteinsEndopeptidasesGliadinGlutens

Identifiers

PMID31511534
PMCPMC6739405
OpenAlexW2972446408

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.