Evidence map›Paper›PMID 32703972›Full record

ArticleScientific reports2020

Der p 1-based immunotoxin as potential tool for the treatment of dust mite respiratory allergy.

Rodrigo Lázaro-Gorines, Juan Carlos López-Rodríguez, Sara Benedé, Miguel González, Cristobalina Mayorga, Lothar Vogel, Álvaro Martínez-Del-Pozo, Javier Lacadena, Mayte Villalba

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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

9 authors at 3 institutions in 2 countries.

Rodrigo Lázaro-GorinesBiochemistry and Molecular Biology Department, Chemical Sciences Faculty, Complutense University of Madrid, Av. Complutense w/n, 28040, Madrid, Spain.
Juan Carlos López-RodríguezBiochemistry and Molecular Biology Department, Chemical Sciences Faculty, Complutense University of Madrid, Av. Complutense w/n, 28040, Madrid, Spain.
Sara BenedéBiochemistry and Molecular Biology Department, Chemical Sciences Faculty, Complutense University of Madrid, Av. Complutense w/n, 28040, Madrid, Spain.
Miguel GonzálezAllergy Research Laboratory, IBIMA, Hospital Regional Universitario de Málaga, UMA, Málaga, Spain.
Cristobalina MayorgaAllergy Research Laboratory, IBIMA, Hospital Regional Universitario de Málaga, UMA, Málaga, Spain.
Lothar VogelDivision of Allergology, Paul-Ehrlich-Institut, Langen, Germany.
Álvaro Martínez-Del-PozoBiochemistry and Molecular Biology Department, Chemical Sciences Faculty, Complutense University of Madrid, Av. Complutense w/n, 28040, Madrid, Spain.
Javier LacadenaBiochemistry and Molecular Biology Department, Chemical Sciences Faculty, Complutense University of Madrid, Av. Complutense w/n, 28040, Madrid, Spain. jlacadena@quim.ucm.es.
Mayte VillalbaBiochemistry and Molecular Biology Department, Chemical Sciences Faculty, Complutense University of Madrid, Av. Complutense w/n, 28040, Madrid, Spain. mvillalb@ucm.es.
Universidad Complutense de Madrid · ESInstituto de Investigación Biomédica de Málaga · ESPaul Ehrlich Institut · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Immunotoxins appear as promising therapeutic molecules, alternative to allergen-specific-immunotherapy. In this work, we achieved the development of a protein chimera able to promote specific cell death on effector cells involved in the allergic reaction. Der p 1 allergen was chosen as cell-targeting domain and the powerful ribotoxin α-sarcin as the toxic moiety. The resultant construction, named proDerp1αS, was produced and purified from the yeast Pichia pastoris. Der p 1-protease activity and α-sarcin ribonucleolytic action were effectively conserved in proDerp1αS. Immunotoxin impact was assayed by using effector cells sensitized with house dust mite-allergic sera. Cell degranulation and death, triggered by proDerp1αS, was exclusively observed on Der p 1 sera sensitized-humRBL-2H3 cells, but not when treated with non-allergic sera. Most notably, equivalent IgE-binding and degranulation were observed with both proDerp1αS construct and native Der p 1 when using purified basophils from sensitized patients. However, proDerp1αS did not cause any cytotoxic effect on these cells, apparently due to its lack of internalization after their surface IgE-binding, showing the complex in vivo panorama governing allergic reactions. In conclusion, herein we present proDerp1αS as a proof of concept for a potential and alternative new designs of therapeutic tools for allergies. Development of new, and more specific, second-generation of immunotoxins following proDerp1αS, is further discussed.

Indexed as

AllergensAnimalsAntigens, DermatophagoidesArthropod ProteinsBasophilsCell DegranulationCell LineCells, CulturedCysteine EndopeptidasesDermatophagoides pteronyssinusDesensitization, ImmunologicHumansHypersensitivityImmunoglobulin EImmunotoxinsRecombinant ProteinsAllergensAntigens, DermatophagoidesArthropod ProteinsCysteine EndopeptidasesDermatophagoides pteronyssinus antigen p 1Immunoglobulin EImmunotoxinsRecombinant Proteins

Identifiers

PMID32703972
PMCPMC7378242
OpenAlexW3044748352

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.