Evidence map›Paper›PMID 34028659›Full record

ArticleBiotechnology letters2021

Expression of recombinant protease MarP from Mycobacterium tuberculosis in Pichia pastoris and its effect on human monocytes.

Gerardo García-González, Jorge Ángel Ascacio-Martínez, Romel Hernández-Bello, Gloria María González, José Prisco Palma-Nicolás

Open access · hybridAbstract read
PubMed Publisher
In one paragraph

Article in Biotechnology letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. Microbial proteases and their applications.Frontiers in microbiology · 2023
    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

5 authors at 1 institution in 1 country.

Gerardo García-GonzálezDepartamento de Microbiología, Facultad de Medicina y Hospital Universitario "Dr. José Eleuterio González", Universidad Autónoma de Nuevo León, Ave. Francisoco I. Madero y Dr. Eduardo Aguirre Pequeño s/n, Col. Mitras Centro, C.P. 64460, Monterrey, Nuevo León, Mexico.
Jorge Ángel Ascacio-MartínezDepartamento de Bioquímica y medicina molecular, Facultad de Medicina y Hospital Universitario "Dr. José Eleuterio González", Universidad Autónoma de Nuevo León, Monterrey, Nuevo León, Mexico.
Romel Hernández-BelloDepartamento de Microbiología, Facultad de Medicina y Hospital Universitario "Dr. José Eleuterio González", Universidad Autónoma de Nuevo León, Ave. Francisoco I. Madero y Dr. Eduardo Aguirre Pequeño s/n, Col. Mitras Centro, C.P. 64460, Monterrey, Nuevo León, Mexico.
Gloria María GonzálezDepartamento de Microbiología, Facultad de Medicina y Hospital Universitario "Dr. José Eleuterio González", Universidad Autónoma de Nuevo León, Ave. Francisoco I. Madero y Dr. Eduardo Aguirre Pequeño s/n, Col. Mitras Centro, C.P. 64460, Monterrey, Nuevo León, Mexico.
José Prisco Palma-NicolásDepartamento de Microbiología, Facultad de Medicina y Hospital Universitario "Dr. José Eleuterio González", Universidad Autónoma de Nuevo León, Ave. Francisoco I. Madero y Dr. Eduardo Aguirre Pequeño s/n, Col. Mitras Centro, C.P. 64460, Monterrey, Nuevo León, Mexico. jose.palman@uanl.mx.ORCID http://orcid.org/0000-0003-3508-9941
Universidad Autónoma de Nuevo León · MX

Funding

Consejo Nacional de Ciencia y Tecnología 238125
6 · The paper itself

Abstract

objectiveMycobacterial acid-resistant protease (MarP) is a membrane-associated serine protease involved in the survival of Mycobacterium tuberculosis in macrophages; here we produced MarP in the yeast Pichia pastoris and study its involvement in macrophage immune modulation.

resultsPichia pastoris vectors, harboring a full-length or a partial sequence of MarP, were constructed. GS115 clones were selected, and homologous recombination at the AOX1 locus was assessed by PCR. Protein was purified by nickel affinity chromatography, and its effect on the cytokine profile was tested in human monocytes. Only the partial MarP protein (121-397 a.a.) lacking the transmembrane domain was successfully expressed as an N-glycosylated proteolytically active protease. In vitro stimulation of THP-1 cells with MarP promoted the release of TNF-α and IL-10.

conclusionMycobacterial MarP was successfully expressed in P. pastoris, and it is capable of cytokine release in vitro.

Indexed as

Aldehyde OxidaseBacterial ProteinsChromatography, AffinityFungal ProteinsGene Expression RegulationHomologous RecombinationHumansInterleukin-10MonocytesMycobacterium tuberculosisPichiaProtein DomainsProtein EngineeringSerine ProteasesTHP-1 CellsTumor Necrosis Factor-alphaAldehyde OxidaseBacterial ProteinsFungal ProteinsIL10 protein, humanInterleukin-10Serine ProteasesTNF protein, humanTumor Necrosis Factor-alphaMarPMonocytesMycobacterium tuberculosisPichia pastorisRecombinant proteins

Identifiers

PMID34028659
OpenAlexW3164455707

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.