Evidence map›Paper›PMID 33891967›Full record

ArticleBiochimie2021

Sialic acid removal by trans-sialidase modulates MMP-2 activity during Trypanosoma cruzi infection.

Daniel Musikant, Romina Higa, Cristina E Rodríguez, Martin M Edreira, Oscar Campetella, Alicia Jawerbaum, María S Leguizamón

Open access · hybridAbstract read
In one paragraph

Article in Biochimie, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. Frontiers in cellular and infection microbiology · 2024
    Article
  4. Article
  5. 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

7 authors at 4 institutions in 1 country.

Daniel MusikantDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Intendente Güiraldes 2160, C1428EGA, Ciudad de Buenos Aires, Argentina.
Romina HigaConsejo Nacional de Investigaciones Científicas y Técnicas, (CONICET) Godoy Cruz 2290, C1425FQB, Ciudad de Buenos Aires, Argentina; Laboratorio de Reproducción y Metabolismo, CEFYBO-CONICET, Facultad de Medicina, Universidad de Buenos Aires, Paraguay 2155 C1121ABG, Ciudad de Buenos Aires, Argentina.
Cristina E RodríguezDepartamento de Microbiología, IMPAM-CONICET, Facultad de Medicina, Universidad de Buenos Aires, Paraguay 2155 C1121ABG, Ciudad de Buenos Aires, Argentina.
Martin M EdreiraDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Intendente Güiraldes 2160, C1428EGA, Ciudad de Buenos Aires, Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas, (CONICET) Godoy Cruz 2290, C1425FQB, Ciudad de Buenos Aires, Argentina; Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales IQUIBICEN-CONICET, Universidad de Buenos Aires, Intendente Güiraldes 2160 C1428EGA, Ciudad de Buenos Aires, Argentina.
Oscar CampetellaConsejo Nacional de Investigaciones Científicas y Técnicas, (CONICET) Godoy Cruz 2290, C1425FQB, Ciudad de Buenos Aires, Argentina; Instituto de Investigaciones Biotecnológicas IIBio, Universidad Nacional de San Martín, 25 de Mayo y Francia B1650HMP, San Martín, San Martin, Argentina.
Alicia JawerbaumConsejo Nacional de Investigaciones Científicas y Técnicas, (CONICET) Godoy Cruz 2290, C1425FQB, Ciudad de Buenos Aires, Argentina; Laboratorio de Reproducción y Metabolismo, CEFYBO-CONICET, Facultad de Medicina, Universidad de Buenos Aires, Paraguay 2155 C1121ABG, Ciudad de Buenos Aires, Argentina.
María S LeguizamónConsejo Nacional de Investigaciones Científicas y Técnicas, (CONICET) Godoy Cruz 2290, C1425FQB, Ciudad de Buenos Aires, Argentina; Instituto de Investigaciones Biotecnológicas IIBio, Universidad Nacional de San Martín, 25 de Mayo y Francia B1650HMP, San Martín, San Martin, Argentina. Electronic address: sleguiza@unsam.edu.ar.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARNational University of General San Martín · ARUniversity of Buenos Aires · ARFundación Ciencias Exactas y Naturales · AR

Funding

Role in pathogenesis and parasite cell biology of the trans-sialidase from Trypanosoma cruzi, the agent of Chagas DiseaseR01AI104531 · NIAID · INSTITUTE/RESEARCH/BIOTECHNOLOGY FDN · PI CAMPETELLA, OSCAR EDUARDO · 2014 to 2023
$1.3M
NIAID NIH HHS R01 AI104531
6 · The paper itself

Abstract

Matrix metalloproteinases (MMPs) not only play a relevant role in homeostatic processes but are also involved in several pathological mechanisms associated with infectious diseases. As their clinical relevance in Chagas disease has recently been highlighted, we studied the modulation of circulating MMPs by Trypanosoma cruzi infection. We found that virulent parasites from Discrete Typing Units (DTU) VI induced higher proMMP-2 and MMP-2 activity in blood, whereas both low (DTU I) and high virulence parasites induced a significant decrease in proMMP-9 plasma activity. Moreover, trans-sialidase, a relevant T. cruzi virulence factor, is involved in MMP-2 activity modulation both in vivo and in vitro. It removes α2,3-linked sialyl residues from cell surface glycoconjugates, which then triggers the PKC/MEK/ERK signaling pathway. Additionally, bacterial sialidases specific for this sialyl residue linkage displayed similar MMP modulation profiles and triggered the same signaling pathways. This novel pathogenic mechanism, dependent on sialic acid removal by the neuraminidase activity of trans-sialidase, can be exploited by different pathogens expressing sialidases with similar specificity. Thus, here we present a new pathogen strategy through the regulation of the MMP network.

Indexed as

MAP Kinase Signaling SystemAnimalsChagas CardiomyopathyGlycoproteinsMaleMatrix Metalloproteinase 2MiceMice, Inbred BALB CN-Acetylneuraminic AcidNeuraminidaseProtozoan ProteinsTrypanosoma cruziGlycoproteinsMatrix Metalloproteinase 2Mmp2 protein, mouseN-Acetylneuraminic AcidNeuraminidaseProtozoan Proteinstrans-sialidaseChagas diseaseMatrix metalloproteinasesNeuraminic acidNeuraminidase

Identifiers

PMID33891967
PMCPMC8187320
OpenAlexW3153266197

What Socratic 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 Socratic graph.