Evidence map›Paper›PMID 38163833›Full record

ArticleParasitology research2024

Influence of CK2 protein kinase activity on the interaction between Trypanosoma cruzi and its vertebrate and invertebrate hosts.

Joyce Eliza de Oliveira Souza, Shayane Martins Rodrigues Gomes, Ana Karina Castro Lima, Andréia Carolinne de Souza Brito, Silvia Amaral Gonçalves Da-Silva, Angela Hampshire de Carvalho Santos Lopes, Mário Alberto Cardoso Silva-Neto, Geórgia Correa Atella, Patricia Maria Lourenço Dutra

Abstract read
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In one paragraph

Article in Parasitology research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

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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 2 institutions in 1 country.

Joyce Eliza de Oliveira Souza *Discipline of Parasitology, Department of Microbiology, Immunology and Parasitology (FCM), State University of Rio de Janeiro, Rio de Janeiro, Brazil.
Shayane Martins Rodrigues Gomes *Discipline of Parasitology, Department of Microbiology, Immunology and Parasitology (FCM), State University of Rio de Janeiro, Rio de Janeiro, Brazil.
Ana Karina Castro LimaDiscipline of Parasitology, Department of Microbiology, Immunology and Parasitology (FCM), State University of Rio de Janeiro, Rio de Janeiro, Brazil.
Andréia Carolinne de Souza BritoDiscipline of Parasitology, Department of Microbiology, Immunology and Parasitology (FCM), State University of Rio de Janeiro, Rio de Janeiro, Brazil.
Silvia Amaral Gonçalves Da-SilvaDiscipline of Parasitology, Department of Microbiology, Immunology and Parasitology (FCM), State University of Rio de Janeiro, Rio de Janeiro, Brazil.
Angela Hampshire de Carvalho Santos LopesInstitute of Microbiology Paulo de Góes, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
Mário Alberto Cardoso Silva-NetoInstitute of Medical Biochemistry Leopoldo de Meis, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
Geórgia Correa AtellaInstitute of Medical Biochemistry Leopoldo de Meis, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
Patricia Maria Lourenço DutraDiscipline of Parasitology, Department of Microbiology, Immunology and Parasitology (FCM), State University of Rio de Janeiro, Rio de Janeiro, Brazil. pmldutra@gmail.com.
Universidade do Estado do Rio de Janeiro · BRUniversidade Federal do Rio de Janeiro · BR

Funding

Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro E-26/211.845/2021
6 · The paper itself

Abstract

Chagas disease, endemic from Latin America, is caused by Trypanosoma cruzi and is transmitted by triatomine feces. This parasite undergoes complex morphological changes through its life cycle, promoted by significant changes in signal transduction pathways. The activity of protein kinase CK2 has been described in trypanosomatids. Using a specific peptide and radioactive ATP, we identified CK2 activity on the cellular surface and the cytoplasmic content in Trypanosoma cruzi, apart from the secreted form. Dephosphorylated casein promoted an increase of 48% in the secreted CK2 activity. Total extract of peritoneal macrophages from BALB/c and inactivated human serum promoted an increase of 67% and 36%, respectively, in this activity. The protein secreted by parasites was purified by HPLC and had shown compatibility with the catalytic subunit of mammalian CK2. Incubation of the parasites with CK2 inhibitors, added to the culture medium, prevented their growth. The opposite was observed when CK2 activators were used. Results of interaction between Trypanosoma cruzi and the gut of the vector have revealed that, in the presence of CK2 inhibitors, there is a reduction in the association rate. A similar inhibition profile was seen in the Trypanosoma cruzi-macrophages interaction, confirming the importance of this enzyme in the life cycle of this protozoan.

Indexed as

Chagas DiseaseTrypanosoma cruziAnimalsCasein Kinase IIHumansInvertebratesMammalsCasein Kinase IICK2 activityHost-parasite interactionProtein kinasesTrypanosoma cruzi

Identifiers

PMID38163833
OpenAlexW4390499180

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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.