Evidence map›Paper›PMID 37999896›Full record

ArticlePurinergic signalling2024

Heterologous expression and biochemical characterization of the recombinant nucleoside triphosphate diphosphohydrolase 2 (LbNTPDase2) from Leishmania (Viannia) braziliensis.

Nancy da Rocha Torres Pavione, João Victor Badaró de Moraes, Isadora Cunha Ribeiro, Raissa Barbosa de Castro, Walmir da Silva, Anna Cláudia Alves de Souza, Victor Hugo Ferraz da Silva, Raphael de Souza Vasconcellos, Gustavo da Costa Bressan, Juliana Lopes Rangel Fietto

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

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

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

10 authors at 1 institution in 1 country.

Nancy da Rocha Torres PavioneBiochemistry and Molecular Biology Department, Universidade Federal de Viçosa, Viçosa, MG, Brazil.ORCID https://orcid.org/0000-0002-3126-3343
João Victor Badaró de MoraesBiochemistry and Molecular Biology Department, Universidade Federal de Viçosa, Viçosa, MG, Brazil.ORCID https://orcid.org/0000-0002-2654-3252
Isadora Cunha RibeiroBiochemistry and Molecular Biology Department, Universidade Federal de Viçosa, Viçosa, MG, Brazil.ORCID https://orcid.org/0000-0003-1695-8080
Raissa Barbosa de CastroBiochemistry and Molecular Biology Department, Universidade Federal de Viçosa, Viçosa, MG, Brazil.ORCID https://orcid.org/0000-0002-9285-6740
Walmir da SilvaBiochemistry and Molecular Biology Department, Universidade Federal de Viçosa, Viçosa, MG, Brazil.ORCID https://orcid.org/0000-0003-3188-8076
Anna Cláudia Alves de SouzaBiochemistry and Molecular Biology Department, Universidade Federal de Viçosa, Viçosa, MG, Brazil.ORCID https://orcid.org/0000-0002-7341-2642
Victor Hugo Ferraz da SilvaBiochemistry and Molecular Biology Department, Universidade Federal de Viçosa, Viçosa, MG, Brazil.ORCID https://orcid.org/0000-0001-9344-1777
Raphael de Souza VasconcellosBiochemistry and Molecular Biology Department, Universidade Federal de Viçosa, Viçosa, MG, Brazil.ORCID https://orcid.org/0000-0002-5064-052X
Gustavo da Costa BressanBiochemistry and Molecular Biology Department, Universidade Federal de Viçosa, Viçosa, MG, Brazil.ORCID https://orcid.org/0000-0002-9741-4554
Juliana Lopes Rangel FiettoBiochemistry and Molecular Biology Department, Universidade Federal de Viçosa, Viçosa, MG, Brazil. jufietto@ufv.br.ORCID https://orcid.org/0000-0001-6122-1710
Universidade Federal de Viçosa · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leishmania braziliensis is a pathogenic protozoan parasite that causes American Tegumentary Leishmaniasis (ATL), an important tropical neglected disease. ENTPDases are nucleotidases that hydrolyze intracellular and/or extracellular nucleotides. ENTPDases are known as regulators of purinergic signalling induced by extracellular nucleotides. Leishmania species have two isoforms of ENTPDase, and, particularly, ENTPDase2 seems to be involved in infectivity and virulence. In this study, we conducted the heterologous expression and biochemical characterization of the recombinant ENTPDase2 of L. braziliensis (rLbNTPDase2). Our results show that this enzyme is a canonical ENTPDase with apyrase activity, capable of hydrolysing triphosphate and diphosphate nucleotides, and it is dependent on divalent cations (calcium or magnesium). Substrate specificity was characterized as UDP>GDP>ADP>GTP>ATP=UTP. The enzyme showed optimal activity at a neutral to basic pH and was partially inhibited by suramin and DIDS. Furthermore, the low apparent Km for ADP suggests that the enzyme may play a role in adenosine-mediated signalling. The biochemical characterization of this enzyme can open new avenues for using LbNTPDase2 as a drug target.

Indexed as

Leishmania braziliensisRecombinant ProteinsApyraseProtozoan ProteinsApyraseProtozoan ProteinsRecombinant ProteinsEnzyme characterizationLbNTPDase2Leishmania braziliensisRecombinant protein expression

Identifiers

PMID37999896
PMCPMC11377403
OpenAlexW4388974818

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Registered trials

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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.