Evidence map›Paper›PMID 27384541›Full record

ArticlePloS one2016

Temporizin and Temporizin-1 Peptides as Novel Candidates for Eliminating Trypanosoma cruzi.

André L A Souza, Robson X Faria, Kátia S Calabrese, Daiane J Hardoim, Noemi Taniwaki, Luiz A Alves, Salvatore G De Simone

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

10 citing papers in PubMed, 19 citations in OpenAlex.

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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 2 institutions in 1 country.

André L A SouzaFIOCRUZ, Center for Technological Development in Health (CDTS)/National Institute of Science and Technology for Innovation on Neglected Diseases (INCT-IDN), Rio de Janeiro, RJ, Brazil.
Robson X FariaFIOCRUZ, Oswaldo Cruz Institute, Laboratory of Toxoplasmosis and other Protozoosis, Rio de Janeiro, RJ, Brazil.
Kátia S CalabreseFIOCRUZ, Oswaldo Cruz Institute, Laboratory of Imunomodulation and Protozoology, Rio de Janeiro, RJ, Brazil.
Daiane J HardoimFIOCRUZ, Oswaldo Cruz Institute, Laboratory of Imunomodulation and Protozoology, Rio de Janeiro, RJ, Brazil.
Noemi TaniwakiFIOCRUZ, Adolfo Lutz Institute, Electronic Microscopy section, Araçatuba, São Paulo, SP, Brazil.
Luiz A AlvesFIOCRUZ, Oswaldo Cruz Institute, Laboratory of Cellular Communication, Rio de Janeiro, RJ, Brazil.
Salvatore G De SimoneFIOCRUZ, Center for Technological Development in Health (CDTS)/National Institute of Science and Technology for Innovation on Neglected Diseases (INCT-IDN), Rio de Janeiro, RJ, Brazil.
Fundação Oswaldo Cruz · BRUniversidade Federal Fluminense · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tropical diseases caused by parasitic infections continue to cause socioeconomic distress worldwide. Among these, Chagas disease has become a great concern because of globalization. Caused by Trypanosoma cruzi, there is an increasing need to discover new, more effective methods to manage infections that minimize disease onset. Antimicrobial peptides represent a possible solution to this challenge. As effector molecules of the innate immune response against pathogens, they are the first line of defense found in all multi-cellular organisms. In amphibians, temporins are a large family of antimicrobial peptides found in skin secretions. Their functional roles and modes of action present unique properties that indicate possible candidates for therapeutic applications. Here, we investigated the trypanocide activity of temporizin and temporizin-1. Temporizin is an artificial, hybrid peptide containing the N-terminal region of temporin A, the pore-forming region of gramicidin and a C-terminus consisting of alternating leucine and lysine. Temporizin-1 is a modification of temporizin with a reduction in the region responsible for insertion into membranes. Their activities were evaluated in a cell permeabilization assay by flow cytometry, an LDH release assay, electron microscopy, an MTT assay and patch clamp experiments. Both temporizin and temporizin-1 demonstrated toxicity against T. cruzi with temporizin displaying slightly more potency. At concentrations up to 100 μg/ ml, both peptides exhibited low toxicity in J774 cells, a macrophage lineage cell line, and no toxicity was observed in mouse primary peritoneal macrophages. In contrast, the peptides showed some toxicity in rat adenoma GH3 cells and Jurkat human lymphoma cells with temporizin-1 displaying lower toxicity. In summary, a shortened form of the hybrid temporizin peptide, temporizin-1, was efficient at killing T. cruzi and it has low toxicity in wild-type mammalian cells. These data suggest that temporizin-1 might be a candidate for Chagas disease therapy.

Indexed as

AnimalsAntimicrobial Cationic PeptidesCell ProliferationChagas DiseaseHEK293 CellsHumansJurkat CellsL-Lactate DehydrogenaseMacrophagesMaleMiceMicroscopy, ElectronPeptidesProteinsTrypanosoma cruziAntimicrobial Cationic PeptidesL-Lactate DehydrogenasePeptidesProteinstemporintemporizin-1 peptide

Identifiers

PMID27384541
PMCPMC4934777
OpenAlexW2472389655

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LicenceCC BY
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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.