Evidence map›Paper›PMID 32698828›Full record

ArticleParasites & vectors2020

The role of the Acanthamoeba castellanii Sir2-like protein in the growth and encystation of Acanthamoeba.

So-Young Joo, Ja Moon Aung, Minsang Shin, Eun-Kyung Moon, Hyun-Hee Kong, Youn-Kyoung Goo, Dong-Il Chung, Yeonchul Hong

Open access · goldAbstract read
In one paragraph

Article in Parasites & vectors, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  5. Encystment and Excystment Processes inPathogens (Basel, Switzerland) · 2025
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  9. Biological characteristics and pathogenicity ofFrontiers in microbiology · 2023
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  12. Curcumin effect onPeerJ · 2022
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  14. Stimulation ofFrontiers in cell and developmental biology · 2022
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  15. 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

8 authors at 3 institutions in 1 country.

So-Young JooDepartment of Parasitology and Tropical Medicine, School of Medicine, Kyungpook National University, Daegu, Republic of Korea.
Ja Moon AungDepartment of Parasitology and Tropical Medicine, School of Medicine, Kyungpook National University, Daegu, Republic of Korea.
Minsang ShinDepartment of Microbiology, School of Medicine, Kyungpook National University, Daegu, Republic of Korea.
Eun-Kyung MoonDepartment of Medical Zoology, Kyung Hee University School of Medicine, Seoul, Republic of Korea.
Hyun-Hee KongDepartment of Parasitology, Dong-A University College of Medicine, Busan, Republic of Korea.
Youn-Kyoung GooDepartment of Parasitology and Tropical Medicine, School of Medicine, Kyungpook National University, Daegu, Republic of Korea.
Dong-Il ChungDepartment of Parasitology and Tropical Medicine, School of Medicine, Kyungpook National University, Daegu, Republic of Korea.
Yeonchul HongDepartment of Parasitology and Tropical Medicine, School of Medicine, Kyungpook National University, Daegu, Republic of Korea. ychong@knu.ac.kr.
Kyungpook National University · KRDong-A University · KRKyung Hee University Medical Center · KR

Funding

National Research Foundation of Korea (KR) NRF-2019R1A2C1004177
6 · The paper itself

Abstract

backgroundThe encystation of Acanthamoeba leads to the development of resilient cysts from vegetative trophozoites. This process is essential for the survival of parasites under unfavorable conditions. Previous studies have reported that, during the encystation of A. castellanii, the expression levels of encystation-related factors are upregulated. However, the regulatory mechanisms for their expression during the encystation process remains unknown. Proteins in the sirtuin family, which consists of nicotinamide adenine dinucleotide-dependent deacetylases, are known to play an important role in various cellular functions. In the present study, we identified the Acanthamoeba silent-information regulator 2-like protein (AcSir2) and examined its role in the growth and encystation of Acanthamoeba.

methodsWe obtained the full-length sequence for AcSir2 using reverse-transcription polymerase chain reaction. In Acanthamoeba transfectants that constitutively overexpress AcSir2 protein, SIRT deacetylase activity was measured, and the intracellular localization of AcSir2 and the effects on the growth and encystation of trophozoites were examined. In addition, the sirtuin inhibitor salermide was used to determine whether these effects were caused by AcSir2 overexpression

resultsAcSir2 was classified as a class-IV sirtuin. AcSir2 exhibited functional SIRT deacetylase activity, localized mainly in the nucleus, and its transcription was upregulated during encystation. In trophozoites, AcSir2 overexpression led to greater cell growth, and this growth was inhibited by treatment with salermide, a sirtuin inhibitor. When AcSir2 was overexpressed in the cysts, the encystation rate was significantly higher; this was also reversed with salermide treatment. In AcSir2-overexpressing encysting cells, the transcription of cellulose synthase was highly upregulated compared with that of control cells, and this upregulation was abolished with salermide treatment. Transmission electron microscope-based ultrastructural analysis of salermide-treated encysting cells showed that the structure of the exocyst wall and intercyst space was impaired and that the endocyst wall had not formed.

conclusionsThese results indicate that AcSir2 is a SIRT deacetylase that plays an essential role as a regulator of a variety of cellular processes and that the regulation of AcSir2 expression is important for the growth and encystation of A. castellanii.

Indexed as

Acanthamoeba castellaniiParasite EncystmentSirtuinsAmebiasisAnimalsGenes, ProtozoanGlucosyltransferasesHistone DeacetylasesHumansNaphtholsPhenylpropionatesPhylogenyProtozoan ProteinsTransfectionTrophozoitescellulose synthaseGlucosyltransferasesHistone DeacetylasesN-(3-((2-hydroxynaphthalen-1-ylmethylene)amino)phenyl)-2-phenylpropionamideNaphtholsPhenylpropionatesProtozoan ProteinsSirtuinsAcanthamoeba castellaniiEncystationSalermideSirtuin-like protein

Identifiers

PMID32698828
PMCPMC7376869
OpenAlexW3044093106

What OpenQuestion holds

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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.