Evidence map›Paper›PMID 42340953›Full record

ArticlePLoS pathogens2026

Schistosoma japonicum histone acetyltransferase 1 (SjHAT1): A novel anti-schistosomal drug target.

Jing Xu, Yu-Xin Wang, Ping Huang, Ya-Nan Zhang, Huan Sun, Ting-Zheng Zhan, Chao-Ming Xia

Abstract read
In one paragraph

Article in PLoS pathogens, 2026. 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
–field-weighted citation impact
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

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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.

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

7 authors.

Jing XuDepartment of Parasitology, School of Basic Medical Sciences, Suzhou Medical College, Soochow University, Suzhou, Jiangsu, P. R. China.
Yu-Xin WangDepartment of Parasitology, School of Basic Medical Sciences, Suzhou Medical College, Soochow University, Suzhou, Jiangsu, P. R. China.
Ping HuangDepartment of Parasitology, School of Basic Medical Sciences, Suzhou Medical College, Soochow University, Suzhou, Jiangsu, P. R. China.
Ya-Nan ZhangExperimental Center of Suzhou Medical College, Soochow University, Suzhou, Jiangsu, P. R. China.
Huan SunThe Second Affiliated Hospital of Soochow University, Suzhou, Jiangsu, P. R. China.
Ting-Zheng ZhanKey Laboratory of Basic Research on Regional Diseases (Guangxi Medical University), Education Department of Guangxi Zhuang Autonomous Region, Nanning, Guangxi, P. R. China.
Chao-Ming XiaDepartment of Parasitology, School of Basic Medical Sciences, Suzhou Medical College, Soochow University, Suzhou, Jiangsu, P. R. China.ORCID https://orcid.org/0000-0003-3541-488X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Schistosomiasis remains a critical global health issue, necessitating novel therapies due to emerging praziquantel resistance. We previously developed a patented praziquantel derivative, DW-3-15, which demonstrated potent broad-spectrum schistosomicidal activity through SjHAT1 inhibition. Here, the full-length SjHAT1 cDNA is cloned by rapid amplification of cDNA ends methods. The protein encoded by the cDNA retains conserved catalytic residues of acetyltransferases although sharing 34% identity with mammalian orthologs. Enzyme activity analysis reveals that recombinant SjHAT1 exhibits 130 μU/mL histone acetyltransferase activity at 25°C for 60 min, and is completely inhibited by DW-3-15 at a concentration of 50 μM. However, DW-3-15 has no effect on the enzymatic activity of the human ortholog HAT1. Phylogenetic analyses place SjHAT1 in a distinct clade, and molecular docking results indicate significant divergence compared to its human ortholog HsHAT1. The expression profiling of SjHAT1 reveals stage- and sex-specific patterns. Fluorescence in situ hybridization localizes SjHAT1 predominantly in female vitellaria and male parenchyma near the gynecophoral canal. Knockdown of SjHAT1 reduces worm survival by 57.5% in vivo, suppresses female oviposition by 90.8% in vitro and 79.2% in vivo, and disrupts ovarian and vitelline architecture. RNA-sequencing analysis reveals that SjHAT1 knockdown disrupts β-alanyl-tryptamine (BATT) pheromone signaling via downregulation of aromatic L-amino acid decarboxylase (AADC) in males and multidrug resistance-associated protein 4 (MRP4) in females. Given that BATT is essential for inducing female sexual development and egg production, the observed transcriptional dysregulation provides mechanistic evidence for disrupted intersexual communication. Our findings identify that SjHAT1 is a central regulator of schistosome reproductive biology. These sex-specific mechanisms highlight SjHAT1 as a potential therapeutic target for treatment and control of schistosomiasis.

Indexed as

Helminth ProteinsHistone AcetyltransferasesSchistosoma japonicumSchistosomiasisSchistosomicidesAnimalsFemaleHumansMaleMicePhylogenyPraziquantelHelminth ProteinsHistone AcetyltransferasesPraziquantelSchistosomicides

Identifiers

PMID42340953
PMCPMC13293438

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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.