Evidence map›Paper›PMID 39232817›Full record

ArticleParasites & vectors2024

Anti-Toxoplasma gondii effects of XYP1-derived peptides and regulatory mechanisms of XYP1.

Jing Li, Kaijuan Wu, Xiaohua Liu, Dongqian Yang, Jing Xie, Yixiao Wang, Kang Liu, Zheng Wang, Wei Liu, Liping Jiang

Abstract read
In one paragraph

Article in Parasites & vectors, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

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

3 citing papers in PubMed.

  1. A novel anti-Microbiology spectrum · 2026
    Article
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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

10 authors.

Jing Li *Department of Parasitology, School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Kaijuan Wu *Department of Parasitology, School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Xiaohua LiuDepartment of Parasitology, School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Dongqian YangDepartment of Parasitology, School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Jing XieDepartment of Parasitology, School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Yixiao WangDepartment of Parasitology, School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Kang LiuDepartment of Parasitology, School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Zheng WangDepartment of Vascular Surgery, The Third Xiangya Hospital, Central South University, Changsha, 410013, Hunan, China.
Wei LiuHunan Key Laboratory of Traditional Chinese Veterinary Medicine, Hunan Agricultural University, Changsha, 410128, China.
Liping JiangDepartment of Parasitology, School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China. jiangliping@csu.edu.cn.

Funding

Hunan graduate research innovation project QL20230021National Natural Science Foundation of China 32170510
6 · The paper itself

Abstract

backgroundToxoplasmosis, caused by Toxoplasma gondii , poses serious health issues for humans and animals. Individuals with impaired immune systems are more susceptible to severe toxoplasmosis. Pregnant women infected by T. gondii can face the possibility of birth defects and miscarriages. While pyrimethamine and sulfadiazine are commonly used drugs in clinical practice, concerns over their side effects and resistance are on the rise. A spider peptide XYP1 isolated from Lycosa coelestis had potent anti-T. gondii effects, but it had a high synthesis cost and strong cytotoxicity.

methodsThis study intended to modify XYP1 for producing derived peptides via amino acid truncation and substitution. The anti-T. gondii effect was evaluated by trypan blue staining assay and killing experiment of RH strain tachyzoites. The CCK8 and hemolysis assays were used to compare their safeties. The morphological changes of T. gondii were observed by scanning electron microscope and transmission electron microscope. In addition, the mechanism of XYP1 against T. gondii through RNA-sequencing was further explored.

resultsIn vivo and in vitro experiments revealed that XYP1-18 and XYP1-18-1 had excellent anti-T. gondii activity with lower cytotoxicity and hemolysis activity than XYP1. XYP1, XYP1-18, and XYP1-18-1 were able to disrupt the surface membrane integrity of T. gondii tachyzoites, forming pores and causing the disruption of organelles. Furthermore, RNA-sequencing analysis indicated that XYP1 could stimulate the host immune response to effectively eliminate T. gondii and lessen the host's inflammatory reaction.

conclusionsXYP1-18 had lower cytotoxicity and hemolysis activity than XYP1, as well as significantly extending the survival time of the mice. XYP1 played a role in host inflammation and immune responses, revealing its potential mechanism. Our research provided valuable insights into the development and application of peptide-based drugs, offering novel strategies and directions for treating toxoplasmosis.

Indexed as

ToxoplasmaAnimalsAntiprotozoal AgentsFemaleHemolysisHumansMicePeptidesToxoplasmosisAntiprotozoal AgentsPeptidesAnti-Toxoplasma gondii activityToxoplasmosisTranscriptome analysisXYP1-derived peptides

Identifiers

PMID39232817
PMCPMC11373213

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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.