Evidence map›Paper›PMID 41530293›Full record

ArticleScientific reports2026

Crystal structure of Echinococcus multilocularis cystatin B reveals a novel feature in classical stefins.

Wenbin Hong, Zhe Cheng, Zhijian Xu, Shukun Zhong, Xianshu Liu, Nouhoum Dibo, Ziyi Dai, Yuzhou Lin, Wenchang Lai, HuaRui Jia and 2 more

Abstract read
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In one paragraph

Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

12 authors.

Wenbin Hong *Department of Medical Parasitology, Xiangya School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Zhe Cheng *State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen, Fujian, China.
Zhijian Xu *State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen, Fujian, China.
Shukun ZhongDepartment of Medical Parasitology, Xiangya School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Xianshu LiuDepartment of Medical Parasitology, Xiangya School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Nouhoum DiboDepartment of Medical Parasitology, Xiangya School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Ziyi DaiDepartment of Medical Parasitology, Xiangya School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China.
Yuzhou LinState Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen, Fujian, China.
Wenchang LaiState Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University, Xiamen, Fujian, China.
HuaRui JiaPingdingshan Polytechnic College, Pingdingshan, Henan, China.
Xiaomin ShangDepartment of Medical Parasitology, Xiangya School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China. xmshang@csu.edu.cn.
Shuaiqin HuangDepartment of Medical Parasitology, Xiangya School of Basic Medical Sciences, Central South University, Changsha, 410013, Hunan, China. sqhuang@csu.edu.cn.

Funding

National Natural Science Foundation of China 32200450National Natural Science Foundation of China 82102428National Natural Science Foundation of China 82272365Natural Science Foundation of Hunan Province 2022JJ40663
6 · The paper itself

Abstract

Alveolar echinococcosis (AE), caused by the metacestode larval of Echinococcus multilocularis, is one of the most lethal helminthic diseases in humans. Current treatment options, such as albendazole, are limited in their efficacy, highlighting the need for a deeper understanding of the parasite-host interaction to identify new therapeutic targets. One promising area of research involves helminth-derived cystatins, which are known to modulate host immune responses to facilitate parasite survival. A cystatin homologue from E. multilocularis (EmCystatin-B) was identified and analyzed. EmCystatin-B was cloned, expressed and purified. Its expression patterns were evaluated by western blot, qPCR and Immunohistochemistry The EmCystatin-B structure was solved by X-ray crystallography. EmCystatin-B was expressed in the mature protoscoleces as well as in the cytosol and nucleus of the metacestode vesicles. Moverover, EmCystatin-B adopts a conserved typical cystatin fold, but also exhibits unique structural features. Notably, a novel feature characterized by two intermolecular disulfide bridges between Cys4 in a EmCystatin-B molecular and Cys76 in adjacent molecule was discovered. Further investigation demonstrated this distinctive feature appears to be involved in the oligomerization of EmCystatin-B, facilitating a monomer-dimer-tetramer assembly pathway. The crystal structure of EmCystatin-B reveals a novel feature in classical stefins, and provides species-specific insights into the sequence, structure, and functional characteristics of EmCystatin-B.

Indexed as

Cystatin BEchinococcus multilocularisHelminth ProteinsAmino Acid SequenceAnimalsCloning, MolecularCrystallography, X-RayModels, MolecularProtein ConformationCystatin BHelminth ProteinsCrystal structureCystatin BDisulfide bridgesEchinococcus multilocularisOligomerization

Identifiers

PMID41530293
PMCPMC12877014

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