ORIGINAL RESEARCH article

Front. Cell. Infect. Microbiol.

Sec. Parasite and Host

Volume 15 - 2025 | doi: 10.3389/fcimb.2025.1560436

Screening and Identification of Protein 29 of Echinococcus granulosus (Eg.P29) Interacting Molecules

Provisionally accepted
Zailing  ShangZailing ShangFei  QiaoFei QiaoYaning  LiYaning LiXuelin  MaXuelin MaMingxia  WangMingxia WangWenji  YangWenji YangTianyu  HeTianyu HeHaixia  MaHaixia MaYana  WangYana Wang*
  • Ningxia Medical University, Yinchuan, China

The final, formatted version of the article will be published soon.

P29 has been reported to play an important role in protoscolex development in Echinococcus granulosus(E.granulosus). However, its specific roles and functions remain unclear. In this study, some basic information of Eg.P29 were obtained by bioinformatics software, it is a soluble cytoplasm protein containing a BAR domain and may play a role in actin polarity and endocytosis. Fifty Eg.P29-interacting molecules were screened using three immunoprecipitation-combined LC-MS/MS intersections. Cells transfected with the Eg.P29/pEGFP-C1 vector exhibited significantly altered morphology being small, round or oval, which were attributed to actin distribution changed. So, Eg.P29-interacting molecules were primarily actin and actin-related proteins, and seven molecules (ACTG1, ACTN4, VCL, LIMA1, FLNB, and MYH10) were screened using Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analyses, and their mRNA and protein levels were found to be significantly affected by Eg.P29. The yeast two-hybrid experiment revealed that VCL does not interact with Eg.P29, whereas the other molecules did. Finally, LIMA1 and actin were verified to interact with Eg.P29 by co-immunoprecipitation. Additionally, The seven molecules were all discovered their homologous protein in E.granulosus and formed a network of interacting protein. Due to Eg.actin had higher homologous with actin of human, furthermore Eg.P29 and Eg.actin had same histological location on rostellum, and suckers of the protoscolex, this supported the speculation of Eg.P29 interact with Eg.actin. Therefore, Eg.P29 collaborate with actin potentially affecting activity and development of protoscolex. These aspects warrant further in-depth study.

Keywords: P29 of Echinococcus granulosus, Immunoprecipitation, Mass Spectrometry, protein-protein interactions, Cytoskeleton

Received: 14 Jan 2025; Accepted: 04 Apr 2025.

Copyright: © 2025 Shang, Qiao, Li, Ma, Wang, Yang, He, Ma and Wang. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

* Correspondence: Yana Wang, Ningxia Medical University, Yinchuan, China

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