China Animal Husbandry & Veterinary Medicine ›› 2025, Vol. 52 ›› Issue (11): 5393-5402.doi: 10.16431/j.cnki.1671-7236.2025.11.034

• Preventive Veterinary Medicine • Previous Articles    

Bioinformatics Analysis and Polyclonal Antibody Preparation of Insulin-like Growth Factor 1 Receptor of Echinococcus granulosus sensu stricto

XIAYIDANMU Tuniyazi1,2, LIAO Xia1,2, LI Jing1,2, JIA Yutong1,2, ZHAO Jinlong1,2, DU Yun1,2, FANG Ziyi2,3, LIN Renyong2, LYU Guodong1,2   

  1. 1. College of Pharmacy, Xinjiang Medical University, Urumqi 830054, China;
    2. First Affiliated Hospital of Xinjiang Medical University, Urumqi 830054, China;
    3. College of Life Sciences and Technology, Xinjiang University, Urumqi 830054, China
  • Received:2025-04-10 Published:2025-10-30

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Abstract: 【Objective】 This study aimed to perform bioinformatics analysis on the insulin-like growth factor 1 receptor of Echinococcus granulosus sensu stricto (EgIGF-1R) protein,prepare polyclonal antibodies against EgIGF-1R,and locate its expression in the larval stage. 【Method】 ClustalW multiple alignment was performed on the amino acid sequences of EgIGF-1R (GenBank accession No.:XP_024354248.1) and its homologous genes using Mega 11.0 software,and the phylogenetic tree was constructed.The physicochemical characteristics,transmembrane regions,protein structure and other biological information of EgIGF-1R protein were analyzed by bioinformatics methods.The dominant peptide of EgIGF-1R was selected to immunize New Zealand White rabbits to prepare its polyclonal antibody,and the antibody titer was detected by ELISA method.The expression of EgIGF-1R in the protoscolex and vesicle stages of Echinococcus granulosus sensu stricto was precisely detected by immunohistochemistry and immunofluorescence assays. 【Result】 The amino acid sequence alignment results showed that EgIGF-1R shared 32.02% and 31.57% similarity with amino acid sequence of homologous genes of Schistosoma japonicum and Homo sapiens IGF-1R,respectively.The phylogenetic tree analysis results showed that EgIGF-1R was closely related to Echinococcus multilocularis, Fasciolopsis buski,and Schistosoma japonicum.The genetic relationship with species such as Homo sapiens and Mus musculus was relatively distant.Bioinformatics analysis results showed that EgIGF-1R protein contained 1 680 amino acids.The molecular weight of EgIGF-1R protein was 1.839×105 u,with an isoelectric point of 8.59.It had two transmembrane regions,located at amino acids 1 034-1 056 and 1 164-1 186,and was a transmembrane protein.It contained 18 tyrosine phosphorylation sites,123 serine phosphorylation sites,and 60 threonine phosphorylation sites.The proportions of alpha helix,beta sheet,and random coil in the secondary structure of EgIGF-1R protein were 21.19%,16.61%,and 62.20%,respectively.The N-terminus and C-terminus were far apart in 3D structure of EgIGF-1R protein.The docking fractions of EgIGF-1R with human insulin-like growth factor 1 and human insulin were －1 739.46 and －1 099.10 kJ/mol,respectively.The ELISA results showed that the titer of EgIGF-1R polyclonal antibody was 1∶64 000.The results of immunohistochemistry and immunofluorescence assays showed that EgIGF-1R was expressed in the rostrum,sucker and tegument of protoscolices and in the germinal layer of vesicles. 【Conclusion】 EgIGF-1R protein had structural domain that binded to human cytokines like IGF-1,and was expressed in the larval stages of Echinococcus granulosus sensu stricto,including the protoscolices and vesicles.The EgIGF-1R antibody prepared in this study provided a foundation for investigating the role of EgIGF-1R in the pathogenic mechanism of Echinococcus granulosus sensu stricto.

Key words: Echinococcus granulosus sensu stricto; insulin-like growth factor 1 receptor; bioinformatics analysis; polyclonal antibody

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