INTRODUCTION: Eg.P29 is a specific protein of METHODS: Some basic information about Eg.P29 through bioinformatics software. A total of 50 molecules interacting with Eg.P29 were screened by three immunoprecipitation-combined liquid chromatography-tandem mass spectrometry intersections. The RESULTS: Eg.P29 is a soluble cytoplasmic protein containing a BAR structural domain that may play a role in actin polarity and endocytosis. Cells in the Eg.P29 group showed marked morphological changes in the form of rounded, or oval shapes, which were attributed to changes in actin distribution. Seven molecules interacting with Eg.P29 were mainly actin and actin-related proteins (ACTG1, ACTN4, VCL, ARPC1A, LIMA1, FLNB and MYH10), and their mRNA and protein levels were significantly affected by Eg.P29. Yeast two-hybridization experiments showed that VCL did not interact with Eg.P29, whereas the other molecules interacted with Eg.P29. The interaction of LIMA1 and actin with Eg.P29 was verified by co-immunoprecipitation. Additionally, Eg.P29 and Eg.actin had the same histological location on rostellum, and suckers of the protoscolex. Additionally, the seven molecules were all discovered their homologous proteins in DISCUSSION: In this study, we confirmed LIMA1 and actin were Eg.P29-interacting molecules, they were forming a compound regulation system to affect cytoskeleton formation. And we also deduced that Eg.P29 interacts with Eg.actin in