Objective To compare the differences in exosomes derived from testicular tissue between WT (wild type) mice and sdy mice with dysbindin-1 (dystrobrevin binding protein 1) deletion mutations, and identify their protein components to explore the possible role of dysbindin-1 in the formation of exosomes derived from mouse testicular tissue.    Methods The exosomes derived from mouse testicular tissue of WT and sdy mice were isolated by sucrose ultracentrifugation method. The expression of exosomes proteins was analyzed by Western blotting, the morphology of exosomes was observed by negative staining under transmission electron microscope(TEM), the particle size and distribution were analyzed by dynamic light scattering particle size analyzer, and the protein contents of exosomes were detected by mass spectrometry analysis. CD63+ exosomes were obtained by immunoprecipitation with magnetic beads. Krt5 (keratin5) protein was selected for validation.    Results Dysbindin-1 deletion did not affect the morphology and quantity of exosomes, but decreased the expression of CD63, a marker of exosomes. Compared with the WT mice, there were 159 proteins that were highly expressed, 209 proteins that were lowly expressed, and 184 proteins that were specifically expressed in the exosomes derived from sdy mice testicular tissue. In this experiment, CD63+ exosomes from testicular tissue were obtained and 12 proteins were screened. There was indeed an interaction between krt5 protein and dysbindin-1. Interestingly, it was found that the expression of krt5 in the exosomes derived from sdy mice testicular tissue decreased after dysbindin-1 deletion.    Conclusion After dysbindin-1 deletion, the morphology and quantity of exosomes derived from mouse testicular tissue are not affected, but dysbindin-1 may affect the types and content of exosomal proteins, by affecting the transport of exosome proteins through protein interactions.