Toxocara canis is one of the globally distributed soil-transmitted helminths, which causes ocular larva migrans and visceral larva migrans in humans. T. canis adapts to different microenvironments by resisting and/or adjusting various biological processes of hosts. Although definitive host can not extinguish T. canis infection, severe tissue damage is not found in definitive host. Knowledge about the molecular mechanism of T. canis-hosts interaction is limited. In the present study, the quantitative mass spectrometry-based data-independent acquisition (DIA) was implemented to investigate the proteomic alterations of Beagle dogs plasma from early to later T. canis infection stages. Parallel reaction monitoring (PRM) was used to validate the expressions of differentially expressed proteins. A total of 418, 414 and 411 plasma proteins were identified at 24 hpi, 96 hpi and 36 dpi, including 6, 5 and 23 differentially expressed proteins, respectively. At 24 hpi, the altered proteins, RARRES2, WDR1, moesin and filamin-A, may participate in pro-inflammatory reaction or promote larvae migration. At 96 hpi, the altered proteins, protein C and fibroleukin, may maintain the stability of the coagulation system to protect the lung. At 36 dpi, the alterations of C-reactive protein (CRP), ficolin (FCN), complement factor H-related protein 5 (CFHR5) and other complements can affect the 3 traditional complement system, including the classic pathway, lectin pathway and alternative pathway. These proteins may play an important roles in the interaction between T. canis and its definitive hosts. Further study on these altered proteins triggered by T. canis infection may discovery novel therapeutic or diagnostic targets for toxocariasis.