579 - 591 Cui J.pmd

Trichinella spiralis surface proteins are directly exposed to the host’s immune system, making them the main target antigens which induce the immune responses and may play an important role in the larval invasion and development process. The analysis and characterization of T. spiralis surface proteins could provide useful information to elucidate the host-parasite interaction, identify the early diagnostic antigens and the targets for vaccine. The purpose of this study was to identify the surface proteins of T. spiralis muscle larvae by two-dimensional gel electrophoresis (2-DE) Western-blot analysis and mass spectrometry. The 2-DE results showed that a total of approximately 33 proteins spots were detected with molecular weights varying from 10 to 66 kDa and isoelectric point (pI) from 4 to 7. Fourteen protein spots were recognized by sera of mice infected with T. spiralis at 42 dpi or at 18 dpi, and 12 spots were successfully identified by MALDI-TOF/TOF-MS, which represented 8 different proteins of T. spiralis. Out of the 8 T. spiralis proteins, 5 proteins (partial P49 antigen, deoxyribonuclease II family protein, two serine proteases, and serine proteinase) had catalytic and hydrolase activity, which might be the invasion-related proteins and the targets for vaccine. The 4 proteins (deoxyribonuclease II family protein, serine protease, 53 kDa ES antigen and hypothetical protein Tsp_08444) recognized by infection sera at 18 dpi might be the early diagnostic antigens for trichinellosis.