XXXX : immunoblot analysis of adult worm proteins.

@entity3208 @entity19 @entity281 @entity2975 @entity380
Proteins of adult @entity380 were separated by @entity3208 - @entity2975 gel electrophoresis and assayed in immunoblots for reactions with individual @entity19 sera. Four weeks after a heavy @entity281 with a few hundred cercariae, IgG antibodies directed predominantly against a protein of 31 kDa were detected. The protein was only weakly recognized by antibodies of @entity19 harboring a 4-week-old light @entity281 with about 60 cercariae. After 6 weeks or more, @entity19 infected with either dose formed antibodies, not only against the 31-kDa protein and a 67-kDa protein, but also against a number of other components. While reactions with the 31- and 67-kDa proteins occurred with sera of all individual @entity19 of four different strains, the reactions with other components were less consistently observed. @entity19 vaccinated with a heavy or light dose of 20,000-rad-irradiated cercariae did not form antibodies detectable in the blotting system. However, in immunofluorescence assays with living skin schistosomula, but not lung schistosomula, antibodies against the larval surface were detected with all sera obtained 4 weeks after @entity281 or vaccination. In addition, immunofluorescence studies using the same sera and sectioned adult parasites demonstrated the presence of antibodies against the parasite surface in all sera except those obtained from @entity19 exposed to a light @entity281 with normal cercariae. @entity19 infected in this latter way were the only animals that did not develop a significant resistance against a challenge @entity281 4 weeks after exposure to normal or irradiated cercariae. The presence of an immunofluorescent reaction against the schistosome gut always coincided with a reaction of the sera with the 31-kDa protein in the immunoblots. Although a role in immune resistance could not be ascribed to any of the proteins reacting in the immunoblots, the data demonstrate important differences in the antibody specificities induced by various @entity281 schemes.
