Paramyosin has been proposed as a vaccine candidate in schistosomiasis and filariasis. However, limited information is available about its protective potential against cysticercosis and the immune response it induces. Immunization of mice with recombinant full-length paramyosin of Taenia solium (TPmy) results in about a 52% reduction in parasite burden after a subsequent challenge by intraperitoneal inoculation of Taenia crassiceps cysticerci. Immunization assays using recombinant fragments of TPmy, corresponding approximately to thirds on the amino, central, or carboxyl regions, suggest that protective epitopes are located mostly in the amino-end third. Proliferation assays using T cells obtained from mice immunized with the full-length recombinant TPmy also showed a preferential response to the amino-terminal fragment. In contrast, antibodies in the sera from these mice predominantly recognize epitopes located in the carboxyl-terminal fragment, being the immunoglobulin G1 subclass, the predominant antibody isotype. Characterization of the cellular immune response induced against the protective amino-terminal fragment reveals production of gamma interferon and interleukin-2, but not interleukin-4, suggesting a Th1-like profile.Paramyosin (Pmy) is a filamentous, ␣-helical, coiled-coil protein of about 100 kDa, present in some muscles of invertebrates. It is also an antigen during infections by several flatworms that are important parasites of humans and of domestic animals such as Schistosoma mansoni (10), Schistosoma japonicum (4), Taenia solium (10, 12), and Echinococcus granulosus (18). The paramyosin of T. solium (TPmy) is present in the musculature but has also been found associated with the tegument of the parasite (7). The collagen-binding and complement-inhibitory properties of TPmy have been described previously (8, 9, 11). TPmy is synthesized by the tegumentary cytons and apparently released through the cyst tegument (8). Furthermore, TPmy can be collected in the culture medium in which T. solium cysts are maintained (8), suggesting that a similar release to the host tissues might occur in vivo and that TPmy may modulate the host response through diminution of the inflammatory mediators at the host-parasite interface (8,11).Paramyosins have been proposed as vaccine candidates in a number of helminthiases including schistosomiasis (3, 20) and filariasis (14,19). Despite their protective abilities against schistosomiasis and filariasis, limited information is available on their potential as vaccines against cysticercosis. Here we report that immunization of mice with recombinant fragments of TPmy induces significant levels of protection in the murine model of cysticercosis by Taenia crassiceps. The profile of cytokine production suggests that the protective amino-terminal fragment of TPmy induces a Th1-like immune response. MATERIALS AND METHODSAnimal model. Mice used in all experiments were 4-to 6-week-old female BALB/c AnN strain mice. The ORF strain of T. crassiceps was maintained by consecutive passa...

Taenia solium paramyosin is an immunodominant antigen in human and porcine cysticercosis that has shown promise as a vaccine candidate against schistosomiasis and some filariasis. There are few studies to identify the immunologically relevant regions of paramyosin. In this work, we characterize the humoral and cellular response of neurocysticercotic patients against T. solium paramyosin. Western blots using different recombinant fragments of T. solium paramyosin, showed that the sera from neurocysticercotic patients were strongly reactive against the carboxyl end region, with poor recognition of the central and amino regions. In contrast, the cellular immune response of patients did not show preferential recognition of any region of paramyosin.