ABSTRACT
The induction of granuloma formation by soluble egg antigens (SEA) of Schistosoma mansoni is accompanied by T cell-mediated lymphokine production that regulates the intensity of the response. In the present study we have examined the ability of SDS-PAGE fractioned SEA proteins to elicit granulomas and lymphokine production in infected and egg-immunized mice. At the acute stage of infection SEA fractions (<21, 25-30, 32-38, 60-66, 70-90, 93-125, and > 200 kD) that elicited pulmonary granulomas also elicited IL-2, IL-4 lymphokine production. At the chronic stage a diminished number of fractions (60-66, 70-90, 93-125, and > 200 kD) were able to elicit granulomas with an overall decrease in IL-2, IL-4 production. Granulomas were elicited by larval-egg crossreactive and egg-specific fractions at both the acute and chronic stage of the infection. Examination of lymphokine production from egg-immunized mice demonstrated that as early as 4 days IL-2 was produced by spleen cells stimulated with <21, 32-38, 40-46, 93-125, and >200 kD fractions. By 16 days, IL-2production was envoked by 8 of 9 fractions. IL-4 production at 4 days in response to all fractions was minimal while at 16 days IL-4 was elicited with the < 21, 25-30, 50-56, 93-125, and > 200 kD fractions. The present study reveals differences in the range of SEA fractions able to elicit granulomas and IL-2, IL-4 production between acute and chronic stages of infection. Additionally, this study demonstrates sequential (IL-2 followed by IL-4) lymphokine production during the primary egg antigen response
Subject(s)
Antigens, Helminth , Granuloma , Ovum/analysis , Schistosoma mansoni/immunologyABSTRACT
La vitelogenina-vitelina (VG-VN) de Triatoma infestans es una glicolipoproteína con un peso molecular de 220 000, es una lipoproteína de alta densidad (1.18-1.2 gm/ml) con poca movilidad electroforética a pH 8.2. Hembras, machos, ninfas y huevos comparten numerosas proteínas pero ninguna de ellas es glicolipoproteica. La proteína común más importante posee un peso molecular de 43 000, es anódica y se encuentra a lo largo de todo el gradiente salino. Machos y hembras poseen una glicolipoproteína con una movilidad electroforética similar a l VG-VN, pero es una proteína de baja densidad. Otra VG-VN, catódica, no glicolipoproteica, se encuentra en huevos y hemolinfa de hembra. La VG-VN principal puede ser aislada por ultracentrifugación en gradiente de BrNa o por cromatografía en DEAE-celulosa. Varias especies dentro del género Triatoma demostraron identidad inmunológica entre sus VG-VN. Las hembras y los huevos de Panstrogylus megistus y las hembras, los huevos y los machos de Rhodnius prolixus poseen identidad inmunológica parcial con las VG-VN de T. infestans