Characterization of a purified glycoprotein from Schistosoma mansoni eggs: specificity, stability, and the involvement of carbohydrate and peptide moieties in its serologic activity.

摘要: A major egg glycoprotein (MEG) was purified from a crude soluble extract of Schistosoma mansoni ova (Egyptian strain) by successive steps lectin affinity and ion-exchange chromatography. Radioiodinated MEG exhibited single precipitation band upon immunodiffusion against antiserum chronically infected mice, ran as on PAGE (Rf 0.38) SDS-PAGE 0.36). Its estimated m.w. 70,000. The degree stage species specificity the effect various treatments its serologic reactivity were determined radioimmunoassay (RIA). low cross-reactivity between similarly prepared antigens adult worms cercariae demonstrated RIA inhibition tests, whereas high found S. haematobium antigen. In similar Puerto Rican had lower with than Egyptian strain. four times more abundant in SEA strain stable to heat at 100 degrees C for 60 min, 0.1 N NaOH or HCl, 10% TCA. Treatment pronase caused limited fragmentation molecule some loss reactivity. Periodate oxidation resulted substantial molecular mass reactivity, leaving residual activity that is only partially cross-reactive bulk MEG. These results suggest importance both carbohydrate peptide moieties