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L.A. WINGER N. TIRAWANCHAI J. NICHOLAS H.E. CARTER J.E. SMITH R.E. SINDEN 《Parasite immunology》1988,10(2):193-207
Zygotes and ookinetes of the rodent malaria Plasmodium berghei can be enriched 50-fold, from whole blood cultures by ammonium chloride lysis. Three monoclonal antibodies (MoAbs) raised against such enriched preparations specifically bind to a determinant of Mr 21 kD as assessed by 125I-labelled goat anti-mouse IgG probed immunoblots of Western transfers of SDS-PAGE gels. Indirect immunofluorescence indicates that the 21 kD determinant bound by specific MoAbs, whilst not detectable on gametocytes or gametes, appears on the parasite surface within 2 h of exflagellation/fertilization and increases thereafter. The three MoAbs specifically binding the 21 kD determinant block oocyst development in mosquitoes by at least 90%, as assessed either by in-vitro membrane feeds or by live feeds on passively immunized mice. These MoAbs reduce ookinete formation in vitro by between 52 and 100%. Possible mechanisms of action of these MoAbs are discussed. 相似文献
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Summary Two-site and competitive ELISA have been developed against a surface antigen of zygotes-ookinetes of Plasmodium berghei using monoclonal antibodies (MoAbs) which block transmission of the parasite to the mosquito. Three such MoAbs have been studied, each of which recognized a protein of an Mr 21 kD (Pbs21) using immunoblot techniques. The assays showed that there are at least 3 single B-cell epitopes expressed in Pbs21. One epitope recognized by MoAb 17.9 is conformation dependent and antibodies bound to it interfered with other MoAbs (12.1 and 13.1) each recognizing a different, apparently linear epitope. Glycosylation might not be relevant to the binding of any of the antibodies tested to their respective epitopes. 相似文献
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