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Surface antigens of Litomosoides carinii microfilariae: agglutinating antibodies react with sheath components of 40 and 120 kiloDalton molecular mass
Published online by Cambridge University Press: 06 April 2009
Summary
This study was conducted to identify surface antigens of the microfilarial sheath of Litomosoides carinii which are accessible to antibodies. Rabbit antisera were raised against the soluble and insoluble fractions of purified sheaths by extracting them with a buffer containing 2-mercaptoethanol and sodium dodecylsulphate. These sera and rabbit hyperimmune sera directed against homogenates of total microfilariae, mature (i.e. microfilariae liberating) female parasites and excretory–secretory products of adult females were able to agglutinate live and formaldehyde-fixed microfilariae. When the antisera directed against sheath constituents were administered to patently infected Mastomys coucha, the microfilaraemia of these animals was rapidly reduced and remained low for a period of 2–3 weeks. Antibodies specifically binding to the microfilarial surface were immunoaffinity-purified on formaldehyde-fixed microfilariae. The antibodies react with sheath antigens of 40 and 120 kDa molecular mass which are produced by the epithelium of the distal uterus of the mature female, secreted and attached to the surface of the sheaths. A 120 kDa antigen recognized by anti-sheath surface antibodies was also detected in the excretory–secretory products of in Vitro-cultured immature female L. carinii from day 30 post-infection onwards. In the excretory–secretory products of mature adult female parasites recovered on day 130 post-infection, this 120 kDa molecule was absent. However, material reacting with the antibody was detected in the stacking gel of SDS-polyacrylamide gels. This finding may indicate that the basic units forming the 120 kDa antigen of immature adults or microfilarial sheath surface antigens occur in a highly polymerized form in the excretory–secretory products of mature female parasites.
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- Copyright © Cambridge University Press 1994
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