Schistosoma mansoni shares a protective carbohydrate epitope with keyhole limpet hemocyanin.

Schistosoma mansoni shares a protective carbohydrate epitope with keyhole limpet hemocyanin.
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DOI:
10.1084/jem.165.3.865
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发表时间:
1987-03-01
期刊:
The Journal of experimental medicine
影响因子:
--
通讯作者:
Capron A
Capron A
中科院分区:
其他
文献类型:
--
作者:
Grzych JM;Dissous C;Capron M;Torres S;Lambert PH;Capron A

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由IPLSm 1保护性mAb定义的38,000 Mr曼氏血吸虫童虫主要免疫原的聚糖表位在海洋软体动物Megathura crenulata的血蓝蛋白中鉴定,更好地称为KLH。利用该抗原社区进一步研究该表位的生物学特性。KLH显示出强烈抑制IPLSm 1 mAb与其38,000 Mr靶抗原的结合。用KLH免疫LOU大鼠,可诱导抗S抗体的产生.能够免疫沉淀38,000 Mrmansoni抗体。抗KLH抗体介导了显著的嗜酸性粒细胞依赖性细胞毒作用,并被动地将免疫力转移至链球菌.曼氏感染。最后,用KLH免疫的大鼠对S.曼氏尾蚴。KLH的去糖基化完全消除了其免疫学和功能性KLH特性,表明天然KLH的寡糖表位也被S.感染曼氏菌的病人这些观察结果提供了获得可能用于血吸虫病免疫预防和血清流行病学的聚糖表位的明确结构的新机会,以及针对化学定义明确的表位的同种型反应的新方法。
The glycanic epitope of the 38,000 Mr Schistosoma mansoni schistosomula major immunogen defined by the IPLSm1 protective mAb was identified in the hemocyanin of the marine mollusc Megathura crenulata, better known as KLH. This antigenic community was exploited to investigate further the biological properties of this epitope. KLH was shown to strongly inhibit the binding of IPLSm1 mAb to its 38,000 Mr target antigen. Immunization of naive LOU rats with KLH elicited the production of anti- S. mansoni antibodies capable of immunoprecipitating the 38,000 Mr schistosomulum antigen. Antibodies to KLH mediated a marked eosinophil- dependent cytotoxicity and passively transferred immunity towards S. mansoni infection. Finally, rats immunized with KLH were significantly protected against a challenge with S. mansoni cercariae. The deglycosylation of KLH completely abolishes its immunological and functional KLH properties, indicating the participation of an oligosaccharidic epitope of the native KLH that is also recognized by the sera of S. mansoni-infected patients. These observations provide new opportunities of access to the well-defined structure of a glycanic epitope potentially available for the immunoprophylaxis and seroepidemiology of schistosomiasis, and a new approach to the isotypic response towards a well-chemically defined epitope.