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细粒棘球绦虫原头节中存在对人IgG1和IgG3具有特异性的Fc结合分子。

Fc-binding molecules specific for human IgG1 and IgG3 are present in Echinococcus granulosus protoscoleces.

作者信息

Baz A, Carol H, Marco M, Casabó L, Jones F, Dunne D, Nieto A

机构信息

Cátedra de Inmunologá, Casilla de Correos 1157, Facultad de Química, Facultad de Ciencias, Montevideo, Uruguay.

出版信息

Parasite Immunol. 1998 Sep;20(9):399-404. doi: 10.1046/j.1365-3024.1998.00147.x.

Abstract

In this work we describe the presence of Fc-binding activity on the suckers and tegument of E. granulosus protoscoleces. A fraction (PSA-Fc+) from protoscolex somatic antigens was isolated by affinity chromatography on human Fc-gamma1-Sepharose. Analysis by SDS-PAGE of PSA-Fc+ showed that it contained two major components. Using mouse F(ab')2-human Fc chimaeric monoclonal antibodies we verified that PSA-Fc+ bound mainly to human Fc-gamma1 and Fc-gamma3 isotypes. In addition, one of the components of PSA-Fc+ showed proteolytic activity. Both, Fc-binding and proteolytic activities localized on the protoscolex surface, may play a relevant role in the host-parasite interaction.

摘要

在本研究中,我们描述了细粒棘球绦虫原头蚴的吸盘和皮层上存在Fc结合活性。通过在人Fc-γ1-琼脂糖凝胶上进行亲和层析,从原头蚴体细胞抗原中分离出一个组分(PSA-Fc+)。对PSA-Fc+进行SDS-PAGE分析表明,它含有两个主要成分。使用小鼠F(ab')2-人Fc嵌合单克隆抗体,我们证实PSA-Fc+主要与人Fc-γ1和Fc-γ3同种型结合。此外,PSA-Fc+的一个成分显示出蛋白水解活性。位于原头蚴表面的Fc结合活性和蛋白水解活性可能在宿主-寄生虫相互作用中发挥重要作用。

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