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利用与大肠杆菌LamB蛋白的融合物对克氏锥虫免疫显性抗原中的B细胞表位进行定位

Mapping of B cell epitopes in an immunodominant antigen of Trypanosoma cruzi using fusions to the Escherichia coli LamB protein.

作者信息

Pereira C M, Yamauchi L M, Levin M J, da Silveira J F, Castilho B A

机构信息

Departamento de Microbiologia, Imunologia e Parasitologia, Escola Paulista de Medicina, UNIFESP, São Paulo, Brazil.

出版信息

FEMS Microbiol Lett. 1998 Jul 1;164(1):125-31. doi: 10.1111/j.1574-6968.1998.tb13077.x.

Abstract

The JL8 protein antigen from Trypanosoma cruzi, a dominant immunogen in man, has been characterized as containing tandem amino acid repeats. Here, we describe the use of the LamB protein of Escherichia coli as a carrier of JL8 derived sequences in order to map the immunodominant B cell epitopes in this antigen. Five different sequences of JL8 were inserted in the LamB protein and the JL8-LamB fusion proteins were tested by ELISA with human chronic chagasic sera. The fusion carrying the sequence AEKQKAAEATKVAE was recognized by most sera. This protein was also capable of inhibiting the binding of human chagasic antibodies to GST-JL8 in competitive ELISA suggesting that it contains an immunodominant B cell epitope of JL8.

摘要

来自克氏锥虫的JL8蛋白抗原是人类的主要免疫原,其特征是含有串联氨基酸重复序列。在此,我们描述了使用大肠杆菌的LamB蛋白作为JL8衍生序列的载体,以便绘制该抗原中免疫显性B细胞表位。将五种不同的JL8序列插入LamB蛋白中,并用人类慢性恰加斯病血清通过ELISA检测JL8-LamB融合蛋白。携带序列AEKQKAAEATKVAE的融合蛋白被大多数血清识别。该蛋白在竞争性ELISA中也能够抑制人类恰加斯病抗体与GST-JL8的结合,表明它含有JL8的免疫显性B细胞表位。

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