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首页> 外文期刊>Infection and immunity >Identification and characterization of B-cell epitopes of IpaC, an invasion-associated protein of Shigella flexneri.
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Identification and characterization of B-cell epitopes of IpaC, an invasion-associated protein of Shigella flexneri.

机译：IpaC的B细胞表位的鉴定和表征，IpaC是弗氏志贺氏菌的入侵相关蛋白。

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摘要

Invasion plasmid antigen C (IpaC) is a 43-kDa plasmid-encoded protein associated with the ability of shigellae to invade epithelial cells. This protein is consistently strongly recognized by sera from convalescent patients and monkeys experimentally infected with shigellae. The strong immunogenicity of IpaC in the course of natural infection makes it a good candidate as a potentially protective antigen. To map the B-cell epitopes of this protein, the gene encoding IpaC was cloned and expressed at a high level in Escherichia coli. The partially purified recombinant protein was used to raise rabbit polyclonal antisera and murine monoclonal antibodies. A lambda gt11 ipaC gene library was screened with the antisera and antibodies. Recombinant DNA clones producing specific antigenic determinants were isolated, and the sequence of their DNA inserts was determined. The amino acid sequence of each determinant was deduced from the minimal overlap of DNA inserts of multiple antibody-positive DNA clones. Two distinct epitopes, located between amino acid residues 25 and 33 and 90 and 97, were identified. Two additional B-cell epitopes which were located between residues 297 and 349, near the carboxy-terminal end of the protein, were characterized. Each of these epitopes was also recognized by sera from convalescent humans and monkeys. Therefore, it seems likely that these epitopes are relevant to the humoral response against IpaC during natural infection.
机译：侵袭质粒抗原C（IpaC）是一种43 kDa质粒编码的蛋白，与志贺氏菌侵袭上皮细胞的能力有关。此蛋白始终被恢复期患者和实验感染志贺氏菌的猴子的血清强烈识别。 IpaC在自然感染过程中的强大免疫原性使其成为潜在保护性抗原的良好候选者。为了定位该蛋白的B细胞表位，克隆了编码IpaC的基因并在大肠杆菌中高水平表达。使用部分纯化的重组蛋白来产生兔多克隆抗血清和鼠单克隆抗体。使用抗血清和抗体筛选了gt11 ipaCλ基因文库。分离产生特异性抗原决定簇的重组DNA克隆，并确定其DNA插入片段的序列。从多个抗体阳性DNA克隆的DNA插入片段的最小重叠推导每个决定簇的氨基酸序列。鉴定出位于氨基酸残基25和33与90和97之间的两个不同的表位。表征了位于蛋白质的羧基末端附近的残基297和349之间的两个另外的B细胞表位。这些表位中的每一个也被恢复期人类和猴子的血清识别。因此，这些表位似乎与自然感染过程中针对IpaC的体液反应有关。

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