The S-layer homology domain as a means for anchoring heterologous proteins on the cell surface of Bacillus anthracis
The S-layer homology domain as a means for anchoring heterologous proteins on the cell surface of Bacillus anthracis
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DOI：
10.1046/j.1365-2672.1999.00880.x
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发表时间：
1999-08-01
影响因子：
4
通讯作者：
Fouet, A
中科院分区：
文献类型：
--
作者：
Mesnage, S;Tosi-Couture, E;Fouet, A
炭疽芽孢杆菌合成两个s层蛋白，每个蛋白在其氨基端都含有三个S-laver同源（SLH）基序。体外实验表明，每种蛋白的三个基序被组织成一个结构域，足以结合纯化的细胞壁。构建了与枯草芽胞杆菌左旋蔗糖酶融合的SLH结构域嵌合基因，并将其整合到染色体上。细胞分离和电镜研究表明，这两种异源多肽都靶向于细胞表面。此外，表面暴露的左旋蔗糖酶保留了它的酶和抗原特性。最后给出了本研究的初步应用结果。
Bacillus anthracis synthesizes two S-layer proteins, each containing three S-laver homology (SLH) motifs towards their amino-terminus. In vitro experiments suggested that the three motifs of-each protein were organized as a structural domain sufficient to bind purified cell walls. Chimeric genes encoding the SLH domains fused to the levansucrase of Bacillurs subtilis were constructed and integrated on the chromosome. Cell fractionation and electron microscopy studies showed that both heterologous polypeptides were targeted to the cell surface. In addition, surface-exposed levansucrase retained its enzymatic and antigenic properties. Preliminary, results concerning applications of this work are presented.