Characterization of FimH adhesins expressed by Salmonella enterica serovar Gallinarum biovars Gallinarum and Pullorum:: Reconstitution of mannose-binding properties by single amino acid substitution
Characterization of FimH adhesins expressed by Salmonella enterica serovar Gallinarum biovars Gallinarum and Pullorum:: Reconstitution of mannose-binding properties by single amino acid substitution
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DOI：
10.1128/iai.73.9.6187-6190.2005
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发表时间：
2005-09-01
影响因子：
3.1
通讯作者：
Ugorski, M
中科院分区：
文献类型：
--
作者：
Kisiela, D;Sapeta, A;Ugorski, M
与大肠沙门氏菌血清型鼠伤寒沙门氏菌相比，鸡痢沙门氏菌和鸡痢沙门氏菌的I型菌毛的重组FimH粘附素不与高甘露寡糖结合，也不与人结肠癌HT-29细胞结合。然而，来自Gallinarum生物变种和Pullorum生物变种的突变的FimH蛋白，其中78位的异亮氨酸被在S. enterica serovar Typhimurium中发现的苏氨酸取代，与携带高甘露糖低聚糖的糖蛋白和结肠癌细胞结合良好。生物变种Gallinarum和生物变种Pullorum的FimH粘附素是I型菌毛的一部分，它们的糖结合特性的丧失很可能是单个T78I突变的结果，FimH蛋白的定点诱变已经证明了这一点。
Recombinant FimH adhesins of type I fimbriae from Salmonella enterica serovar Gallinarum biovars Gallinarum and Pullorum, in contrast to those of Salmonella enterica serovar Typhimurium, did not bind to high-mannose oligosaccharides or to human colon carcinoma HT-29 cells. However, mutated FimH proteins from biovar Gallinarum and biovar Pullorum, in which the isoleucine at position 78 was replaced by the threonine found in S. enterica serovar Typhimurium, bound well to glycoproteins carrying high-mannose oligosaccharides and colon carcinoma cells. The loss of sugar-binding properties by biovar Gallinarum and biovar Pullorum FimH adhesins, which are a part of the type I fimbriae, is most probably the result of a single T78I mutation, as was proven by site-directed mutagenesis of FimH proteins.