Hansson L, Wallbrandt P, Andersson J O, Byström M, Bäckman A, Carlstein A, Enquist K, Lönn H, Otter C, Strömqvist M
Symbicom AB, Umeå, Sweden.
Biochim Biophys Acta. 1995 Jun 9;1244(2-3):377-83. doi: 10.1016/0304-4165(95)00028-a.
The adherence of pyelonephritic Escherichia coli isolates to mammalian host cells is mediated by the P-pili structures on the bacterial surface. The protein constituting the distal part of the pili structure, papG, interacts with glycan receptors on the host cell. Variation in specificity for different glycoconjugates between the isolates, that may reflect variation in host tropism, has been correlated to three different classes of papG. Truncated variants of the class I, II and III papG adhesins were produced as fusion protein in E. coli and analysed for carbohydrate binding. The results showed that both carbohydrate binding and specificity of the papG adhesin resided in a linear part of the N-terminus of the protein.
肾盂肾炎大肠杆菌分离株对哺乳动物宿主细胞的黏附是由细菌表面的P菌毛结构介导的。构成菌毛结构远端部分的蛋白质papG与宿主细胞上的聚糖受体相互作用。分离株之间对不同糖缀合物的特异性差异可能反映宿主嗜性的差异，这与三种不同类型的papG相关。I类、II类和III类papG黏附素的截短变体在大肠杆菌中作为融合蛋白产生，并分析其碳水化合物结合情况。结果表明，papG黏附素的碳水化合物结合和特异性都存在于该蛋白质N端的一个线性区域。
