Payne D
Chemical and Biological Defence Establishment, Salisbury, Wiltshire, United Kingdom.
New Microbiol. 1994 Apr;17(2):99-110.
The K88 fimbrial adhesin is a major virulence determinant of certain strains of enterotoxigenic Escherichia coli (ETEC) that infect and colonise neonatal pigs. This study investigates the haemagglutination properties of all three serotypes (ab, ac and ad) with eleven erythrocyte species. Wide variation in the haemagglutination properties indicated differences in both the K88 receptor and adhesin structure. In particular, the receptor binding properties of E. coli serotype K88ad were significantly different from both K88ab and K88ac. K88-mediated haemagglutination was inhibited strongly by a range of glucosides, glucosamine, chondrosine and pig gastric mucin but only weakly by mamman and heparin. The most effective inhibitor was n-dodecyl-beta-D-glucopyranoside which prevented haemagglutination at a concentration of 0.72 mM. It is hypothesised that the potent inhibition observed with glucosides may be due to interference with hydrophobic interactions and is not necessarily specific.
K88菌毛黏附素是某些感染并定植于新生仔猪的产肠毒素大肠杆菌（ETEC）菌株的主要毒力决定因素。本研究调查了K88三种血清型（ab、ac和ad）与11种红细胞的血凝特性。血凝特性的广泛差异表明K88受体和黏附素结构均存在差异。特别是，大肠杆菌血清型K88ad的受体结合特性与K88ab和K88ac均有显著不同。一系列糖苷、氨基葡萄糖、软骨素和猪胃黏蛋白能强烈抑制K88介导的血凝，但甘露聚糖和肝素的抑制作用较弱。最有效的抑制剂是正十二烷基-β-D-吡喃葡萄糖苷，其在浓度为0.72 mM时可阻止血凝。据推测，糖苷产生的有效抑制作用可能是由于干扰了疏水相互作用，不一定具有特异性。
