Schryvers A B
Department of Microbiology and Infectious Diseases, University of Calgary, Alberta, Canada.
Mol Microbiol. 1988 Jul;2(4):467-72. doi: 10.1111/j.1365-2958.1988.tb00052.x.
The expression of human transferrin and lactoferrin binding activity in Haemophilus influenzae, detected by a binding assay using human transferrin or lactoferrin conjugated to peroxidase, was regulated by the level of available iron in the medium. Transferrin binding activity was present in all H. influenzae isolates tested but not detected in other Haemophilus species or in species of Pasteurella or Actinobacillus. Lactoferrin binding activity was only detected in 1/15 H. influenzae isolates tested. The transferrin and lactoferrin receptors were shown to be specific for the respective human proteins by means of a competition binding assay. Competition binding assays also showed that iron-loaded transferrin was more effective at blocking the transferrin receptor than apotransferrin, but no differences in receptor blocking were observed between iron-loaded lactoferrin and apolactoferrin.
通过使用与过氧化物酶偶联的人转铁蛋白或乳铁蛋白的结合试验检测，流感嗜血杆菌中人转铁蛋白和乳铁蛋白结合活性的表达受培养基中可利用铁水平的调节。在所测试的所有流感嗜血杆菌分离株中均存在转铁蛋白结合活性，但在其他嗜血杆菌属物种或巴斯德菌属或放线杆菌属物种中未检测到。仅在1/15所测试的流感嗜血杆菌分离株中检测到乳铁蛋白结合活性。通过竞争结合试验表明，转铁蛋白和乳铁蛋白受体对各自的人蛋白质具有特异性。竞争结合试验还表明，铁负载的转铁蛋白比脱铁转铁蛋白更有效地阻断转铁蛋白受体，但在铁负载的乳铁蛋白和脱铁乳铁蛋白之间未观察到受体阻断的差异。
