Hofstra H, Dankert J
J Gen Microbiol. 1979 Apr;111(2):293-302. doi: 10.1099/00221287-111-2-293.
The protein constituents in the outer membrane (OM) of several serotypes of Escherichia coli and some other Enterobacteriaceae cross-reacted antigenically. Solubilized OM preparations of these bacteria were applied in interfacial precipitin tests to antisera elicited in rabbits against whole bacterial cells, absorbed with their appropriate lipopolysaccharide before testing. The resulting immunecomplexes were analysed on polyacrylamide gels. Protein profiles of the immunoprecipitates showed a considerable antigenic cross-reactivity of outer membrane proteins between most E. coli serotypes. Cross-reactivity, though substantially lower, was also found with OM from three other Enterobacteriaceae species, but was not detectable with Pseudomonas aeruginosa OM. When OM preparations were solubilized at room temperature, the peptidoglycan-bound proteins in the molecular weight range 37,000 to 41,000 predominated in the protein profiles of the immunecomplexes. In profiles of immunecomplexes obtained with boiled OM preparations, a heat-modifiable protein (mol. wt 33,000) predominated. The major OM proteins of the Gram-negative bacterium may therefore play a role as common surface antigens of the family of Enterobacteriaceae.
几种血清型大肠杆菌及其他一些肠杆菌科细菌外膜（OM）中的蛋白质成分存在抗原交叉反应。将这些细菌的可溶性外膜制剂用于界面沉淀试验，检测对象是用全菌细胞免疫家兔所得的抗血清，检测前用相应的脂多糖进行吸收处理。所得免疫复合物在聚丙烯酰胺凝胶上进行分析。免疫沉淀物的蛋白质图谱显示，大多数大肠杆菌血清型之间的外膜蛋白存在相当程度的抗原交叉反应。虽然交叉反应程度低得多，但在其他三种肠杆菌科细菌的外膜中也发现了交叉反应，而铜绿假单胞菌的外膜则未检测到交叉反应。当外膜制剂在室温下溶解时，分子量在37000至41000之间与肽聚糖结合的蛋白质在免疫复合物的蛋白质图谱中占主导地位。在用煮沸的外膜制剂获得的免疫复合物图谱中，一种热可变蛋白（分子量33000）占主导地位。因此，革兰氏阴性菌的主要外膜蛋白可能作为肠杆菌科的共同表面抗原发挥作用。
