Engleberg N C, Pearlman E, Dixon D, Eisenstein B I
J Immunol. 1986 Feb 15;136(4):1415-7.
We studied the antigenic cross-reactivity of surface proteins among various strains of Legionella pneumophila and other Legionella species by using a novel method of antibody purification. Anti-bacterial antibodies in hyperimmune sera were adsorbed to and eluted from the surface of recombinant E. coli cells that express individual L. pneumophila antigens on their surface. These affinity-purified antibodies were then used to probe protein immunoblots prepared from the test strains to detect cross-reactive domains. We found that antigenic proteins are generally conserved in all L. pneumophila serogroups. Although some of these antigenic domains are shared with members of other Legionella species, they are associated with proteins of different molecular mass. Our approach to the study of antigenic cross-reactivity has potential advantages over similar studies that use either monoclonal antibodies or monospecific antibodies prepared by immunization with purified antigens.
我们采用一种新型抗体纯化方法，研究了嗜肺军团菌各菌株及其他军团菌属细菌表面蛋白的抗原交叉反应性。超免疫血清中的抗菌抗体吸附于表达单个嗜肺军团菌抗原的重组大肠杆菌细胞表面，并从该表面洗脱。然后，将这些亲和纯化的抗体用于探测由测试菌株制备的蛋白质免疫印迹，以检测交叉反应结构域。我们发现，抗原蛋白在所有嗜肺军团菌血清型中通常是保守的。虽然其中一些抗原结构域与其他军团菌属成员共有，但它们与不同分子量的蛋白质相关。我们研究抗原交叉反应性的方法，相对于使用单克隆抗体或用纯化抗原免疫制备的单特异性抗体的类似研究，具有潜在优势。
