de Sa C, Souriau A, Bernard F, Salinas J, Rodolakis A
Laboratoire de Pathologie Infectieuse et Immunologie, Centre de Tours, Institut National de la Recherche Agronomique, Nouzilly, France.
Infect Immun. 1995 Dec;63(12):4912-6. doi: 10.1128/iai.63.12.4912-4916.1995.
Monoclonal antibodies (MAbs) were generated against an ovine abortive strain of Chlamydia psittaci. A plaque reduction assay was used to select 19 neutralizing antibodies which appeared to be heterogeneous in isotype, specificity, and recognized proteins. Different neutralizing MAbs were tested for their protective abilities against abortion in a pregnant-mouse model. All of the protective MAbs selected had the same isotype, were serotype 1 specific, and recognized a protein of about 110 kDa by immunoblotting. The recognized epitopes were resistant to sodium dodecyl sulfate and reducing agents, but all of them were heat sensitive. The protein was able to form disulfide-linked polymers. Immunological cross-reaction studies with rabbit sera showed a link between the 110-kDa protein and the major outer membrane protein (MOMP). The 110-kDa protein was purified by immunoaffinity and shown to be dissociated after heating into MOMP by silver staining and immunoblotting. These results show homogeneity among protective MAbs directed to heat-sensitive epitopes located on an oligomer of the MOMP of C. psittaci.
制备了针对鹦鹉热衣原体羊流产株的单克隆抗体（MAb）。采用蚀斑减少试验筛选出19种中和抗体，这些抗体在同种型、特异性和识别蛋白方面似乎具有异质性。对不同的中和单克隆抗体在孕鼠模型中针对流产的保护能力进行了测试。所选择的所有保护性单克隆抗体具有相同的同种型，对血清型1具有特异性，并且通过免疫印迹法识别一种约110 kDa的蛋白。所识别的表位对十二烷基硫酸钠和还原剂具有抗性，但所有表位均对热敏感。该蛋白能够形成二硫键连接的聚合物。用兔血清进行的免疫交叉反应研究表明，110 kDa蛋白与主要外膜蛋白（MOMP）之间存在联系。通过免疫亲和法纯化了110 kDa蛋白，经银染和免疫印迹法显示加热后该蛋白可解离为MOMP。这些结果表明，针对位于鹦鹉热衣原体MOMP寡聚体上热敏感表位的保护性单克隆抗体具有同质性。
