细粒棘球绦虫抗原5和抗原B单克隆抗体的进一步特性分析。

Further characterization of monoclonal antibodies to Echinococcus granulosus antigen 5 and antigen B.

作者信息

Liu D, Rickard M D, Lightowlers M W

机构信息

University of Melbourne, Veterinary Clinical Centre, Werribee, Victoria, Australia.

出版信息

Int J Parasitol. 1992 May;22(3):391-4. doi: 10.1016/s0020-7519(05)80019-0.

DOI:10.1016/s0020-7519(05)80019-0

PMID:1379216

Abstract

Two monoclonal antibodies (24.14, 61A12) to Echinococcus granulosus Antigen 5 and two (31.15 and 39B3) to Antigen B were further characterized using modified sheep hydatid cyst fluid antigens (SHCF) in ELISA. None of these four monoclonals were directed against carbohydrate or lipid epitopes of SHCF antigens since they all reacted strongly with periodate or lipase-treated SHCF. On the other hand, they appeared to recognize SHCF determinants of protein nature as protease treatment of SHCF destroyed binding with the monoclonals. Anti-Antigen B monoclonals 31.15 and 39B3 showed strong reaction with boiled SHCF and anti-Antigen 5 monoclonal 24.14 did not. However, the second anti-Antigen 5 monoclonal 61A12 also reacted with boiled SHCF suggesting that some epitopes of Antigen 5 are heat stable. 24.14 and 61A12 may recognize a similar epitope of Antigen 5 whereas 39B3 may be against an epitope of Antigen B different from that recognized by 31.15.

摘要

使用改良的绵羊包虫囊肿液抗原（SHCF）在酶联免疫吸附测定（ELISA）中进一步鉴定了两种针对细粒棘球绦虫抗原5的单克隆抗体（24.14、61A12）和两种针对抗原B的单克隆抗体（31.15和39B3）。这四种单克隆抗体均未针对SHCF抗原的碳水化合物或脂质表位，因为它们都与经高碘酸盐或脂肪酶处理的SHCF发生强烈反应。另一方面，它们似乎识别蛋白质性质的SHCF决定簇，因为SHCF经蛋白酶处理后会破坏与单克隆抗体的结合。抗抗原B单克隆抗体31.15和39B3与煮沸的SHCF反应强烈，而抗抗原5单克隆抗体24.14则不反应。然而，第二种抗抗原5单克隆抗体61A12也与煮沸的SHCF反应，这表明抗原5的一些表位是热稳定的。24.14和61A12可能识别抗原5的相似表位，而39B可能针对与31.15识别的不同的抗原B表位。