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针对立氏立克次体表面蛋白热敏感和耐热表位的单克隆抗体的中和活性

Neutralizing activity of monoclonal antibodies to heat-sensitive and heat-resistant epitopes of Rickettsia rickettsii surface proteins.

作者信息

Anacker R L, McDonald G A, List R H, Mann R E

出版信息

Infect Immun. 1987 Mar;55(3):825-7. doi: 10.1128/iai.55.3.825-827.1987.

Abstract

Antiprotein monoclonal antibodies derived from mice inoculated with Rickettsia rickettsii heated at 56 degrees C for 15 min are of two types: one is type specific for epitopes denatured by moderate temperatures, and the other is specific for epitopes resistant to 100 degrees C for 5 min. The heat-resistant epitopes are found by immunoblotting on multiple polypeptides after solubilization of the rickettsiae at temperatures of 56 degrees C or higher. Most, but not all, antibodies to the heat-sensitive epitopes passively protected mice against two 50% lethal doses of R. rickettsii, whereas none of the antibodies to heat-resistant epitopes did.

摘要

用在56℃加热15分钟的立氏立克次氏体接种小鼠所产生的抗蛋白质单克隆抗体有两种类型:一种对经适度温度变性的表位具有型特异性,另一种对在100℃耐受5分钟的表位具有特异性。通过在56℃或更高温度下溶解立克次氏体后对多种多肽进行免疫印迹发现了耐热表位。大多数(但不是全部)针对热敏表位的抗体被动保护小鼠抵抗两个50%致死剂量的立氏立克次氏体,而针对耐热表位的抗体均无此作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8c42/260417/a7786278830c/iai00087-0338-a.jpg

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