单核细胞增生李斯特菌和伊氏李斯特菌中新型内化素相关蛋白的鉴定与纯化
Identification and purification of novel internalin-related proteins in Listeria monocytogenes and Listeria ivanovii.
作者信息
Lingnau A, Chakraborty T, Niebuhr K, Domann E, Wehland J
机构信息
Gesellschaft für Biotechnologische Forschung, Braunschweig, Germany.
出版信息
Infect Immun. 1996 Mar;64(3):1002-6. doi: 10.1128/iai.64.3.1002-1006.1996.
Abstract
Monoclonal antibodies were generated against a 30-kDa protein fraction derived from culture supernatants of a Listeria monocytogenes strain complemented with additional copies of the prfA regulator gene. Several of the antibodies reacted specifically with a hitherto unidentified, secreted 30-kDa polypeptide. By immunoblot analysis, the expression of this 30kDa polypeptide was found to be dependent on the presence of the PrfA regulator protein. Microsequencing of peptides derived from the partially purified 30-kDa protein revealed homologies to the InlA and InlB polypeptides of L. monocytogenes, which are required for the internalization of the bacteria into nonphagocytic cell lines. This prompted us to term the 30-kDa polypeptide internalin-related protein (Irp). Irp-specific monoclonal antibodies cross-reacted with a 24-kDa polypeptide present in culture supernatants of Listeria ivanovii, indicating the existence of an Irp-related protein in this pathogenic Listeria species.
摘要
针对从单核细胞增生李斯特菌菌株培养上清液中获得的30 kDa蛋白组分制备了单克隆抗体，该菌株补充了额外拷贝的prfA调节基因。其中几种抗体与一种迄今未鉴定的分泌型30 kDa多肽发生特异性反应。通过免疫印迹分析，发现这种30 kDa多肽的表达依赖于PrfA调节蛋白的存在。对部分纯化的30 kDa蛋白衍生肽段进行微测序，发现其与单核细胞增生李斯特菌的InlA和InlB多肽具有同源性，这两种多肽是细菌内化进入非吞噬细胞系所必需的。这促使我们将这种30 kDa多肽称为内化素相关蛋白（Irp）。Irp特异性单克隆抗体与伊氏李斯特菌培养上清液中存在的一种24 kDa多肽发生交叉反应，表明在这种致病性李斯特菌中存在一种Irp相关蛋白。
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