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致病性和非致病性分枝杆菌对α2层粘连蛋白的结合以及对雪旺细胞的黏附。

Binding of alpha2-laminins by pathogenic and non-pathogenic mycobacteria and adherence to Schwann cells.

作者信息

Marques M A, Ant nio V L, Sarno E N, Brennan P J, Pessolani M C

机构信息

Laboratório de Hanseníase, Fundaçao Oswaldo Cruz, Rio de Janeiro, RJ, Brazil.

出版信息

J Med Microbiol. 2001 Jan;50(1):23-8. doi: 10.1099/0022-1317-50-1-23.

Abstract

The ability of Mycobacterium leprae to specifically bind alpha2-laminins of Schwann cells has been described recently as being an important property of the leprosy bacillus, which could explain the neural tropism of M. leprae. Therefore, the extent of the expression of alpha2-laminin-binding properties among mycobacteria was investigated. In an ELISA-based assay, all three species of Mycobacterium tested (M. tuberculosis, M. chelonae and M. smegmatis) expressed laminin-binding capacity, suggesting that the ability to bind alpha2-laminins is conserved within the genus Mycobacterium. This report also demonstrated that not only M. leprae but all the mycobacterial species tested readily interacted with the ST88-14 cells, a human schwannoma cell line, and that the addition of soluble alpha2-laminins significantly increased their adherence to these cells. These results failed to demonstrate the presence in M. leprae of a unique system based on alpha2-laminins for adherence to Schwann cells.

摘要

麻风分枝杆菌特异性结合施万细胞α2-层粘连蛋白的能力最近被描述为麻风杆菌的一个重要特性,这可以解释麻风分枝杆菌的神经嗜性。因此,研究了分枝杆菌中α2-层粘连蛋白结合特性的表达程度。在基于酶联免疫吸附测定(ELISA)的试验中,所测试的三种分枝杆菌(结核分枝杆菌、龟分枝杆菌和耻垢分枝杆菌)均表达了层粘连蛋白结合能力,这表明结合α2-层粘连蛋白的能力在分枝杆菌属内是保守的。本报告还证明,不仅麻风分枝杆菌,而且所有测试的分枝杆菌物种都能与人类施万细胞瘤细胞系ST88-14细胞轻松相互作用,并且添加可溶性α2-层粘连蛋白显著增加了它们对这些细胞的粘附。这些结果未能证明麻风分枝杆菌中存在基于α2-层粘连蛋白粘附施万细胞的独特系统。

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