Garduño R A, Garduño E, Hoffman P S
Department of Microbiology and Immunology and Department of Medicine, Division of Infectious Diseases, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7.
Infect Immun. 1998 Oct;66(10):4602-10. doi: 10.1128/IAI.66.10.4602-4610.1998.
HeLa cells have been previously used to demonstrate that virulent strains of Legionella pneumophila (but not salt-tolerant avirulent strains) efficiently invade nonphagocytic cells. Hsp60, a member of the GroEL family of chaperonins, is displayed on the surface of virulent L. pneumophila (R. A. Garduño et al., J. Bacteriol. 180:505-513, 1988). Because Hsp60 is largely involved in protein-protein interactions, we investigated its role in adherence-invasion in the HeLa cell model. Hsp60-specific antibodies inhibited the adherence and invasiveness of two virulent L. pneumophila strains in a dose-dependent manner but had no effect on the association of their salt-tolerant avirulent derivatives with HeLa cells. A monospecific anti-OmpS (major outer membrane protein) serum inhibited the association of both virulent and avirulent strains of L. pneumophila to HeLa cells, suggesting that while both Hsp60 and OmpS may mediate bacterial association to HeLa cells, only virulent strains selectively displayed Hsp60 on their surfaces. Furthermore, the surface-associated Hsp60 of virulent bacterial cells was susceptible to the action of trypsin, which rendered the bacteria noninvasive. Additionally, pretreatment of HeLa cells with purified Hsp60 or precoating of the plastic surface where HeLa cells attached with Hsp60 reduced the adherence and invasiveness of the two virulent strains. Finally, recombinant Hsp60 covalently bound to latex beads promoted the early association of beads with HeLa cells by a factor of 20 over bovine serum albumin (BSA)-coated beads and competed with virulent strains for association with HeLa cells. Hsp60-coated beads were internalized in large numbers by HeLa cells and remained in tight endosomes that did not fuse with other vesicles, whereas internalized BSA-coated beads, for which endocytic trafficking is well established, resided in more loose or elongated endosomes. Mature intracellular forms of L. pneumophila, which were up to 100-fold more efficient than agar-grown bacteria at associating with HeLa cells, were enriched for Hsp60 on the bacterial surface, as determined by immunolocalization techniques. Collectively, these results establish a role for surface-exposed Hsp60 in invasion of HeLa cells by L. pneumophila.
先前已利用海拉细胞证明嗜肺军团菌的致病菌株(而非耐盐无毒菌株)能有效侵入非吞噬细胞。伴侣蛋白GroEL家族的成员Hsp60展示在致病嗜肺军团菌的表面(R. A. 加尔杜尼奥等人,《细菌学杂志》180:505 - 513, 1988)。由于Hsp60在很大程度上参与蛋白质 - 蛋白质相互作用,我们在海拉细胞模型中研究了其在黏附 - 侵袭过程中的作用。Hsp60特异性抗体以剂量依赖方式抑制了两种致病嗜肺军团菌菌株的黏附性和侵袭性,但对其耐盐无毒衍生物与海拉细胞的结合没有影响。一种单特异性抗OmpS(主要外膜蛋白)血清抑制了嗜肺军团菌致病和无毒菌株与海拉细胞的结合,这表明虽然Hsp60和OmpS都可能介导细菌与海拉细胞的结合,但只有致病菌株在其表面选择性展示Hsp60。此外,致病细菌细胞表面相关的Hsp60对胰蛋白酶的作用敏感,这使得细菌失去侵袭性。另外,用纯化的Hsp60预处理海拉细胞或用Hsp60预包被海拉细胞附着的塑料表面,可降低两种致病菌株的黏附性和侵袭性。最后,与乳胶珠共价结合的重组Hsp60使珠子与海拉细胞的早期结合比牛血清白蛋白(BSA)包被的珠子增加了20倍,并与致病菌株竞争与海拉细胞的结合。Hsp60包被的珠子被海拉细胞大量内化,并保留在不与其他囊泡融合的紧密内体中,而内化的BSA包被的珠子(其胞吞运输已得到充分证实)存在于更松散或细长的内体中。通过免疫定位技术确定,与琼脂培养的细菌相比,在与海拉细胞结合方面效率高达100倍的嗜肺军团菌成熟细胞内形式,其细菌表面富含Hsp60。总体而言,这些结果确立了表面暴露的Hsp60在嗜肺军团菌侵袭海拉细胞中的作用。