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首页> 外文期刊>Infection and immunity >GroEL Heat Shock Protein of Haemophilus ducreyi: Association with Cell Surface and Capacity To Bind to Eukaryotic Cells
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GroEL Heat Shock Protein of Haemophilus ducreyi: Association with Cell Surface and Capacity To Bind to Eukaryotic Cells

机译：杜氏嗜血杆菌的GroEL热休克蛋白：与细胞表面和绑定到真核细胞的能力的关联。

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The Haemophilus ducreyi homolog of GroEL, a 58.5-kDa heat shock protein (Hsp), is a dominant protein produced not only in response to heat stress but also under in vitro growth conditions. Extracellular localization of the 58.5-kDa Hsp was investigated by whole-cell enzyme-linked immunosorbent assay (ELISA) and immunoelectron microscopy and in supernatants of washed bacteria by immunoblotting with a Haemophilus ducreyi GroEL-specific mouse monoclonal antibody (BB11). To investigate binding of the Hsp to eukaryotic cells, the 58.5-kDa Hsp was purified by ion-exchange and size exclusion chromatography; incubated with HEp-2 cells, HeLa cells, and human fibroblasts; and then analyzed by immunoblotting. Direct involvement of the 58.5-kDa Hsp in the adherence of H. ducreyi to HEp-2 cells was investigated by using an inhibition assay. An epitope of the 58.5-kDa Hsp was detected by whole-cell ELISA on all of the strains tested, suggesting that it is associated with the cell surface. This was also supported by immunoelectron microscopy results. In supernatants of washed bacteria, the 58.5-kDa Hsp was detected by immunoblotting after 10 h of cultivation. The 58.5-kDa Hsp bound to the eukaryotic cells tested but exerted only limited (about 20%) inhibition of H. ducreyiadherence to HEp-2 cells. These results demonstrate that the 58.5-kDa Hsp of H. ducreyi is associated with the bacterial surface, binds to eukaryotic cells, and partially influences H. ducreyi adherence to HEp-2 cells, indicating possible involvement of the 58.5-kDa Hsp in the attachment of bacteria to host cells and to each other.
机译：GroEL的 Haemophilus ducreyi 同源物是58.5 kDa的热激蛋白（Hsp），是一种主要蛋白，不仅响应热应激，而且在体外生长条件下均产生。通过全细胞酶联免疫吸附测定（ELISA）和免疫电子显微镜研究58.5 kDa Hsp的细胞外定位，并通过 Duemyi嗜血杆菌 GroEL特异性小鼠单克隆抗体免疫印迹法在洗涤细菌的上清液中进行研究（BB11）。为了研究Hsp与真核细胞的结合，通过离子交换和尺寸排阻色谱法纯化了58.5-kDa Hsp。与HEp-2细胞，HeLa细胞和人成纤维细胞一起孵育;然后通过免疫印迹进行分析。 58.5 kDa Hsp直接参与 H的参与。用抑制试验研究了杜克雷伊对HEp-2细胞的影响。通过全细胞ELISA在所有测试的菌株上检测到58.5-kDa Hsp的表位，表明它与细胞表面有关。免疫电子显微镜结果也证明了这一点。在洗涤的细菌的上清液中，培养10小时后通过免疫印迹检测到58.5 kDa Hsp。 58.5 kDa Hsp与测试的真核细胞结合，但对H的抑制作用有限（约20％）。 ducreyi 对HEp-2细胞的粘附。这些结果证明 H的58.5-kDa Hsp。 ducreyi 与细菌表面相关，与真核细胞结合，并部分影响 H。 ducreyi 对HEp-2细胞的粘附，表明58.5 kDa Hsp可能参与细菌与宿主细胞以及彼此之间的粘附。

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