热诱导表面应激蛋白（Hsp70）介导呼吸道病原体流感嗜血杆菌对硫脂的识别。
Heat-inducible surface stress protein (Hsp70) mediates sulfatide recognition of the respiratory pathogen Haemophilus influenzae.
作者信息
Hartmann E, Lingwood C A, Reidl J
机构信息
Zentrum für Infektionsforschung, Universität Würzburg, Röntgenring 11, Würzburg, Germany.
出版信息
Infect Immun. 2001 May;69(5):3438-41. doi: 10.1128/IAI.69.5.3438-3441.2001.
Abstract
The in vitro glycolipid binding specificity of clinical strains of nontypeable Haemophilus influenzae is altered to include sulfated glycolipids following a brief heat shock. We have constructed, expressed, and purified a recombinant protein of H. influenzae Hsp70, which showed significant specific binding to sulfated galactolipids in vitro. Furthermore, indirect immunofluorescence demonstrates that Hsp70 proteins are surface exposed in H. influenzae only after heat shock and are contained in the outer membrane protein fractions.
摘要
不可分型流感嗜血杆菌临床菌株的体外糖脂结合特异性在短暂热休克后发生改变，包括与硫酸化糖脂结合。我们构建、表达并纯化了流感嗜血杆菌Hsp70的重组蛋白，该蛋白在体外显示出与硫酸化半乳糖脂有显著的特异性结合。此外，间接免疫荧光显示，Hsp70蛋白仅在热休克后暴露于流感嗜血杆菌表面，并存在于外膜蛋白组分中。
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