Hemin-binding protein 35 (HBP35) plays an important role in bacteria-mammalian cells interactions in Porphyromonas gingivalis
Hemin-binding protein 35 (HBP35) plays an important role in bacteria-mammalian cells interactions in Porphyromonas gingivalis
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DOI：
10.1016/j.micpath.2010.01.001
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发表时间：
2010-03-01
影响因子：
3.8
通讯作者：
Abiko, Yoshimitsu
中科院分区：
文献类型：
--
作者：
Hiratsuka, Koichi;Kiyama-Kishikawa, Michiko;Abiko, Yoshimitsu
血红素结合蛋白35（HBP 35）可能是牙龈卟啉单胞菌逃避环境胁迫生存的必需蛋白。抗重组HBP 35抗体抑制牙龈卟啉单胞菌血凝。本研究使用源自牙龈卟啉单胞菌FDC 381的HBP 35缺陷突变体（MD 774）考虑了该蛋白在血凝和粘附宿主细胞中的作用。FDC 381具有较强的血凝活性，而MD 774没有活性。抗130 kDa血凝素抗体mAb-Pg-vc主要与膜组分中的43和49 kDa分子反应。然而，在MD 774中没有蛋白质反应。MD 774的溶血活性远低于FDC 381。抗重组HBP 35抗体强烈抑制牙龈卟啉单胞菌FDC 381对上皮细胞的粘附。此外，MD 774显示出粘附性显著降低。MD 774的疏水性相当于FDC 381的19.4%。两种菌株的膜组分的SDS-PAGE分析显示非常不同的配置文件。总之，这些发现表明HBP 35不仅在氯化血红素结合中起作用，而且在多种牙龈卟啉单胞菌与红细胞和宿主上皮牙龈细胞的结合中起作用。此外，这种蛋白质可能直接和/或间接影响该生物体的毒力。(C)2010爱思唯尔有限公司保留所有权利。
Hemin-binding protein 35 (HBP35) may be an essential protein for bacterial survival in evasion from environmental stress in Porphyromonas gingivalis. The anti-recombinant HBP35 antibody inhibits P gingivalis hemagglutination. This study considered the role of this protein for hemagglutination and adherence to host cells using the HBP35-deficient mutant (MD774) derived from P. gingivalis FDC381. FDC381 had strong hemagglutination activity, whereas MD774 had no activity. Anti-130-kDa hemagglutinin antibody, mAb-Pg-vc, reacted mainly with the 43- and 49-kDa molecules in the membrane fraction. However, no proteins reacted in the MD774. The hemolytic activity in MD774 was much lower than that in FDC381. Anti-recombinant HBP35 antibody strongly inhibited the P. gingivalis FDC381 adherence to epithelial cells. In addition, MD774 exhibited a significant decrease in the adherence. The hydrophobicity of MD774 was equal to 19.4% of that of FDC381. SDS-PAGE profiling of the membrane fractions of both strains showed very different profiles. Taken together, these findings suggest that HBP35 plays a role, not only in hemin-binding, but also in multiple P. gingivalis binding to erythrocytes, and host epithelial gingival cells. In addition, this protein may directly and/or indirectly affect the virulence of this organism. (C) 2010 Elsevier Ltd. All rights reserved.