Cellular localization of a Hsp90 homologue in Porphyromonas gingivalis.
Cellular localization of a Hsp90 homologue in Porphyromonas gingivalis.
复制标题
牙龈卟啉单胞菌中 Hsp90 同源物的细胞定位。
DOI：
10.1111/j.1574-6968.1999.tb08820.x
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发表时间：
1999
影响因子：
2.1
通讯作者：
Shelburne,CE
中科院分区：
文献类型：
--
作者：
Lopatin,DE;Jaramillo,E;Edwards,CA;VanPoperin,N;Combs,A;Shelburne,CE
We previously reported an association between elevated serum antibody titers to the 90-kDa human heat shock protein (Hsp90), periodontal health and colonization byPorphyromonas gingivalis. In this study, we examined the cellular localization of the Hsp90 homologue ofP. gingivalis. Cultures ofP. gingivaliswere heat-stressed (45°C) and examined for localization of the Hsp90 homologue. Heat stress induced a 4–5-fold increase in anti-Hsp90 antibody reactivity over that of the unstressed controls. Western blot analysis revealed two bands (44 and 68 kDa) that reacted with anti-Hsp90 antibodies. The 68-kDa band was heat-inducible, while the 44-kDa band was not. Immunogold staining revealed that the Hsp90 homologue localized principally to the membrane and extracellular vesicles. Subcellular fractionation confirmed that the Hsp90 homologue was primarily membrane-associated.
