Cellular localization of a Hsp90 homologue in Porphyromonas gingivalis

We previously reported an association between elevated serum antibody titers to the 90-kDa human heat shock protein (Hsp90), periodontal health and colonization by Porphyromonas gingivalis. In this study, we examined the cellular localization of the Hsp90 homologue of P. gingivalis. Cultures of P. g...

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Bibliographic Details
Published in:FEMS microbiology letters 1999-12, Vol.181 (1), p.9-16
Main Authors: Lopatin, Dennis E., Jaramillo, Eduardo, Edwards, Chris A., Van Poperin, Neal, Combs, Allison, Shelburne, Charles E.
Format: Article
Language:English
Subjects:
90-kDa human heat shock protein
Extracellular vesicle
Heat shock
Hsp90 protein
Porphyromonas gingivalis
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Summary:We previously reported an association between elevated serum antibody titers to the 90-kDa human heat shock protein (Hsp90), periodontal health and colonization by Porphyromonas gingivalis. In this study, we examined the cellular localization of the Hsp90 homologue of P. gingivalis. Cultures of P. gingivalis were 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.
ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-1097(99)00506-6