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. gingivalis were heat-stressed (45 degrees 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.
Lopatin
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DE
Department of Biologic and Materials Science, University of Michigan School of Dentistry, 1011 North University Ave, Campus Box 1078, Ann Arbor, MI 48109-1078, USA.
Jaramillo
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E
Edwards
C A
CA
Van Poperin
N
N
Combs
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A
Shelburne
C E
CE
D015153:Blotting, Western; D005455:Fluorescent Antibody Technique; D018841:HSP90 Heat-Shock Proteins / Q000032:analysis* / Q000378:metabolism; D018869:Heat-Shock Response; D007150:Immunohistochemistry; D016966:Porphyromonas gingivalis / Q000737:chemistry* / Q000254:growth & development / Q000378:metabolism; D013347:Subcellular Fractions
D018841:HSP90 Heat-Shock Proteins