Heat-shock proteins (hsp) are ubiquitously produced molecules which participate in the protection of cells from environmental perturbation. Moreover, the members of the heat-shock protein 60 (hsp60) and 70 (hsp70) families play an important role in pathogen-host interactions. We studiedin vivo production of the 70-kDa heat-shock proteins in the extract of peritoneal exudate cells (PEC) from mice injected intraperitoneally with an attenuated vaccine strain (LVS) ofFrancisella tularensis. We found a differential production of a highly stress-inducible member of the hsp70 family, designated hsp72, in three inbred strains of mice exhibiting either resistance or susceptibility toF. tularensis LVS infection. Whereas in tularemia-resistant mice hsp72 was even expressed in PEC without injection of bacteria and its production further increased on day 3 and slowly declined on days 5 and 7 after injection, in susceptible mice hsp72 production was highly inducble and restricted only to day 3 afterin vivo infection. Further analysis of hsp72 expression revealed intracellular hsp72 accumulation and its preferential production by peritoneal adherent cells.
Peritoneal Cell Peritoneal Exudate Cell Francisella Tularensis Live Vaccine Strain Hsp72 Production
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