Production of stress-inducible form of heat-shock protein 70 in mouse peritoneal adherent cells after in vivo infection by Francisella tularensis.
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 studied in 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) of Francisella 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 to F. 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 inducible and restricted only to day 3 after in vivo infection. Further analysis of hsp72 expression revealed intracellular hsp72 accumulation and its preferential production by peritoneal adherent cells.
Stulík
J
J
Institute of Radiobiology and Immunology, Purkynĕ Military Medical Academy, Hradec Králové, Czech Republic. jstulik@pmfhk.cz
Hernychová
L
L
Macela
A
A
Krocová
Z
Z
Kroca
M
M
D000818:Animals; D002448:Cell Adhesion; D050884:HSP72 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D051379:Mice; D008809:Mice, Inbred C3H; D008810:Mice, Inbred C57BL; D010529:Peritoneal Cavity / Q000166:cytology / Q000382:microbiology*; D014406:Tularemia / Q000378:metabolism*
D050884:HSP72 Heat-Shock Proteins; D006360:Heat-Shock Proteins