Differential heat-shock protein synthesis and response to stress in three avirulent and virulent Listeria species.
Two strains of Listeria monocytogenes, a virulent (V) and an avirulent (A) strain obtained by repeated in vitro cultivation at 37 degrees C, exhibited differing constitutive syntheses of heat-shock proteins (HSP) at 37 degrees C, the temperature of the infected host, and a differential response to heat treatment. These two strains also reacted differently to addition of a superoxide ion inducer and acid to treatments. Our observations were not limited to these two strains of L. monocytogenes: the level of HSP synthesis at 37 degrees C varied from one species of Listeria to another and was correlated with the thermo-inducibility of HSP. In an accompanying paper, we will attempt to establish whether these different biosynthetic properties observed in vitro between A and V L. monocytogenes enable the prediction of their properties/survival once inside the resident peritoneal murine macrophages.
Morange
M
M
Unité d'Immunophysiologie cellulaire, Institut Pasteur, Paris.
Hévin
B
B
Fauve
R M
RM
D001426:Bacterial Proteins / Q000096:biosynthesis*; D015153:Blotting, Western; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008089:Listeria monocytogenes / Q000145:classification / Q000378:metabolism* / Q000472:pathogenicity; D010100:Oxygen; D014774:Virulence / Q000502:physiology*
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D010100:Oxygen