The homolog of the chromosomally encoded stationary-phase sigma factor RpoS
in Borrelia burgdorferi was inactivated using gyrB(r) as a selectable mark
er. Two-dimensional nonequilibrium pH gradient electrophoresis of stationar
y-phase cell lysates identified at least 11 differences between the protein
profiles of the rpoS mutant and wild-type organisms. Wild-type B. burgdorf
eri had a growth phase-dependent resistance to 1 N NaCl, similar to the sta
tionary-phase response reported for other bacteria. The B. burgdorferi rpoS
mutant strain was less resistant to osmotic stress in stationary phase tha
n the isogenic rpoS wild-type organism. The results indicate that the B. bu
rgdorferi rpoS homolog influences protein composition and participates in s
tationary-phase-dependent osmotic resistance. This rpoS mutant will be usef
ul for studying regulation of gene expression in response to changing envir
onmental conditions.