physiological function |
leptospiral HslUV is an ATP-dependent chaperone-peptidase complex containing ATPase associated with various cellular activity (AAA+) and N-terminal nucleophile (Ntn) hydrolase superfamily domains, respectively, which hydrolyzes casein and chymotrypsin-like substrates. Hydrolysis is blocked by threonine protease inhibitors. The infection of J774A.1 acrophages causes the increase of leptospiral denatured protein aggresomes, but more aggresomes accumulate in hslUV gene-deleted mutant. Compared to the wild-type strain, infection of cells in vitro with the mutant result in a higher number of dead leptospires, less leptospiral colonyforming units and lower growth ability, but also display a lower half lethal dose, attenuated histopathological injury and decreased leptospiral loading in lungs, liver, kidneys, peripheral blood and urine in hamsters |
Leptospira interrogans serovar Canicola |