Abstract
Lysosomal components were obtained as a Triton-lysate of the lung and spleen granular fractions of mice infected with virulent tubercle bacilli or BCG. Incubation of tubercle bacilli with the components resulted in that the bacilli gained the lysosomal acid phosphatase activity, whereas the phosphatase activity specific for the bacilli decreased with simultaneous reduction of viability. Lysosomal components were subjected to gel-filtration on Sephadex G-100 and G-200 column with the hope of separation of antimycobacterial and phosphatase activities. A fraction was obtained which had a mycobactericidal property and a property of inhibiting bacillary acid phosphatase activity. On the other hand, a separate fraction showed the affinity to the bacilli giving them the additional phosphatase activity at the lower pH range, but exerting no bactericidal action. These results reveal one aspect of the lysosome-bacillus interaction in tuberculous infection. The results also support the idea that the pH pattern of phosphatase activity shown by “in vivo grown tubercle bacilli” is the combined results of inhibition of the bacillus-specific enzymatic activity and coating of such bacilli with lysosomal acid phosphatase.
