DETECTION OF HOST-ORIGINATED ACID PHOSPHATASE ON THE SURFACE OF ^|^ldquo;IN VIVO GROWN TUBERCLE BACILLI^|^rdquo;

Abstract
Acid phosphatase activity of the mouse lungs was elevated in response to tuberculous infection. This elevation was accelerated when the mice had been immunized with BCG. "In vivo grown tubercle bacilli" (H37RvL) were separated and purified mechanically from the lungs of moribund mice which had been infected intravenously with 1 mg of H37Rv grown on Sauton medium. The pH activity curve of acid phosphatase of H37RvL was different from that of Sauton H37Rv, taking the pattern similar to the lung tissue. Several evidences were presented to indicate that this enzyme activity of H37RvL was due to the presence of host-originated acid phosphatase bound on the surface of the bacilli. In addition, it was admitted that acid phosphatase activity peculiar to Sauton H37Rv bacilli was lost or masked during their stay in the mouse lungs. The intensity of acid phosphatase activity of H37RvL was not affected essentially by treatment with trypsin or Triton X-100, but was completely abolished by NaOH (4%) treatment without loss of bacillary viability. After incubation at 37 C with lung tissue extract or "lysosomal fraction", Sauton H37Rv bacilli acquired totally or partially the same pattern of acid phosphatase activity as H37RvL. The enzyme activity of H37RvL was interpreted as the result of lysosome-parasite interaction within phagocytes, and discussion is made referring to the recent informations concerning phagocytosis.