Control and location of acyl-hydrolysing phospholipase activity in pathogenic mycobacteria.

Phospholipase activities releasing fatty acyl moieties from phosphatidylcholine and phosphatidylethanolamine and lysophospholipase activity releasing fatty acid from lyso-phosphatidylcholine were detected in both Mycobacterium microti and Mycobacterium avium. Fatty acyl groups were released from both the 1- and 2-positions of phosphatidylcholine. Generally, phospholipase activities of M. avium were cryptic while phospholipase activities of M. microti were located on the bacterial surface. However, intact M. microti did not release fatty acids from phospholipids faster than M. avium. Neither Mycobacterium secreted acyl-hydrolysing phospholipase activity. All phospholipase activities were stimulated by including phospholipids in growth media: generally, cell extracts contained 6- to 15-fold higher specific activities than extracts from mycobacteria grown in media without added phospholipid. However, not all phospholipase activities were stimulated to the same degree in any given set of conditions, suggesting the existence of more than one phospholipase gene in each Mycobacterium.