Abstract
Phagocytosis and killing of gram-positive Bacillus megaterium and Micrococcus lysodeikticus by granulocytes in vitro is associated with almost immediate cessation of bacterial protein synthesis. By contrast, protein synthesis by Escherichia coli continues after ingestion and killing. After preincubation of E. coli with intact granulocytes for 15 min, when 95% or more of the bacteria can no longer multiply, induction of beta-galactosidase proceeds at rates about half of control values. With disrupted granulocytes, which kill E. coli as rapidly as intact cells, the rate of induction of beta-galactosidase does not fall until after 30 min of preincubation. We attribute the different effects of phagocytosis on the biochemical apparatus of these microorganisms to the different fates of their envelopes. Specifically labeled protein, ribonucleic acid, deoxyribonucleic acid, and lipid of all three species of bacteria and peptidoglycan of E. coli are apparently incompletely degraded during phagocytosis. However, the cell walls of M. lysodeikticus and B. megaterium undergo rapid and almost complete degradation. The resulting structural disintegration of these gram-positive microorganisms must cause extensive biochemical disorganization as well. Our evidence indicates that the E. coli envelope, on the other hand, retains sufficient structural organization to preserve integrated biochemical function for at least 1 h after the bacteria have lost the ability to multiply.