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Phagocytosis and killing of gram-positiveBacillus megaterium andMicrococcus lysodeikticus by granulocytes in vitro is associated with almost immediate cessation of bacterial protein synthesis. By contrast, protein synthesis byEscherichia coli continues after ingestion and killing. After preincubation ofE. coli with intact granulocytes for 15 min, when 95% or more of the bacteria can no longer multiply, induction of β-galactosidase proceeds at rates about half of control values. With disrupted granulocytes, which killE. coli as rapidly as intact cells, the rate of induction of β-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 ofE. coli are apparently incompletely degraded during phagocytosis. However, the cell walls ofM. lysodeikticus andB. 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 theE. 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.

Effects of Phagocytosis by Rabbit Granulocytes on Macromolecular Synthesis and Degradation in Different Species of Bacteria