Affiliation:
1. Department of Medicine, New York University School of Medicine, New York, New York 10016
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 β-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 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 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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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