title: Increased permeability and subsequent resealing of the host cell membrane early after infection of Escherichia coli with bacteriophage T1.
abstract: The addition of T1 to cells growing at 37 degrees C in a minimal medium at 0.4 mM Mg2+ rapidly induced an irreversible loss of K+ and Mg2+ and uptake of Na+ by the cells. Both the ATP pool of the cells and the transmembrane proton motive force were reduced. These cells did not lyse from within, since viral DNA replication and the maturation of the 36,000-molecular-weight phage head protein were inhibited. By contrast, cells lysed when infected at 5.4 mM Mg2+. In these cells, T1 initially induced K+ efflux and Na+ influx and lowered the cytoplasmic ATP concentration. After a few minutes, the cation gradients and ATP pool were restored to levels close to that of control cells. At 5.4 mM Mg2+, the shutoff of host protein synthesis was delayed and coincided with the restoration of the ATP pool. In an ATP synthase-negative mutant, infection with T1 did not affect the cytoplasmic ATP concentration but inhibited host protein synthesis with the same rate as it did in wild-type cells.
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D002463:Cell Membrane Permeability; D004261:DNA Replication; D004926:Escherichia coli / Q000378:metabolism*; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D011188:Potassium / Q000378:metabolism; D014176:Protein Biosynthesis; D012964:Sodium / Q000378:metabolism; D013604:T-Phages / Q000378:metabolism*; D013997:Time Factors
chemical_list: D000255:Adenosine Triphosphate; D012964:Sodium; D008274:Magnesium; D011188:Potassium