The structural proteins of the purified lipid-containing anthrax phage AP 50 were studied by SDS-polyacrylamide gel electrophoresis. Nine major structural proteins were found. The pattern of phage DNA was determined by agarose gel electrophoresis after its treatment with I restriction endonuclease. The mol. wt. of phage DNA was calculated as 9.0 ± 0.5 × 10. The infection process was followed by thin sectioning and electron microscopy. During infection phage were attached to the cell wall of the host, and the adsorbed phage apparently injected their DNA through an electron microscopically visible channel formed across the cell wall. Maturation of the phage capsid appears to take place within the nuclear region of the cell. Before lysis, intact phage with DNA could be seen first in vesicles at the cell periphery and afterwards between the cell wall and the cytoplasmic membrane. Mature phage were finally released by the rupture of the cell wall.


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