Anthrax-specific "AP 50-like" phages isolated from Bacillus cereus strains.

Phages exerting a specific action on Bacillus anthracis were isolated from mitomycin C-induced concentrated lysates of 5 Bacillus cereus strains producing megacin A (phospholipase A). In electron micrographs the phages closely resembled the anthrax-specific, lipid containing phage AP 50 isolated earlier from soil sample. The phages were similar to AP 50 also in their antigenic and chemical structure, host range and sensitivity to organic solvents, detergents and caesium chloride.

Mapping the uroporphyrinogen decarboxylase, coproporphyrinogen oxidase and ferrochelatase loci in Bacillus subtilis.

Three genes hemE, hemF, hemG taking part in the porphyrin biosynthesis of Baccillus subtilis were mapped by two- and three-factor transduction crosses. The gene hemE determines uroporphyrinogen decarboxylase (EC 4.1.

Characteristics of phage AP50, an RNA phage containing phospholipids.

A bacteriophage specific for Bacillus anthracis was isolated and designated as AP50. The nucleic acid of phage AP50 is RNA and the virion contains five different phospholipids. Some physical and biological characteristics of the phage, including morphology, were examined.

Studies on megacinogeny in Bacillus cereus. II. Bacillus cereus isolates characterized by prophage-controlled production of megacin A (phospholipase A).

Five out of a number of Bacillus cereus strains isolated from soil produced high titre specific bacteriocin (megacin A) in mitomycin C-induced cultures. In the course of cultivation with ethidium bromide, the strains gave off segregants not producing bacteriocin (cin-). The lysate of two wild strains formed plaques on the corresponding cin- bacteria.