Bacteriophages of Clostridium saccharoperbutylacetonicum

Abstract

To understand the mechanism of inactivation of HM 2 phage by DNase, studies were made on the properties of the inactivated phage, the structure of the intact and inactivated phages and the properties of the tail.

HM 2 phage inactivated by DNase still retained the unique and large protein structure which combined fully with anti-HM 2 phage serum. According to electron microscopic observation, DNase-inactivated HM 2 phage looked empty and retained its tail surrounded with appendages. Ultracentrifugal analysis indicated that DNase-inactivated phage became a low molecular weight material after DNA had been extruded. The tail of the ghost retained normal ability to attach to its host bacteria, Cl. saccharoperbutylacetonicum N1-4. The tail of HM 2 phage does not have killing and lysing ability.

From these results, it is concluded that the inactivation of HM 2 phage by DNase is not due to the damage of the coat protein and tail structure, but due to the damage of DNA itself.