The pneumococcal bacteriophage Dp-1 seems to require the activity of the
N-acetylmuramic acid-
L-alanine amidase of the host bacterium for the liberation of phage progeny into the medium. This conclusion is based on a series of observations indicating that the exit of progeny phage particles is prevented by conditions that specifically inhibit the activity of the pneumococcal
autolysin. These inhibitory conditions are as follows: (i) growth of the bacteria on
ethanolamine-containing medium; (ii) growth of the cells at pH values that inhibit
penicillin-induced lysis of pneumococcal cultures and lysis in the stationary phase of growth; (iii) addition of
trypsin or the
autolysin-inhibitory pneumococcal
Forssman antigen (lipoteichoric
acid) to the growth medium before lysis; (iv)
infection of an
autolysin-defective pneumococcal mutant at a multiplicity of
infection less than 10 (treatment of such infected mutant bacteria with wild-type
autolysin from without can liberate the entrapped progeny phage particles); (v) release of phage particles and culture lysis can also be inhibited by the addition of
chloramphenicol to infected cultures just before the time at which lysis would normally occur. Bacteria infected with Dp-1 under conditions nonpermissive for culture lysis and phage release secrete into the growth medium a substantial portion of their cellular
Forssman antigen in the form of a macromolecular complex that has
autolysin-inhibitory activity. We suggest that a phage product may trigger the bacterial
autolysin by a mechanism similar to that operating during treatment of pneumococci with
penicillin (Tomasz and Waks, 1975).