[Phenotypical curing of Streptococcus pneumoniae treated with amidase induced by the Dp-1 bacteriophage].
A phage-associated murein hydrolase activity (PAL) induced in an autolysis-defective mutant of Streptococcus pneumoniae infected with the bacteriophage Dp-1 has been recently isolated and purified to electrophoretic homogeneity as well as biochemically characterized as an endo-N-acetyl-muramyl-L-alanine amidase (1, 3, 4). The PAL and the inactive form (E-form) of the host cell autolysin show a remarkable biochemical similarity, although they differ in their immunological characteristics. The PAL was adsorbed onto a live, defective mutant of pneumococcus (cwl) and such cells reverted to the wild type phenotype ("cured" cells) in some important characteristics present in the wild type strain (R6), as: i) lysis of the culture in the stationary phase, ii) protoplast formation by hypertonic sucrose, and iii) bacteriolytic response against the penicillin in contrast with the bacteriostatic response of the "non-cured" cwl. The adsorbed enzyme segregates during growth of the "cured" cells. Our results demonstrate that PAL acts in the phenotypically "cured" cells in a similar way to that previously described for the host enzyme, and also confirm the finding that the autolysins play a direct role in the irreversible effects produced in S. pneumoniae by the betalactamic antibiotics.
García
P
P
Instituto de Inmunología y Biología Microbiana, Madrid, España.
García
E
E
Ronda
C
C
López
R
R
D000581:Amidohydrolases / Q000502:physiology*; D001435:Bacteriophages / Q000201:enzymology*; D009154:Mutation; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000502:physiology*; D010641:Phenotype; D013296:Streptococcus pneumoniae / Q000201:enzymology* / Q000235:genetics; D014169:Transformation, Bacterial
D000581:Amidohydrolases; D009238:N-Acetylmuramoyl-L-alanine Amidase
Curación fenotípica de Streptococcus pneumoniae tratado con amidasa inducida por el bacteriófago Dp-1.