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. 1987 Aug;61(8):2573-80.
doi: 10.1128/JVI.61.8.2573-2580.1987.

Cloning, purification, and biochemical characterization of the pneumococcal bacteriophage Cp-1 lysin

J L García, E García, A Arrarás, P García, C Ronda, R López

Cloning, purification, and biochemical characterization of the pneumococcal bacteriophage Cp-1 lysin

J L García et al. J Virol. 1987 Aug.

Abstract

Cp-1, a small virulent bacteriophage infecting Streptococcus pneumoniae, encodes its own lytic enzyme (CPL). A fragment of Cp-1 DNA containing the gene cpl coding for CPL was cloned and expressed in high amounts in Escherichia coli. CPL was purified to electrophoretic homogeneity by using affinity chromatography on choline-Sepharose (T. Briese and R. Hakenbeck, Eur. J. Biochem. 146:417-427, 1985), and the enzyme showing a Mr of 39,000 was characterized as a muramidase. This muramidase required for in vivo and in vitro activity the presence of choline in the teichoic acids of the pneumococcal cell walls. Free choline or lipoteichoic acid noncompetitively inhibited the activity of CPL.

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