Pneumococcal bacteriophage Cp-1 encodes its own protease essential for phage maturation.
The major capsid protein of the pneumococcal phage Cp-1 that accounts for 90% of the total protein found in the purified virions is synthesized by posttranslational processing of the product of the open reading frame (ORF) orf9. Cloning of different ORFs of the Cp-1 genome in Escherichia coli and Streptococcus pneumoniae combined with Western blot analysis of the expressed products led to the conclusion that the product of orf13 is an endoprotease that cleaves off the first 48 amino acid residues of the major head protein. This protease appears to be a key enzyme in the morphopoietic pathway of the Cp-1 phage head. To our knowledge, this is the first case of a bacteriophage infecting gram-positive bacteria that encodes a protease involved in phage maturation.
Martín
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Departamento de Microbiología Molecular, Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
López
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García
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D004268:DNA-Binding Proteins / Q000235:genetics*; D005814:Genes, Viral; D017108:Streptococcus Phages / Q000201:enzymology* / Q000235:genetics / Q000502:physiology*; D014764:Viral Proteins / Q000235:genetics*; D014779:Virus Replication
D004268:DNA-Binding Proteins; D014764:Viral Proteins; C048231:terminal protein, Streptococcus phage Cp-1