Details

Autor(en) / Beteiligte

• Volozhantsev, Nikolay V
• Verevkin, Vladimir V
• Bannov, Vasily A
• Krasilnikova, Valentina M
• Myakinina, Vera P
• Zhilenkov, Eugeni L
• Svetoch, Edward A
• Stern, Norman J
• Oakley, Brian B
• Seal, Bruce S

Titel

The genome sequence and proteome of bacteriophage I[brvbar]CPV1 virulent for Clostridium perfringens

Ist Teil von

• Virus research, 2011-02, Vol.155 (2), p.433-439

Erscheinungsjahr

2011

Quelle

Elsevier ScienceDirect Journals

Beschreibungen/Notizen

• Application of bacteriophages and their lytic enzymes to control Clostridium perfringens is one potential approach to reduce the pathogen on poultry farms and in poultry-processing facilities. Bacteriophages lytic for C. perfringens were isolated from sewage, feces and broiler intestinal contents and I[brvbar]CPV1, a virulent bacteriophage, was classified in the family Podoviridae. The purified virus had an icosahedral head and collar of approximately 42nm and 23nm in diameter, respectively, with a structurally complex tail of 37nm lengthwise and a basal plate of 30nm. The I[brvbar]CPV1 double-stranded DNA genome was 16,747 base pairs with a GC composition of 30.5%. Twenty-two open reading frames (ORFs) coding for putative peptides containing 30 or more amino acid residues were identified and analyzed in the genome. Amino acid sequences of the predicted proteins from the I[brvbar]CPV1 genome ORFs were compared with those from the NCBI database and potential functions of 12 proteins were predicted by sequence homology. Three putative proteins were similar to hypothetical proteins with unknown functions, whereas seven proteins did not have similarity with any known bacteriophage or bacterial proteins. Identified ORFs formed at least four genomic clusters that accounted for predicted proteins involved with replication of the viral DNA, its folding, production of structural components and lytic properties. One bacteriophage genome encoded lysin was predicted to share homology with N-acetylmuramoyl-l-alanine amidases and a second structural lysin was predicted to be a lysozyme-endopeptidase. These enzymes digest peptidoglycan of the bacterial cell wall and could be considered potential therapeutics to control C. perfringens.