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United States Department of Agriculture

Agricultural Research Service


item Volozhantsev, N
item Verevkin, V
item Bannov, V
item Krasilnikova, V
item Popova, A
item Zhilenkov, E
item Svetoch, E
item Seal, Bruce

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 7/28/2009
Publication Date: 10/19/2009
Citation: Volozhantsev, N.V., Verevkin, V.V., Bannov, V.A., Krasilnikova, V.M., Popova, A.V., Zhilenkov, E.L., Svetoch, E.A., Seal, B.S. 2009. THE GENOME SEQUENCE OF BACTERIOPHAGE CpV1 LYTIC FOR CLOSTRIDIUM PERFRINGENS. Meeting Abstract.

Interpretive Summary:

Technical Abstract: Application of bacteriophages and their lytic enzymes to control Clostri-dium perfringens is one potential approach to reduce the pathogen on poultry farms and in poultry-processing facilities. We have established a collection of 30 bacteriophages lytic for C. perfringens. These were isolated from sewage, feces and broiler intestinal contents. Phage CpV1 one of the more virulent phages was classified in the family Podoviridae. The phage had an icosahedral head and collar of approximately 42nm and 23 nm in diameter, respectively with a structurally complex tail of about 37nm lengthwise and a basal plate of 30 nm. To date the phage double-strand DNA genome was sequenced up to 16.2 kb pairs with a net GC composition of 31 %. Twenty-four open reading frames (ORFs) coding for putative peptides containing 30 or more amino acid residues were identified and analyzed. Amino acid sequences of the putative pro-teins from phage CpV1 were compared with those from the NCBI database and potential functions of 10 proteins were determined by sequence homology. Five putative proteins were similar to hypothetical proteins with unknown functions, whereas nine proteins did not have similarity with any phage or bacterial proteins. Identified ORFs form at least four genomic clusters accounted for replication of the phage DNA, its folding, production of structural components and lytic properties. One lysin was predicted to share homology with N-acetylmuramoyl-L-alanine amidases and a second lytic enzyme was predicted to be a lysozyme-endopeptidase. These enzymes digest peptidoglycan of the bacterial cell wall and are considered potential therapeutics to control C. perfringens.

Last Modified: 09/18/2017
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