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Bioorg Khim ; 37(6): 807-14, 2011.
Article in Russian | MEDLINE | ID: mdl-22497079

ABSTRACT

The properties of the isolated Pseudomonas aeruginosa bacteriophage phiPMG1 include the lytic infection cycle, and the formation of a broad halo (semi-transparent zone) around the plaques. We consider phiPMG1 as a potential member of therapeutic cocktails of live phages, and as a source of peptidoglycan and lipopolysaccharide degrading enzymes. Partial sequencing of phiPMG1 genome has revealed high similarity with known temperate P. aeruginosa phage D3. An open reading frame encoding lytic transglycosilase was identified in the genome. This enzyme PMG MUR was obtained in recombinant form, and its activity and substrate specificity has been studied.


Subject(s)
Bacteriophages/enzymology , N-Acetylmuramoyl-L-alanine Amidase/genetics , Pseudomonas aeruginosa/virology , Amino Acid Sequence , Bacteriophages/ultrastructure , Enzyme Stability , Genome , Humans , Molecular Sequence Data , N-Acetylmuramoyl-L-alanine Amidase/chemistry , N-Acetylmuramoyl-L-alanine Amidase/metabolism , Pseudomonas aeruginosa/genetics , Sequence Analysis, DNA
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