Properties of the peptidoglycan-degrading enzyme of the ϕPMG1 bacteriophage

O. V. Chertkov, R. N. Chuprov-Netochin, S. V. Legotskiy,N. N. Sykilinda,M. M. Shneider, M. A. Ivanova,E. A. Pleteneva,O. V. Shaburova, M. B. Burkal’tseva, E. S. Kostryukova,V. N. Lazarev,N. L. Klyachko,K. A. Miroshnikov

Russian Journal of Bioorganic Chemistry(2011)

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Abstract
The ϕPMG1 bacteriophage was isolated. It is characterized by certain peculiarities of the lytic infection cycle and forms a halo (clear zone) around negative colonies. The phage was studied with regard to its potential use in therapeutic phage preparations and as a source of peptidoglycan- and lipopolysacchraide-degrading enzymes. Partial sequencing of the ϕPMG1 genome revealed a high degree of homology with the D3 moderate bacteriophage. An open reading frame coding for a lytic transglycosylase has been identified in ϕPMG1 genome. The enzyme has been obtained in a recombinant form, and its activity and substrate specificity have been characterized.
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Key words
Pseudomonas aeruginosa,bacteriophage,peptidoglycan-degrading enzyme,transglycosylase
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