Properties of the peptidoglycan-degrading enzyme of the Pseudomonas aeruginosa ϕPMG1 bacteriophage

The ϕPMG1 Pseudomonas aeruginosa 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 p...

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Bibliographic Details
Published in:Russian journal of bioorganic chemistry 2011-11, Vol.37 (6), p.732-738
Main Authors: Chertkov, O. V., Chuprov-Netochin, R. N., Legotskiy, S. V., Sykilinda, N. N., Shneider, M. M., Ivanova, M. A., Pleteneva, E. A., Shaburova, O. V., Burkal’tseva, M. B., Kostryukova, E. S., Lazarev, V. N., Klyachko, N. L., Miroshnikov, K. A.
Format: Article
Language:English
Subjects:
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Life Sciences
Organic Chemistry
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Summary:The ϕPMG1 Pseudomonas aeruginosa 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.
ISSN:1068-1620
1608-330X
DOI:10.1134/S1068162011060057