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Degradation of Citrobacter O-Serogroup Ci23Vi+ murein with Vi phages
Zentralblatt Fur Bakteriologie, Mikrobiologie, Und Hygiene. Series A, Medical Microbiology, Infectious Diseases, Virology, Parasitology
|October 1, 1984
Abstract:
Dialysable products resulting from the digestion of the Citrobacter O-Serogroup Ci23Vi+ murein with Vi phages show a decrease of their reducing power/muropeptides. It is accompanied with an increase of free amino groups amount/muropeptide when compared to the one obtained after the lysozyme treatment. It leads to a suggestion, that Vi phage particles possess two enzyme activities: "lysozyme-like" and deacetylase which might be a transacetylase.
Insights
Vi phages digest Citrobacter murein, reducing its power and increasing amino groups compared to lysozyme. This suggests Vi phages have "lysozyme-like" and deacetylase (transacetylase) activities.
Area of Science:
- Microbiology
- Enzymology
- Bacteriology
Background:
- Murein, a major component of bacterial cell walls, is susceptible to enzymatic digestion.
- Bacteriophages, viruses that infect bacteria, often possess enzymes that degrade host cell walls for replication.
- Lysozyme is a well-known enzyme that hydrolyzes peptidoglycan, a key component of murein.
Purpose of the Study:
- To investigate the enzymatic activities of Vi phages against Citrobacter murein.
- To compare the digestion products of Vi phage treatment with those of lysozyme treatment.
- To identify potential enzymatic mechanisms employed by Vi phages for host cell lysis.
Main Methods:
- Digestion of Citrobacter O-Serogroup Ci23Vi+ murein using purified Vi phages.
- Digestion of the same murein using lysozyme as a control.
- Analysis of dialysable products from both digestion methods.
- Quantification of reducing power and free amino groups in the resulting muropeptides.
Main Results:
- Vi phage digestion of murein resulted in a decrease in reducing power of muropeptides.
- Vi phage digestion led to an increase in the amount of free amino groups per muropeptide compared to lysozyme treatment.
- These changes suggest distinct enzymatic activities of Vi phages compared to lysozyme.
Conclusions:
- Vi phage particles exhibit enzymatic activities beyond simple hydrolysis.
- The observed changes indicate the presence of a "lysozyme-like" activity and a deacetylase activity, potentially a transacetylase, in Vi phages.
- These enzymatic capabilities likely contribute to the phage's life cycle and interaction with the bacterial host.