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PMID:27766357
| Citation |
Maciejewska, B, Roszniowski, B, Espaillat, A, Kęsik-Szeloch, A, Majkowska-Skrobek, G, Kropinski, AM, Briers, Y, Cava, F, Lavigne, R and Drulis-Kawa, Z (2017) Klebsiella phages representing a novel clade of viruses with an unknown DNA modification and biotechnologically interesting enzymes. Appl. Microbiol. Biotechnol. 101:673-684 |
|---|---|
| Abstract |
Lytic bacteriophages and phage-encoded endolysins (peptidoglycan hydrolases) provide a source for the development of novel antimicrobial strategies. In the present study, we focus on the closely related (96 % DNA sequence identity) environmental myoviruses vB_KpnM_KP15 (KP15) and vB_KpnM_KP27 (KP27) infecting multidrug-resistant Klebsiella pneumoniae and Klebsiella oxytoca strains. Their genome organisation and evolutionary relationship are compared to Enterobacter phage phiEap-3 and Klebsiella phages Matisse and Miro. Due to the shared and distinct evolutionary history of these phages, we propose to create a new phage genus "Kp15virus" within the Tevenvirinae subfamily. In silico genome analysis reveals two unique putative homing endonucleases of KP27 phage, probably involved in unrevealed mechanism of DNA modification and resistance to restriction digestion, resulting in a broader host spectrum. Additionally, we identified in KP15 and KP27 a complete set of lysis genes, containing holin, antiholin, spanin and endolysin. By turbidimetric assays on permeabilized Gram-negative strains, we verified the ability of the KP27 endolysin to destroy the bacterial peptidoglycan. We confirmed high stability, absence of toxicity on a human epithelial cell line and the enzymatic specificity of endolysin, which was found to possess endopeptidase activity, cleaving the peptide stem between L-alanine and D-glutamic acid. |
| Links |
PubMed PMC5219037 Online version:10.1007/s00253-016-7928-3 |
| Keywords |
Bacteriophages/classification; Bacteriophages/enzymology; Bacteriophages/genetics; Bacteriophages/isolation & purification; DNA, Viral/chemistry; DNA, Viral/genetics; Endopeptidases/metabolism; Gene Order; Klebsiella oxytoca/virology; Klebsiella pneumoniae/virology; Myoviridae/classification; Myoviridae/enzymology; Myoviridae/genetics; Myoviridae/isolation & purification; Phylogeny; Sequence Homology |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004175: endopeptidase activity |
ECO:0000314: |
F |
Figure 4 AND S4 show the digestion of E. coli peptidoglycan sacculus KP27 endolysin and shows that KP27 endolysin is a l-alanyl-d-glutamate endopeptidase. It further shows that KP27 endolysins has an endopeptidase activity cleaving between l-Ala and d-Glu of the stem peptide and no d-alanyl-d-alanine carboxypeptidase activity. |
complete | ||||
Notes
See also
References
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