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PMID:24690638
| Citation |
Lim, JA, Shin, H, Heu, S and Ryu, S (2014) Exogenous lytic activity of SPN9CC endolysin against gram-negative bacteria. J. Microbiol. Biotechnol. 24:803-11 |
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| Abstract |
Concerns over drug-resistant bacteria have stimulated interest in developing alternative methods to control bacterial infections. Endolysin, a phage-encoded enzyme that breaks down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle, is reported to be effective for the control of bacterial pathogenic bacteria. Bioinformatic analysis of the SPN9CC bacteriophage genome revealed a gene that encodes an endolysin with a domain structure similar to those of the endolysins produced by the P1 and P22 coliphages. The SPN9CC endolysin was purified with a C-terminal oligo-histidine tag. The endolysin was relatively stable and active over a broad temperature range (from 24°C to 65°C). It showed maximal activity at 50°C, and its optimum pH range was from pH 7.5 to 8.5. The SPN9CC endolysin showed antimicrobial activity against only gram-negative bacteria and functioned by cutting the glycosidic bond of peptidoglycan. Interestingly, the SPN9CC endolysin could lyse intact gram-negative bacteria in the absence of EDTA as an outer membrane permeabilizer. The exogenous lytic activity of the SPN9CC endolysin makes it a potential therapeutic agent against gram-negative bacteria. |
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| Keywords |
Amino Acid Sequence; Anti-Bacterial Agents/chemistry; Anti-Bacterial Agents/pharmacology; Bacteriophages/chemistry; Bacteriophages/enzymology; Bacteriophages/genetics; Endopeptidases/chemistry; Endopeptidases/genetics; Endopeptidases/metabolism; Endopeptidases/pharmacology; Enzyme Stability; Gram-Negative Bacteria/drug effects; Hydrogen-Ion Concentration; Molecular Sequence Data; Protein Structure, Tertiary; Sequence Alignment |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0008932: lytic endotransglycosylase activity |
ECO:0000314: |
F |
Fig 4. Author analyzes endolysin target sites by isolating peptidoglycan from E. coli and treating it with SPN9CC endolysin. Different byproducts of the reactions were analyzed to determine glycosidase, amidase, and peptidase activity. Results conclusively showed that the lysin possesses glycosidase activity. Since glycosidase activity involves alteration of glycosides, it can be categorized as transglycosylase activity. The reaction product used to measure glycosidase activity was 1,6-anhydromuramic acid, which is indicative of cleavage within the peptidoglycan chain instead of cleavage at the ends. This shows that the lysin possesses endotransglycosylase activity. |
complete | ||||
Notes
See also
References
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