GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
PMID:26506338
| Citation |
Lai, MJ, Liu, CC, Jiang, SJ, Soo, PC, Tu, MH, Lee, JJ, Chen, YH and Chang, KC (2015) Antimycobacterial Activities of Endolysins Derived From a Mycobacteriophage, BTCU-1. Molecules 20:19277-90 |
|---|---|
| Abstract |
The high incidence of Mycobacterium infection, notably multidrug-resistant M. tuberculosis infection, has become a significant public health concern worldwide. In this study, we isolate and analyze a mycobacteriophage, BTCU-1, and a foundational study was performed to evaluate the antimycobacterial activity of BTCU-1 and its cloned lytic endolysins. Using Mycobacterium smegmatis as host, a mycobacteriophage, BTCU-1, was isolated from soil in eastern Taiwan. The electron microscopy images revealed that BTCU-1 displayed morphology resembling the Siphoviridae family. In the genome of BTCU-1, two putative lytic genes, BTCU-1_ORF7 and BTCU-1_ORF8 (termed lysA and lysB, respectively), were identified, and further subcloned and expressed in Escherichia coli. When applied exogenously, both LysA and LysB were active against M. smegmatis tested. Scanning electron microscopy revealed that LysA and LysB caused a remarkable modification of the cell shape of M. smegmatis. Intracellular bactericidal activity assay showed that treatment of M. smegmatis-infected RAW 264.7 macrophages with LysA or LysB resulted in a significant reduction in the number of viable intracellular bacilli. These results indicate that the endolysins derived from BTCU-1 have antimycobacterial activity, and suggest that they are good candidates for therapeutic/disinfectant agents to control mycobacterial infections. |
| Links |
PubMed Online version:10.3390/molecules201019277 |
| Keywords |
Amino Acid Sequence; Animals; Antitubercular Agents/chemistry; Antitubercular Agents/isolation & purification; Antitubercular Agents/pharmacology; Bacteriophages/enzymology; Bacteriophages/ultrastructure; Conserved Sequence; Endopeptidases/chemistry; Endopeptidases/isolation & purification; Endopeptidases/pharmacology; Mice; Microbial Sensitivity Tests; Microbial Viability/drug effects; Molecular Sequence Data; Mycobacterium smegmatis/drug effects; Mycobacterium smegmatis/virology; RAW 264.7 Cells; Viral Proteins/chemistry; Viral Proteins/isolation & purification; Viral Proteins/pharmacology |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0044659: cytolysis by virus of host cell |
ECO:0000314: |
P |
Figure 2B shows LysB shares about 63% identity with another previously characterized LysB (gp12) in mycobacteriophage D29, which has been proved to be a mycolylarabinogalactan esterase (Payne et al., 2009). It cleaves the ester linkage joining the mycolic acid-rich outer membrane to arabinogalactan, releasing free mycolic acids. Figure 3B shows that LysB has antibacterial activity on M. smegmatis. |
complete | ||||
| GO:0008233: peptidase activity |
ECO:0000314: |
F |
Figure 2A suggests that LysA contains an N-terminal peptidase domain, a central catalytic GH19 (glycoside hydrolase family 19) domain, and a C-terminal cell wall binding domain. Figure 3B shows that LysA has antibacterial activity on M. smegmatis. |
complete | ||||
Notes
See also
References
See Help:References for how to manage references in GONUTS.
