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Tuning natural antimicrobials to improve their effectiveness at battling superbugs
Date:8/22/2011

e at each end. One domain is thought to be responsible for the specificity of the endolysin, allowing it to bind specifically to wall molecules unique to the bacterial species. This is what was thought to give the endolysin its specific host range. The other catalytic domain attacks the cell wall, causing lysis.

They produced shortened versions of the endolysin containing only one of these domains. The truncated CD27L containing only the catalytic domain showed a much higher activity against the C. difficile cells. Surprisingly, however, the truncated endolysin was still inactive on a range of other bacteria, even though the domain thought to make it specific had been removed.

Working with colleagues at the European Molecular Biology Laboratory (EMBL) in Hamburg, the structure of the catalytic domain was solved and used to design mutants to investigate what controls the specificity and activity of the endolysins. The researchers propose that the catalytic domain contributes to the specificity of the endolysin.

In the case of CD27L, binding to the cell wall is not a critical part of the activity of the endolysin, and from these results seems to reduce the activity. This fundamental science on the mode of action of endolysins establishes that in the development of valuable novel therapeutics it may be more appropriate to use truncated versions of endolysins.


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Contact: Andrew Chapple
andrew.chapple@nbi.ac.uk
01-603-251-490
Norwich BioScience Institutes
Source:Eurekalert  

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