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closeHost-pathogen parallelism
Posted by ramy on 14 Apr 2009 at 20:34 GMT
This article presents very interesting findings. It is amazing that the bacterial protease SpeB is acting similarly both on the bacterial (self) and host proteins. As the authors pointed out, SpeB is a braod-spectrum protease; still, few very important proteins either escape its action or are partially degraded by it, often becoming more active. It has been shown how SpeB activates some of the S. pyogenes surface virulence factors by post-translational degradation, e.g., the antiphagocytic M protein (e.g., http://www.jbc.org/cgi/co...) and how it acts differentially on streptococcal toxins, e.g. MF/SpeF (http://www.journals.uchic...) and <a href="http://www.jbc.org/cgi/co...> are readily degradable in contrast to the pyrogenic exotoxin A, SpeA that resists degradation. Now the same thing is shown to happen at the host protein level as has been demonstrated here by Egesten et al.
This is a good example of the diversification within protein families leading to their evolution.