A single modular serine protease integrates signals from pattern-recognition receptors upstream of the Drosophila Toll pathway

The Drosophila Toll receptor does not interact directly with microbial determinants, but is instead activated by a cleaved form of the cytokine-like molecule Spätzle. During the immune response, Spätzle is processed by complex cascades of serine proteases, which are activated by secreted pattern-recognition receptors. Here, we demonstrate the essential role of ModSP, a modular serine protease, in the activation of the Toll pathway by gram-positive bacteria and fungi. Our analysis shows that ModSP integrates signals originating from the circulating recognition molecules GNBP3 and PGRP-SA and connects them to the Grass-SPE-Spätzle extracellular pathway upstream of the Toll receptor. It also reveals the conserved role of modular serine proteases in the activation of insect immune reactions.


Published in:
Proceedings of the National Academy of Sciences of the United States of America, 106, 30, 12442-7
Year:
2009
Publisher:
National Academy of Sciences
ISSN:
1091-6490
Keywords:
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 Record created 2010-09-17, last modified 2018-09-13

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