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

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

Proceedings of the National Academy of Sciences of the United States of America (2009-07-11)
Nicolas Buchon, Mickael Poidevin, Hyun-Mi Kwon, Aurélien Guillou, Valentin Sottas, Bok-Luel Lee, Bruno Lemaitre
ANOTACE

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.

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Sigma-Aldrich
Protease from Bacillus sp., liquid, ≥16 U/g
Sigma-Aldrich
Protease from Aspergillus oryzae, ≥500 U/g