Abstract

The antifungal defense of Drosophila is controlled by the spaetzle/Toll/cactus gene cassette. Here, a loss-of-function mutation in the gene encoding a blood serine protease inhibitor, Spn43Ac, was shown to lead to constitutive expression of the antifungal peptide drosomycin, and this effect was mediated by the spaetzle and Toll gene products. Spaetzle was cleaved by proteolytic enzymes to its active ligand form shortly after immune challenge, and cleaved Spaetzle was constitutively present in Spn43Ac -deficient flies. Hence, Spn43Ac negatively regulates the Toll signaling pathway, and Toll does not function as a pattern recognition receptor in the Drosophila host defense.

Keywords

SerpinSerine proteaseBiologyGeneToll-like receptorImmune systemInnate immune systemCell biologyFunction (biology)ReceptorProteaseAntifungalEnzymeMicrobiologyGeneticsBiochemistry

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Publication Info

Year
1999
Type
article
Volume
285
Issue
5435
Pages
1917-1919
Citations
434
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Closed

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Elena A. Levashina, Emma Langley, Clare Green et al. (1999). Constitutive Activation of Toll-Mediated Antifungal Defense in Serpin-Deficient <i>Drosophila</i>. Science , 285 (5435) , 1917-1919. https://doi.org/10.1126/science.285.5435.1917

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DOI
10.1126/science.285.5435.1917