ArticleThe Journal of biological chemistry2011
Structure-function analysis of grass clip serine protease involved in Drosophila Toll pathway activation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- An evolutionarily conserved serine protease network mediates melanization and Toll activation inScience advances · 2023Article
- Nitric Oxide-Induced Calcineurin A Mediates Antimicrobial Peptide Production Through the IMD Pathway.Frontiers in immunology · 2022Article
- Roles of the clip domains of two protease zymogens in the coagulation cascade in horseshoe crabs.The Journal of biological chemistry · 2020Article
- Spatially Restricted Regulation of Spätzle/Toll Signaling during Cell Competition.Developmental cell · 2018Article
- Transcriptome-wide responses of adult melon thrips (Thrips palmi) associated with capsicum chlorosis virus infection.PloS one · 2018Article
- Serine protease SP105 activates prophenoloxidase in Asian corn borer melanization, and is regulated by serpin-3.Scientific reports · 2017Article
- Arthropod Innate Immune Systems and Vector-Borne Diseases.Biochemistry · 2017Review
- Clip-domain serine proteases as immune factors in insect hemolymph.Current opinion in insect science · 2015Article
- Sequence conservation, phylogenetic relationships, and expression profiles of nondigestive serine proteases and serine protease homologs in Manduca sexta.Insect biochemistry and molecular biology · 2015Article
- Switching between humoral and cellular immune responses in Drosophila is guided by the cytokine GBP.Nature communications · 2014Article
- Lifestyle and host defense mechanisms of the dung beetle, Euoniticellus intermedius: the toll signaling pathway.Journal of insect science (Online) · 2013Article
- Bacteria- and IMD pathway-independent immune defenses against Plasmodium falciparum in Anopheles gambiae.PloS one · 2013Article
- Crystal structure of Diedel, a marker of the immune response of Drosophila melanogaster.PloS one · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Grass is a clip domain serine protease (SP) involved in a proteolytic cascade triggering the Toll pathway activation of Drosophila during an immune response. Epistasic studies position it downstream of the apical protease ModSP and upstream of the terminal protease Spaetzle-processing enzyme. Here, we report the crystal structure of Grass zymogen. We found that Grass displays a rather deep active site cleft comparable with that of proteases of coagulation and complement cascades. A key distinctive feature is the presence of an additional loop (75-loop) in the proximity of the activation site localized on a protruding loop. All biochemical attempts to hydrolyze the activation site of Grass failed, strongly suggesting restricted access to this region. The 75-loop is thus proposed to constitute an original mechanism to prevent spontaneous activation. A comparison of Grass with clip serine proteases of known function involved in analogous proteolytic cascades allowed us to define two groups, according to the presence of the 75-loop and the conformation of the clip domain. One group (devoid of the 75-loop) contains penultimate proteases whereas the other contains terminal proteases. Using this classification, Grass appears to be a terminal protease. This result is evaluated according to the genetic data documenting Grass function.
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