Serine protease persephone; Serine protease that plays a key role in innate immunity in response to Gram-positive bacterial and fungal proteases. Acts as a component of the Toll pathway upstream of protease spz processing enzyme SPE and Tl ligand spz. Nec regulates the cascade by inhibiting psh ; Belongs to the peptidase S1 family. CLIP subfamily.

Peptidoglycan-recognition protein SA; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to peptidoglycans (PGN) of Gram-positive bacteria and activating the Toll pathway upstream of spz activating enzyme SPE. Has no activity against Gram-negative bacteria and fungi. Shows some partial redundancy with PRPGP-SD in Gram-positive bacteria recognition. May act by forming a complex with GNBP1 that activates the proteolytic cleavage of Spatzle and the subsequent activation of Toll pathway. Binds to diaminopimelic acid-type tetrapeptide PGN (DAP-type PGN) an [...]

Spaetzle-processing enzyme heavy chain; Endopeptidase which plays a key role in innate immunity by cleaving Tl ligand spz and thereby activating the Toll pathway in response to fungal and Gram-positive bacterial infections. Acts downstream of pathogen recognition receptors PGRP-SA and GNBP1 and protease grass in response to Gram-positive bacterial infection. Acts downstream of protease psh in response to fungal infection. Belongs to the peptidase S1 family. CLIP subfamily.

Peptidoglycan-recognition protein SD; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to peptidoglycans (PGN) of Gram-positive bacteria and activating the Toll pathway. Has no activity against on Gram-negative bacteria and fungi. Shows some partial redundancy with PRPGP-SA in Gram-positive bacteria recognition. May act by activating the proteolytic cleavage of Spatzle and the subsequent activation of Toll pathway. Recognizes S.aureus PGN; Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Protein spaetzle C-106; Spatzle (spz) encodes a secreted protein which, after cleavage by an extracellular serine protease (encoded by ea or SPE), can induce the dimerization of the product of Tl, and the subsequent activation of the Toll pathway. It contributes to function of the Toll signaling cascade, which plays a key role in various developmental and immune processes, notably embryonic dorso-ventral patterning and regulation of antimicrobial peptides.

Protein immune deficiency; Essential for the imd/NF-kappa-B (Imd) humoral and epithelial immune response to Gram-negative bacteria. Functions as an adapter protein that transduces immunity signals from the activation of pathogen recognition receptors (PRRs) by bacterial infection to the Imd signaling pathway. Binding of diaminopimelic acid-type (DAP-type) bacterial peptidoglycans (PGN) causes multimerization or clustering of PGRP receptors which activate the Imd cascade probably by recruiting imd, Fadd and Dredd to the receptor complex. Once in proximity, Dredd cleaves imd in a Fadd-de [...]

Prophenoloxidase 1 (PPO1) encodes a protein produced by crystal cells (a type of hemocyte cell) and is involved in the melanization reaction, notably upon wounding. It is thought to be activated by proteolytic cleavage by the serine protease encoded by Hayan.

Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...]