ArticleThe Journal of biological chemistry2007
Manduca sexta hemolymph proteinase 21 activates prophenoloxidase-activating proteinase 3 in an insect innate immune response proteinase cascade.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 117 citations in OpenAlex.
- Hemolymph protease-17b activates proHP6 to stimulate melanization and Toll signaling in Manduca sexta.Insect biochemistry and molecular biology · 2024Article
- Identification of immunity-related genes distinctly regulated by Manduca sexta Spӓtzle-1/2 and Escherichia coli peptidoglycan.Insect biochemistry and molecular biology · 2024Article
- Serpin-4 Negatively Regulates Prophenoloxidase Activation and Antimicrobial Peptide Synthesis in the Silkworm,International journal of molecular sciences · 2023Article
- An evolutionarily conserved serine protease network mediates melanization and Toll activation inScience advances · 2023Article
- A fat body transcriptome analysis of the immune responses of Rhodnius prolixus to artificial infections with bacteria.Parasites & vectors · 2022Article
- A Kazal-type serine protease inhibitor mediates innate immunity in wild silkworm Actias selene Hübner.Journal of biosciences · 2022Article
- Article
- Activation of the Host Immune Response inInsects · 2021Article
- The CLIP-domain serine protease CLIPC9 regulates melanization downstream of SPCLIP1, CLIPA8, and CLIPA28 in the malaria vector Anopheles gambiae.PLoS pathogens · 2020Article
- Hemolymph protease-5 links the melanization and Toll immune pathways in the tobacco hornworm,Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Identification of a Conserved Prophenoloxidase Activation Pathway in Cotton BollwormFrontiers in immunology · 2020Article
- CLIPB10 is a Terminal Protease in the Regulatory Network That Controls Melanization in the African Malaria MosquitoFrontiers in cellular and infection microbiology · 2020Article
- Effect of food plants onToxicology reports · 2020Article
- Inhibition of immune pathway-initiating hemolymph protease-14 by Manduca sexta serpin-12, a conserved mechanism for the regulation of melanization and Toll activation in insects.Insect biochemistry and molecular biology · 2020Article
- Role of a serine protease gene (AccSp1) from Apis cerana cerana in abiotic stress responses and innate immunity.Cell stress & chaperones · 2019Article
- Building a platform for predicting functions of serine protease-related proteins in Drosophila melanogaster and other insects.Insect biochemistry and molecular biology · 2018Article
- Clip domain prophenoloxidase activating protease is required for Ostrinia furnacalis Guenée to defend against bacterial infection.Developmental and comparative immunology · 2018Article
- Manduca sexta hemolymph protease-2 (HP2) activated by HP14 generates prophenoloxidase-activating protease-2 (PAP2) in wandering larvae and pupae.Insect biochemistry and molecular biology · 2018Article
- Manduca sexta serpin-12 controls the prophenoloxidase activation system in larval hemolymph.Insect biochemistry and molecular biology · 2018Article
- The initial analysis of a serine proteinase gene (AccSp10) from Apis cerana cerana: possible involvement in pupal development, innate immunity and abiotic stress responses.Cell stress & chaperones · 2017Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Melanization, an insect immune response, requires a set of hemolymph proteins including pathogen recognition proteins that initiate the response, a cascade of mostly unknown serine proteinases, and phenoloxidase. Until now, only initial and final proteinases in the pathways have been conclusively identified. Four such proteinases have been purified from the larval hemolymph of Manduca sexta: hemolymph proteinase 14 (HP14), which autoactivates in the presence of microbial surface components, and three prophenoloxidase-activating proteinases (PAP1-3). In this study, we have used two complementary approaches to identify a serine proteinase that activates proPAP3. Partial purification from hemolymph of an activator of proPAP3 resulted in an active fraction with two abundant polypeptides of approximately 32 and approximately 37 kDa. Labeling of these polypeptides with a serine proteinase inhibitor, diisopropyl fluorophosphate, indicated that they were active serine proteinases. N-terminal sequencing revealed that both were cleaved forms of the previously identified hemolymph serine proteinase, HP21. Surprisingly, cleavage of proHP21 had occurred not at the predicted activation site but more N-terminal to it. In vitro reactions carried out with purified HP14 (which activates proHP21), proHP21, proPAP3, and site-directed mutant forms of the latter two proteinases confirmed that HP21 activates proPAP3 by limited proteolysis. Like the HP21 products purified from hemolymph, HP21 that was activated by HP14 in the in vitro reactions was not cleaved at its predicted activation site.
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