ArticleThe Journal of biological chemistry2009
Functions of Manduca sexta hemolymph proteinases HP6 and HP8 in two innate immune pathways.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed, 169 citations in OpenAlex.
- Partial reconstitution of the prophenoloxidase activation system inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Penaeus monodon fibrinogen-related lectin interacts with lipopolysaccharide and β-1,3-glucan binding protein to activate the innate immune system.The Biochemical journal · 2025Article
- Morphotype-Specific Antifungal Defense inInsects · 2025Article
- Unveiling the Multifaceted Role of HP6: A Critical Regulator of Humoral Immunity inInternational journal of molecular sciences · 2025Article
- The expanded immunoregulatory protease network in mosquitoes is governed by gene coexpression.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A phytoplasma effector suppresses insect melanization immune response to promote pathogen persistent transmission.Science advances · 2025Article
- Hemolymph protease-17b activates proHP6 to stimulate melanization and Toll signaling in Manduca sexta.Insect biochemistry and molecular biology · 2024Article
- Type VI secretion systems promote intraspecific competition and host interactions in a bee gut symbiont.Proceedings of the National Academy of Sciences of the United States of America · 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
- Serpin-1a and serpin-6 regulate the Toll pathway immune homeostasis by synergistically inhibiting the Spätzle-processing enzyme CLIP2 in silkworm, Bombyx mori.PLoS pathogens · 2023Article
- Mechanisms and roles of the first stage of nodule formation in lepidopteran insects.Journal of insect science (Online) · 2023Article
- Two venom serpins from the parasitoid wasp Microplitis mediator inhibit the host prophenoloxidase activation and antimicrobial peptide synthesis.Insect biochemistry and molecular biology · 2023Article
- Preferential binding of DAP-PGs by major peptidoglycan recognition proteins found in cell-free hemolymph of Manduca sexta.Insect biochemistry and molecular biology · 2022Article
- A fat body transcriptome analysis of the immune responses of Rhodnius prolixus to artificial infections with bacteria.Parasites & vectors · 2022Article
- Advances in the Immune Regulatory Role of Non-Coding RNAs (miRNAs and lncRNAs) in Insect-Pathogen Interactions.Frontiers in immunology · 2022Review
- Article
- Serpin-4 Facilitates Baculovirus Infection by Inhibiting Melanization in Asian Corn Borer,Frontiers in immunology · 2022Article
- Nitric Oxide-Induced Calcineurin A Mediates Antimicrobial Peptide Production Through the IMD Pathway.Frontiers in immunology · 2022Article
16 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Serine proteinases in insect plasma have been implicated in two types of immune responses; that is, activation of prophenoloxidase (proPO) and activation of cytokine-like proteins. We have identified more than 20 serine proteinases in hemolymph of the tobacco hornworm, Manduca sexta, but functions are known for only a few of them. We report here functions of two additional M. sexta proteinases, hemolymph proteinases 6 and 8 (HP6 and HP8). HP6 and HP8 are each composed of an amino-terminal clip domain and a carboxyl-terminal proteinase domain. HP6 is an apparent ortholog of Drosophila Persephone, whereas HP8 is most similar to Drosophila and Tenebrio spätzle-activating enzymes, all of which activate the Toll pathway. proHP6 and proHP8 are expressed constitutively in fat body and hemocytes and secreted into plasma, where they are activated by proteolytic cleavage in response to infection. To investigate activation and biological activity of HP6 and HP8, we purified recombinant proHP8, proHP6, and mutants of proHP6 in which the catalytic serine was replaced with alanine, and/or the activation site was changed to permit activation by bovine factor Xa. HP6 was found to activate proPO-activating proteinase (proPAP1) in vitro and induce proPO activation in plasma. HP6 was also determined to activate proHP8. Active HP6 or HP8 injected into larvae induced expression of antimicrobial peptides and proteins, including attacin, cecropin, gloverin, moricin, and lysozyme. Our results suggest that proHP6 becomes activated in response to microbial infection and participates in two immune pathways; activation of PAP1, which leads to proPO activation and melanin synthesis, and activation of HP8, which stimulates a Toll-like pathway.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.