ArticleInsect biochemistry and molecular biology2016
In search of a function of Manduca sexta hemolymph protease-1 in the innate immune system.
Article in Insect biochemistry and molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Unveiling the Multifaceted Role of HP6: A Critical Regulator of Humoral Immunity inInternational journal of molecular sciences · 2025Article
- Pattern recognition, hemolymph protease-14 activation, and enhancement of lysozyme-mediated bacteria killing by soluble peptidoglycan recognition proteins in Manduca sexta.Insect biochemistry and molecular biology · 2025Article
- Hemolymph protease-17b activates proHP6 to stimulate melanization and Toll signaling in Manduca sexta.Insect biochemistry and molecular biology · 2024Article
- Two venom serpins from the parasitoid wasp Microplitis mediator inhibit the host prophenoloxidase activation and antimicrobial peptide synthesis.Insect biochemistry and molecular biology · 2023Article
- Dual roles and evolutionary implications of P26/poxin in antagonizing intracellular cGAS-STING and extracellular melanization immunity.Nature communications · 2022Article
- Article
- 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
- 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
- Serpin-9 and -13 regulate hemolymph proteases during immune responses of Manduca sexta.Insect biochemistry and molecular biology · 2017Article
- Inhibition of melanization by serpin-5 and serpin-9 promotes baculovirus infection in cotton bollworm Helicoverpa armigera.PLoS pathogens · 2017Article
- Hemolymph proteins of Anopheles gambiae larvae infected by Escherichia coli.Developmental and comparative immunology · 2017Article
- Manduca sexta hemolymph protease-1, activated by an unconventional non-proteolytic mechanism, mediates immune responses.Insect biochemistry and molecular biology · 2017Article
- Prophenoloxidase activation and antimicrobial peptide expression induced by the recombinant microbe binding protein of Manduca sexta.Insect biochemistry and molecular biology · 2017Article
- Article
- Solution Structure and Expression Profile of an Insect Cytokine: Manduca sexta Stress Response Peptide-2.Protein and peptide letters · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Extracellular serine protease cascades mediate immune signaling and responses in insects. In the tobacco hornworm Manduca sexta, nearly 30 serine proteases (SPs) and their homologs (SPHs) are cloned from hemocytes and fat body. Some of them participate in prophenoloxidase (proPO) activation and proSpätzle processing. Here we report the cDNA cloning of hemolymph protease-1b (HP1b), which is 90% identical and 95% similar to HP1a (formerly HP1). The HP1a and HP1b mRNA levels in hemocytes was down- and up-regulated after an immune challenge, respectively. Quantitative real-time polymerase chain reactions revealed their tissue-specific and development-dependent expression, mostly in hemocytes of the feeding larvae. We isolated HP1 precursor (proHP1) from larval hemolymph and observed micro-heterogeneity caused by N-linked glycosylation. Supplementation of the purified proHP1 to plasma samples from naïve larvae or induced ones injected with bacteria caused a small PO activity increase, much lower than those elicited by recombinant proHP1a/b, but no proteolytic cleavage was detected in the zymogens. Incubation of proHP1a/b or their catalytic domains with a cationic detergent, cetylpyridinium chloride, induced an amidase activity that hydrolyzed LDLH-p-nitroanilide. Since LDLH corresponds to the P4-P1 region before the proteolytic activation site of proHP6, we propose that the active but uncleaved proHP1 may cut proHP6 to generate HP6 that in turn activates proPAP1 and proHP8. The catalytic domain of HP1a/b, which by itself does not activate purified proHP6 or hydrolyze LDLH-p-nitroanilide, somehow generated active HP6, HP8, PAP1 and PO in plasma. Together, these results indicate that proHP1 participates in the proPO activation system, although detailed mechanism needs further exploration.
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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.