ArticleProceedings of the National Academy of Sciences of the United States of America2015
Initiating protease with modular domains interacts with β-glucan recognition protein to trigger innate immune response in insects.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 62 citations in OpenAlex.
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- 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
- Immune-Related Genes in the Honey Bee MiteInsects · 2025Article
- Innate Immunity in Insects: The Lights and Shadows of Phenoloxidase System Activation.International journal of molecular sciences · 2025Review
- CLIPA protein pairs function as cofactors for prophenoloxidase activation in Anopheles gambiae.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
- Identification of immunity-related genes distinctly regulated by Manduca sexta Spӓtzle-1/2 and Escherichia coli peptidoglycan.Insect biochemistry and molecular biology · 2024Article
- Immune Gene Repertoire of Soft Scale Insects (Hemiptera: Coccidae).International journal of molecular sciences · 2024Article
- The accumulation of modular serine protease mediated by a novel circRNA sponging miRNA increases Aedes aegypti immunity to fungus.BMC biology · 2024Article
- Serine protease homolog pairs CLIPA4-A6, A4-A7Δ, and A4-A12 act as cofactors for proteolytic activation of prophenoloxidase-2 and -7 in Anopheles gambiae.Insect biochemistry and molecular biology · 2024Article
- An evolutionarily conserved serine protease network mediates melanization and Toll activation inScience advances · 2023Article
- Recognition of Arboviruses by the Mosquito Immune System.Biomolecules · 2023Review
- Identification and gene expression analysis of serine proteases and their homologs in the Asian corn borer Ostrinia furnacalis.Scientific reports · 2023Article
- A mechanistic analysis of bacterial recognition and serine protease cascade initiation in larval hemolymph of Manduca sexta.Insect biochemistry and molecular biology · 2022Article
- A Short-Type Peptidoglycan Recognition Protein 1 (PGRP1) Is Involved in the Immune Response in Asian Corn Borer,International journal of molecular sciences · 2021Article
- Distinct Responses ofJournal of immunology (Baltimore, Md. : 1950) · 2021Article
- Immune mediation of HMG-like DSP1 via Toll-Spätzle pathway and its specific inhibition by salicylic acid analogs.PLoS pathogens · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The autoactivation of an initiating serine protease upon binding of pattern recognition proteins to pathogen surfaces is a crucial step in eliciting insect immune responses such as the activation of Toll and prophenoloxidase pathways. However, the molecular mechanisms responsible for autoactivation of the initiating protease remains poorly understood. Here, we investigated the molecular basis for the autoactivation of hemolymph protease 14 (HP14), an initiating protease in hemolymph of Manduca sexta, upon the binding of β-1,3-glucan by its recognition protein, βGRP2. Biochemical analysis using HP14 zymogen (proHP14), βGRP2, and the recombinant proteins as truncated forms showed that the amino-terminal modular low-density lipoprotein receptor class A (LA) domains within HP14 are required for proHP14 autoactivation that is stimulated by its interaction with βGRP2. Consistent with this result, recombinant LA domains inhibit the activation of proHP14 and prophenoloxidase, likely by competing with the interaction between βGRP2 and LA domains within proHP14. Using surface plasmon resonance, we demonstrated that immobilized LA domains directly interact with βGRP2 in a calcium-dependent manner and that high-affinity interaction requires the C-terminal glucanase-like domain of βGRP2. Importantly, the affinity of LA domains for βGRP2 increases nearly 100-fold in the presence of β-1,3-glucan. Taken together, these results present the first experimental evidence to our knowledge that LA domains of an insect modular protease and glucanase-like domains of a βGRP mediate their interaction, and that this binding is essential for the protease autoactivation. Thus, our study provides important insight into the molecular basis underlying the initiation of protease cascade in insect immune responses.
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