ArticleToxins2015
Molecular Cloning and Functional Studies of Two Kazal-Type Serine Protease Inhibitors Specifically Expressed by Nasonia vitripennis Venom Apparatus.
Article in Toxins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Conkazal-M1 from the MKAVA family of conotoxins: A dual-function protease inhibitor and neuroactive peptide.Protein science : a publication of the Protein Society · 2026Article
- Multi-omics characterization of toxin expression and producing organs in the predatory gastropods Monoplex corrugatus and Stramonita haemastoma.BMC genomics · 2026Article
- Conkazal-M1 from the MKAVA family of conotoxins - a dual-function protease inhibitor and neuroactive peptide.bioRxiv : the preprint server for biology · 2025Article
- Insights into platypus crural gland transcriptomics - venom and beyond.BMC genomics · 2025Article
- Innate Immunity in Insects: The Lights and Shadows of Phenoloxidase System Activation.International journal of molecular sciences · 2025Review
- Molecular Characterization and Functional Analysis of the Dipeptidyl Peptidase IV from Venom of the EctoparasitoidToxins · 2023Article
- Host Transcriptome Analysis ofInsects · 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
- Identification and functional analysis of serine protease inhibitor gene family ofFrontiers in physiology · 2023Article
- A Kazal-type serine protease inhibitor mediates innate immunity in wild silkworm Actias selene Hübner.Journal of biosciences · 2022Article
- Proteo-Transcriptomic Characterization ofToxins · 2021Article
- An integrated transcriptomic and proteomic approach to identify the main Torymus sinensis venom components.Scientific reports · 2021Article
- Transcriptional profiling and physiological roles of Aedes aegypti spermathecal-related genes.BMC genomics · 2020Article
- Venomics of the ectoparasitoid wasp Bracon nigricans.BMC genomics · 2020Article
- Identification and Comparative Analysis of Venom Proteins in a Pupal Ectoparasitoid,Frontiers in physiology · 2020Article
- Cloning and Immunosuppressive Properties of an Acyl-Activating Enzyme from the Venom Apparatus ofToxins · 2019Article
- The Pupal EctoparasitoidFrontiers in physiology · 2019Article
- Are Fireworms Venomous? Evidence for the Convergent Evolution of Toxin Homologs in Three Species of Fireworms (Annelida, Amphinomidae).Genome biology and evolution · 2018Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two cDNA sequences of Kazal-type serine protease inhibitors (KSPIs) in Nasonia vitripennis, NvKSPI-1 and NvKSPI-2, were characterized and their open reading frames (ORFs) were 198 and 264 bp, respectively. Both NvKSPI-1 and NvKSPI-2 contained a typical Kazal-type domain. Real-time quantitative PCR (RT-qPCR) results revealed that NvKSPI-1 and NvKSPI-2 mRNAs were mostly detected specifically in the venom apparatus, while they were expressed at lower levels in the ovary and much lower levels in other tissues tested. In the venom apparatus, both NvKSPI-1 and NvKSPI-2 transcripts were highly expressed on the fourth day post eclosion and then declined gradually. The NvKSPI-1 and NvKSPI-2 genes were recombinantly expressed utilizing a pGEX-4T-2 vector, and the recombinant products fused with glutathione S-transferase were purified. Inhibition of recombinant GST-NvKSPI-1 and GST-NvKSPI-2 to three serine protease inhibitors (trypsin, chymotrypsin, and proteinase K) were tested and results showed that only NvKSPI-1 could inhibit the activity of trypsin. Meanwhile, we evaluated the influence of the recombinant GST-NvKSPI-1 and GST-NvKSPI-2 on the phenoloxidase (PO) activity and prophenoloxidase (PPO) activation of hemolymph from a host pupa, Musca domestica. Results showed PPO activation in host hemolymph was inhibited by both recombinant proteins; however, there was no significant inhibition on the PO activity. Our results suggested that NvKSPI-1 and NvKSPI-2 could inhibit PPO activation in host hemolymph and trypsin activity in vitro.
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