ArticlePloS one2012
Biochemical characterization of Anopheles gambiae SRPN6, a malaria parasite invasion marker in mosquitoes.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- TheProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Response of the mosquito immune system and symbiotic bacteria to pathogen infection.Parasites & vectors · 2024Review
- Parasitoid Serpins Evolve Novel Functions to Manipulate Host Homeostasis.Molecular biology and evolution · 2023Article
- A Genome-Wide Analysis of Serine Protease Inhibitors inInternational journal of molecular sciences · 2023Article
- Article
- Fasciola hepatica serine protease inhibitor family (serpins): Purposely crafted for regulating host proteases.PLoS neglected tropical diseases · 2020Article
- Identification and characterization of serine protease inhibitors in a parasitic wasp, Pteromalus puparum.Scientific reports · 2017Article
- Characterization and expression profiling of serine protease inhibitors in the diamondback moth, Plutella xylostella (Lepidoptera: Plutellidae).BMC genomics · 2017Article
- Serpins in arthropod biology.Seminars in cell & developmental biology · 2017Review
- CLIPB8 is part of the prophenoloxidase activation system in Anopheles gambiae mosquitoes.Insect biochemistry and molecular biology · 2016Article
- Plasmodium falciparum evades mosquito immunity by disrupting JNK-mediated apoptosis of invaded midgut cells.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Comparison of two serpins of Clonorchis sinensis by bioinformatics, expression, and localization in metacercaria.Pathogens and global health · 2014Article
- Amblyomma americanum tick saliva serine protease inhibitor 6 is a cross-class inhibitor of serine proteases and papain-like cysteine proteases that delays plasma clotting and inhibits platelet aggregation.Insect molecular biology · 2013Article
- Enterobacter-activated mosquito immune responses to Plasmodium involve activation of SRPN6 in Anopheles stephensi.PloS one · 2013Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Serine proteinase inhibitors of the serpin family are well known as negative regulators of hemostasis, thrombolysis and innate immune responses. Additionally, non-inhibitory serpins serve functions as chaperones, hormone transporters, or anti-angiogenic factors. In the African malaria mosquito, Anopheles gambiae s.s., at least three serpins (SRPNs) are implicated in the innate immune response against malaria parasites. Based on reverse genetic and cell biological analyses, AgSRPN6 limits parasite numbers and transmission and has been postulated to control melanization and complement function in mosquitoes. This study aimed to characterize AgSRPN6 biophysically and determine its biochemical mode of action. The structure model of AgSRPN6, as predicted by I-Tasser showed the protein in the native serpin fold, with three central β-sheets, nine surrounding α-helices, and a protruding reactive center loop. This structure is in agreement with biophysical and functional data obtained from recombinant (r) AgSRPN6, produced in Escherichia coli. The physical properties of purified rAgSRPN6 were investigated by means of analytical ultracentrifugation, circular dichroism, and differential scanning calorimetry tools. The recombinant protein exists predominantly as a monomer in solution, is composed of a mixture of α-helices and β-sheets, and has a mid-point unfolding temperature of 56°C. Recombinant AgSRPN6 strongly inhibited porcine pancreatic kallikrein and to a lesser extent bovine pancreatic trypsin in vitro. Furthermore, rAgSRPN6 formed inhibitory, SDS-stable, higher molecular weight complexes with prophenoloxidase-activating proteinase (PAP)1, PAP3, and Hemolymph protein (HP)6, which are required for melanization in the lepidopteran model organism, Manduca sexta. Taken together, our results strongly suggest that AgSRPN6 takes on a native serpin fold and is an inhibitor of trypsin-like serine proteinases.
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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.