ArticleInternational journal for parasitology2014
A blood meal-induced Ixodes scapularis tick saliva serpin inhibits trypsin and thrombin, and interferes with platelet aggregation and blood clotting.
Article in International journal for parasitology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 73 citations in OpenAlex.
- Chromosome-Scale Atlas ofGenes · 2026Article
- Feeding on different hosts displays different hemolymph protein compositions in Haemaphysalis qinghaiensis tick.Experimental & applied acarology · 2025Article
- Serpins in the Spotlight: Novel Bioinformatic Insights IntoBiochemistry research international · 2025Article
- A tick saliva serpin, IxsS17 inhibits host innate immune system proteases and enhances host colonization by Lyme disease agent.PLoS pathogens · 2024Article
- Article
- Protein profiling of hemolymph in Haemaphysalis flava ticks.Parasites & vectors · 2022Article
- Host Immune Responses to Salivary Components - A Critical Facet of Tick-Host Interactions.Frontiers in cellular and infection microbiology · 2022Review
- Serpins in Tick Physiology and Tick-Host Interaction.Frontiers in cellular and infection microbiology · 2022Review
- rDromaserpin: A Novel Anti-Hemostatic Serpin, from the Salivary Glands of the Hard TickToxins · 2021Article
- Proteomics informed by transcriptomics for a qualitative and quantitative analysis of the sialoproteome of adult Ornithodoros moubata ticks.Parasites & vectors · 2021Article
- Acquired tick resistance: The trail is hot.Parasite immunology · 2021Review
- Borrelia burgdorferi infection modifies protein content in saliva of Ixodes scapularis nymphs.BMC genomics · 2021Article
- Changing the Recipe: Pathogen Directed Changes in Tick Saliva Components.International journal of environmental research and public health · 2021Review
- Insights into the Role of Tick Salivary Protease Inhibitors during Ectoparasite-Host Crosstalk.International journal of molecular sciences · 2021Review
- Iripin-3, a New Salivary Protein Isolated FromFrontiers in immunology · 2021Article
- Amblyomma americanum serpin 41 (AAS41) inhibits inflammation by targeting chymase and chymotrypsin.International journal of biological macromolecules · 2020Article
- Identification of proteins from the secretory/excretory products (SEPs) of the branchiuran ectoparasite Argulus foliaceus (Linnaeus, 1758) reveals unique secreted proteins amongst haematophagous ecdysozoa.Parasites & vectors · 2020Article
- Discovery of Exosomes From Tick Saliva and Salivary Glands Reveals Therapeutic Roles for CXCL12 and IL-8 in Wound Healing at the Tick-Human Skin Interface.Frontiers in cell and developmental biology · 2020Article
- Amblyomma americanum serpin 27 (AAS27) is a tick salivary anti-inflammatory protein secreted into the host during feeding.PLoS neglected tropical diseases · 2019Article
- Immunomodulatory effects of Rhipicephalus haemaphysaloides serpin RHS2 on host immune responses.Parasites & vectors · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Ixodes scapularis is a medically important tick species that transmits causative agents of important human tick-borne diseases including borreliosis, anaplasmosis and babesiosis. An understanding of how this tick feeds is needed prior to the development of novel methods to protect the human population against tick-borne disease infections. This study characterizes a blood meal-induced I. scapularis (Ixsc) tick saliva serine protease inhibitor (serpin (S)), in-house referred to as IxscS-1E1. The hypothesis that ticks use serpins to evade the host's defense response to tick feeding is based on the assumption that tick serpins inhibit functions of protease mediators of the host's anti-tick defense response. Thus, it is significant that consistent with hallmark characteristics of inhibitory serpins, Pichia pastoris-expressed recombinant IxscS-1E1 (rIxscS-1E1) can trap thrombin and trypsin in SDS- and heat-stable complexes, and reduce the activity of the two proteases in a dose-responsive manner. Additionally, rIxscS-1E1 also inhibited, but did not apparently form detectable complexes with, cathepsin G and factor Xa. Our data also show that rIxscS-1E1 may not inhibit chymotrypsin, kallikrein, chymase, plasmin, elastase and papain even at a much higher rIxscS-1E1 concentration. Native IxscS-1E1 potentially plays a role(s) in facilitating I. scapularis tick evasion of the host's hemostatic defense as revealed by the ability of rIxscS-1E1 to inhibit adenosine diphosphate- and thrombin-activated platelet aggregation, and delay activated partial prothrombin time and thrombin time plasma clotting in a dose-responsive manner. We conclude that native IxscS-1E1 is part of the tick saliva protein complex that mediates its anti-hemostatic, and potentially inflammatory, functions by inhibiting the actions of thrombin, trypsin and other yet unknown trypsin-like proteases at the tick-host interface.
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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.