Abstract

Antihistamine response: a dynamically refined function at the host-tick interface

Highlights

  • Ticks counteract host inflammatory responses by secreting proteins from their saliva that compete for histamine binding

  • In response to tissue damage or a hypersensitivity reaction, histamine is released by mast cells and basophils that bind to its native receptors to facilitate repairing agents or mediators of the immune response arriving at the injury site [1]

  • The crystal structure of one of these tick salivary RaHBPs (Ra-HBP2) revealed a few structural deviations from the archetypal lipocalin protein family, that it sequesters two histamine molecules, and causes an inhibition of guinea-pig ileum to contract by competing with Human histamine 1 receptor (H1R)/H2R for histamine binding [6]

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Summary

Introduction

Ticks counteract host inflammatory responses by secreting proteins from their saliva that compete for histamine binding. Among these tick salivary proteins are lipocalins, antiparallel beta-barrel proteins that sequester small molecules. A salivary lipocalin from the tick Dermacentor reticulates sequesters both serotonin and histamine causing an inhibition of guinea-pig ileum to contract [5]. The crystal structure of one of these tick salivary RaHBPs (Ra-HBP2) revealed a few structural deviations from the archetypal lipocalin protein family, that it sequesters two histamine molecules, and causes an inhibition of guinea-pig ileum to contract by competing with H1R/H2R for histamine binding [6]. Understanding the mechanics of tick salivary lipocalins will provide a better insight of the hostectoparasite interface

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