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Structure, function, and evolution of biogenic amine-binding proteins in soft ticks.

Ben J Mans1, José M C Ribeiro, John F Andersen

  • 1Laboratory for Malaria and Vector Research, NIAID, National Institutes of Health, Rockville, Maryland 20852, USA.

The Journal of Biological Chemistry
|May 1, 2008
PubMed
Summary
This summary is machine-generated.

Two tick lipocalins, monomine and monotonin, bind histamine and serotonin. Their structures reveal a single binding site, differing from other tick proteins, suggesting independent evolution of histamine binding.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Evolutionary Biology

Background:

  • Lipocalins are abundant proteins in tick salivary glands.
  • Some lipocalins bind biogenic amines like histamine and serotonin, crucial for tick feeding.
  • Previous studies suggested multiple binding sites in tick lipocalins.

Purpose of the Study:

  • To determine the crystal structures of monomine and a monotonin paralog.
  • To compare ligand binding determinants in tick lipocalins.
  • To investigate the evolution of biogenic amine binding in ticks.

Main Methods:

  • Isolation and purification of monomine and monotonin from Argas monolakensis salivary glands.
  • X-ray crystallography to determine protein-ligand complex structures.
  • Biochemical binding assays.
  • Bioinformatic analysis and gene expression.

Main Results:

  • Monomine and monotonin possess single ligand-binding sites, unlike the previously described two sites in FS-HBP.
  • Binding site analysis revealed conserved interactions with the aliphatic amine group and variable interactions with the aromatic portion of ligands.
  • Histamine binding mechanisms differ between monomine and FS-HBP, indicating independent evolution.
  • Biogenic amine-binding proteins were identified in soft and hard ticks, enabling evolutionary reconstruction.

Conclusions:

  • Tick lipocalins monomine and monotonin exhibit distinct ligand-binding characteristics.
  • The evolution of biogenic amine binding in ticks is likely a result of independent events.
  • A conserved tick lipocalin biogenic amine-binding motif was identified, aiding in functional prediction for other lipocalins.