An insight into the proteome of the saliva of the argasid tick Ornithodoros moubata reveals important differences in saliva protein composition between the sexes

J Proteomics. 2013 Mar 27:80:216-35. doi: 10.1016/j.jprot.2013.01.015. Epub 2013 Feb 4.

Abstract

Tick saliva contains pharmacologically active molecules that allow these parasites to obtain a blood meal from the host and facilitate host infection by tick-borne pathogens. Recent transcriptomic and proteomic analyses of the salivary glands of several tick species have provided data sets that are invaluable for a better understanding of tick sialomes and tick-host-pathogen relationships. Here we performed a proteomic study of the saliva from the argasid tick Ornithodoros moubata. Saliva samples from female and male specimens were analyzed separately by LC-MS/MS before and after their equalization to facilitate the identification of the less abundant proteins. We report the array of 193 proteins identified in the saliva of O. moubata showing: (i) the broad and complex composition of the saliva of this tick, in good agreement with the complexity of the argasid and ixodid sialomes described previously; (ii) a notable difference in the saliva proteomes of females and males, since only 10 of the proteins identified appeared to be shared by both sexes; and (iii) the presence in the salivary fluid of a wide range of proteins known to be housekeeping/intracellular, which could be secreted in unconventional ways, including exosome secretion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Animals
  • Chromatography, Liquid
  • Computational Biology
  • Electrophoresis, Polyacrylamide Gel
  • Exosomes / metabolism
  • Expressed Sequence Tags
  • Female
  • Male
  • Ornithodoros / physiology*
  • Phosphopyruvate Hydratase / metabolism
  • Proteome / metabolism*
  • Proteomics
  • Recombinant Proteins / metabolism
  • Saliva / metabolism*
  • Sex Factors*
  • Tandem Mass Spectrometry

Substances

  • Actins
  • Proteome
  • Recombinant Proteins
  • Phosphopyruvate Hydratase