Parasitology Research

, Volume 96, Issue 6, pp 402–409

Mechanisms associated with Acanthamoeba castellanii (T4) phagocytosis

  • Selwa Alsam
  • James Sissons
  • Ricky Dudley
  • Naveed Ahmed Khan
Original Paper

DOI: 10.1007/s00436-005-1401-z

Cite this article as:
Alsam, S., Sissons, J., Dudley, R. et al. Parasitol Res (2005) 96: 402. doi:10.1007/s00436-005-1401-z

Abstract

Using fluorescein isothiocyanate (FITC)-labelled Escherichia coli, phagocytosis in Acanthamoeba is studied. This assay is based on the quenching effect of trypan blue on FITC-labelled E. coli. Only intracellular E. coli retain their fluorescence, which are easily discriminated from non-fluorescent adherent bacteria. Acanthamoeba uptake of E. coli is significantly reduced in the presence of genistein, a protein tyrosine kinase inhibitor. In contrast, sodium orthovanadate (protein tyrosine phosphatase inhibitor) increases bacterial uptake by Acanthamoeba. Treatment of Acanthamoeba with cytochalasin D (actin polymerization inhibitor) abolished the ability of Acanthamoeba to phagocytose E. coli suggesting that tyrosine kinase-mediated signaling may play a role in Acanthamoeba phagocytosis. In addition, we showed that phosphatidylinositol 3-kinase (PI3K) plays an important role in Acanthamoeba uptake of E. coli. Role of mannose-binding protein in Acanthamoeba phagocytosis is discussed further.

Copyright information

© Springer-Verlag 2005

Authors and Affiliations

  • Selwa Alsam
    • 1
  • James Sissons
    • 1
  • Ricky Dudley
    • 1
  • Naveed Ahmed Khan
    • 1
  1. 1.School of Biological and Chemical Sciences, BirkbeckUniversity of LondonLondonUK

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