Cell surface lectin-binding glycoconjugates on marine planktonic protists

FEMS Microbiol Lett. 2006 Dec;265(2):202-7. doi: 10.1111/j.1574-6968.2006.00484.x.

Abstract

Carbohydrate-protein interactions appear to play an important role in the phagocytosis of microbial prey by free-living protozoa. The present study utilizes FITC-labelled plant lectins to investigate the presence and localization of cell surface glycoconjugates on live and fixed planktonic protists (Dunaliella primolecta, Oxyrrhis marina, Goniomonas amphinema, Paraphysomonas vestita and Euplotes vannus). With live flagellate preparations, lectins primarily bound to external cell surfaces, with minimal internal staining observed. In contrast, cell fixation permeabilized cell membranes, allowing lectins to bind to internal structures, such as nuclear membranes and food vacuoles, interfering with the characterization of cell surface glycoconjugates. The method developed to label cell surface sugar moieties of live planktonic protists successfully overcomes the problems associated with fixation, and thus provides a useful protocol for future studies on protistan cell surface carbohydrate characterization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Membrane Structures / chemistry*
  • Ciliophora / chemistry*
  • Ciliophora / microbiology
  • Concanavalin A
  • Eukaryota / chemistry*
  • Eukaryota / microbiology
  • Fluorescein-5-isothiocyanate
  • Glycoconjugates / chemistry*
  • Lectins / metabolism*
  • Plankton / chemistry*
  • Plankton / microbiology
  • Receptors, Concanavalin A / chemistry
  • Receptors, Mitogen / chemistry
  • Seawater / microbiology
  • Staining and Labeling / methods*
  • Wheat Germ Agglutinins

Substances

  • Glycoconjugates
  • Lectins
  • Receptors, Concanavalin A
  • Receptors, Mitogen
  • Wheat Germ Agglutinins
  • wheat germ agglutinin receptor
  • Concanavalin A
  • Fluorescein-5-isothiocyanate