Characterization of FITC-conjugated lectin binding to Candida albicans

Stephen N. Smith*, Richard A. Armstrong, Roger A. Bird, Rita Chohan, Nick A. Hartell, David A. Poyner

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Avidity of yeast and hyphal forms of Candida albicans for FITC-conjugated lectins was determined by flow cytometry and digital microscopy. Yeast phase cells bound Con A, a lectin with marked affinity for mannose, irrespective of growth phase, yet demonstrated little avidity for WGA and SBA. Yeast phase cell avidity for mannose-specific lectins was characterized through determination of FITC-conjugated Con A, LcH, PSA and GNA binding and subsequent calculation of Bmax, EC50 and Hn values. Such an approach, through comparison among FITC-conjugated lectins of differing specific activities, furnishes further insight into exposed outer cell wall mannose moieties. The rank order of lectin affinity as defined by EC50 values was GNA > Con A > LcH > PSA. Values for Hn suggest that lectins predominantly bind to a single receptor class, the relative abundance of which as defined by Bmax values was PSA > GNA > Con A > LcH. Hyphal surfaces in common with yeast phase cells demonstrated marked avidity for FITC-Con A, however, fluorescence of Candida morphological forms differed significantly, indicative of varying outer cell wall mannose exposure.

Original languageEnglish
Pages (from-to)422-431
Number of pages10
Issue number3
Publication statusPublished - 9 Oct 2002


  • avidity
  • flourescence
  • hyphal
  • mannose
  • yeast


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