Characterization of FITC-conjugated lectin binding to Candida albicans

Smith, Stephen N., Armstrong, Richard A., Bird, Roger A., Chohan, Rita, Hartell, Nick A. and Poyner, David A. (2002). Characterization of FITC-conjugated lectin binding to Candida albicans. Mycologia, 93 (3), pp. 422-431.


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.

Divisions: Life & Health Sciences > Biosciences
Life & Health Sciences > Optometry
Life & Health Sciences > Ophthalmic Research Group
Life & Health Sciences
Life & Health Sciences > Pharmacy
Uncontrolled Keywords: avidity,flourescence,hyphal,mannose,yeast,Agricultural and Biological Sciences (miscellaneous),Plant Science
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Published Date: 2002-10-09
Authors: Smith, Stephen N.
Armstrong, Richard A. ( 0000-0002-5046-3199)
Bird, Roger A.
Chohan, Rita
Hartell, Nick A.
Poyner, David A. ( 0000-0003-1590-112X)

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