Related Experiment Video
Updated: Jul 27, 2026

Candida albicans Biofilm Chip (CaBChip) for High-throughput Antifungal Drug Screening
Published on: July 18, 2012
Recombinant human antibody single chain variable fragments reactive with Candida albicans surface antigens
C G Haidaris1, J Malone, L A Sherrill
1Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, 601 Elmwood Ave, Rochester, NY 14642, USA. haid@mail.rochester.edu
Abstract:
A combinatorial phage display library expressing human immunoglobulin heavy and light chain variable regions was used to identify phage clones capable of binding to the surface of Candida albicans blastoconidia. Single chain antibody variable fragments (scFv) derived from three clones detected C. albicans antigens by indirect immunofluorescence assay (IFA), enzyme-linked immunosorbent assay (ELISA), and Western blotting. The antigens detected were conserved among different strains of C. albicans and several other Candida species. Two scFv clones detected antigens specifically expressed by C. albicans blastoconidia; the third detected antigens in both blastoconidia and filamentous forms of C. albicans. The antigens containing the epitopes recognized by all three scFv could be extracted from blastoconidia by dithiothreitol, suggesting attachment to the cell wall via sulfhydryl bonds. Epitope detection by the scFv was sensitive to treatment of C. albicans blastoconidia with sodium periodate, but not proteinase K, indicating the cognate epitopes were composed of carbohydrate. Antigenic determinants for each of the three scFv were detected by immunohistochemical staining of skin sections from a model of cutaneous candidiasis, demonstrating expression in vivo. Through selection for the ability to bind intact organisms, the phage display system provides a means to rapidly identify monoclonal binding ligands to Candida surface antigens. Being entirely human, mature antibodies generated from the scFv have potential utility in the treatment of candidiasis.
Insights
Researchers identified human antibody fragments that bind to Candida albicans surface antigens. These fragments target carbohydrate epitopes and show potential for treating candidiasis.
Area of Science:
- Immunology
- Microbiology
- Biotechnology
Background:
- Candida albicans is a significant human pathogen.
- Developing effective treatments for candidiasis requires understanding its surface antigens.
- Phage display is a powerful tool for antibody discovery.
Purpose of the Study:
- To identify human antibody fragments targeting Candida albicans surface antigens using phage display.
- To characterize the binding properties and epitope specificities of identified antibody fragments.
- To assess the in vivo relevance and therapeutic potential of these antibody fragments.
Main Methods:
- Construction and screening of a human immunoglobulin phage display library.
- Selection of phage clones binding to Candida albicans blastoconidia.
- Characterization of single-chain variable fragments (scFv) using indirect immunofluorescence assay (IFA), ELISA, and Western blotting.
- Epitope analysis through dithiothreitol extraction, sodium periodate, and proteinase K treatment.
- Immunohistochemical staining in a model of cutaneous candidiasis.
Main Results:
- Three scFv clones successfully detected Candida albicans antigens.
- Antigens were conserved across C. albicans strains and other Candida species.
- Two scFv clones recognized blastoconidia-specific antigens; one recognized both blastoconidia and filamentous forms.
- Epitopes were linked to the cell wall via sulfhydryl bonds and were carbohydrate in nature.
- Antigenic determinants were expressed in vivo during cutaneous candidiasis.
Conclusions:
- Phage display enables rapid identification of monoclonal binding ligands to Candida surface antigens.
- The identified human scFv fragments offer potential for developing novel therapeutics against candidiasis.
- Understanding the carbohydrate nature of these epitopes could guide targeted antifungal strategies.
Related Concept Videos
Cross-reactivity
Candidiasis

