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Updated: Aug 11, 2026

Live-cell Video Microscopy of Fungal Pathogen Phagocytosis
Published on: January 9, 2013
The C-type lectin DC-SIGN (CD209) is an antigen-uptake receptor for Candida albicans on dendritic cells
Alessandra Cambi1, Karlijn Gijzen, l Jolanda M de Vries
1Department of Tumor Immunology, Nijmegen Center for Molecular Life Sciences, University Medical Center Nijmegen, Nijmegen, The Netherlands.
Insights
Dendritic cells (DC) utilize DC-SIGN to bind Candida albicans. This receptor internalizes the fungus, revealing its role in capturing both viruses and fungi.
Area of Science:
- Immunology
- Microbiology
- Cell Biology
Background:
- Dendritic cells (DCs) in submucosal tissues are crucial for HIV-1 entry.
- The fungus Candida albicans frequently infects similar submucosal sites.
Purpose of the Study:
- To investigate the role of DC-SIGN (CD209) in binding and internalizing Candida albicans.
- To determine if DC-SIGN acts as a pathogen-uptake receptor for fungi.
Main Methods:
- Binding assays using DC-SIGN-transfected cell lines and human monocyte-derived DCs.
- Experiments with live and heat-inactivated C. albicans.
- Microscopy to observe internalization into DC-SIGN-enriched vesicles.
Main Results:
- DC-SIGN effectively binds both live and inactivated C. albicans in a time- and concentration-dependent manner.
- Immature DCs internalize C. albicans via DC-SIGN into distinct vesicles.
- This internalization pathway is separate from the mannose receptor pathway.
Conclusions:
- DC-SIGN functions as a significant receptor for C. albicans uptake by dendritic cells.
- DC-SIGN's role extends beyond viral capture to include fungal pathogens.
- This finding highlights DC-SIGN as a versatile receptor in innate immunity against diverse microbes.
Abstract:
Dendritic cells (DC) that express the type II C-type lectin DC-SIGN (CD209) are located in the submucosa of tissues, where they mediate HIV-1 entry. Interestingly, the pathogen Candida albicans, the major cause of hospital-acquired fungal infections, penetrates at similar submucosal sites. Here we demonstrate that DC-SIGN is able to bind C. albicans both in DC-SIGN-transfected cell lines and in human monocyte-derived DC. The binding was shown to be time- as well as concentration-dependent, and live as well as heat-inactivated C. albicans were bound to the same extent. Moreover, in immature DC, DC-SIGN was able to internalize C. albicans in specific DC-SIGN-enriched vesicles, distinct from those containing the mannose receptor, the other known C. albicans receptor expressed by DC. Together, these results demonstrate that DC-SIGN is an exquisite pathogen-uptake receptor that captures not only viruses but also fungi.
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