Opsonizing properties of rat ficolin-A in the defence against Cryptococcus neoformans

We further assessed the biological consequence of the ficolin-A recognition of acapsular C. neoformans by investigating their interaction with lung epithelial cells (type II pneumocytes cell line A549). Flow cytometric analysis demonstrated that ficolin-A opsonized acapsular C. neoformans showed significantly increased adherence to A549 cells when exposed to acidic conditions compared to the unopsonized controls (p = 0.04). We conclude that ficolin-A binds acapsular C. neoformans via their carbohydrate recognizing fibrinogen-like domains leading to enhanced uptake by lung epithelial cells in vitro.