While Dectin-1 is a well-known C-type lectin receptor recognizing b-glucan and involved in anti-fungal immunity, human Dectin-1 is O-glycosylated and acts as a ligand for another C-type lectin receptor, CLEC-2, expressed by platelets that mediates homeostatic responses such as lymphangiogenesis.

The establishment of forward genetics in S. rosetta reveals the first gene known to be required for choanoflagellate multicellular development.

The diffusional barrier formed between phagocyte integrin and fungal glucans preserves the microbiostatic phagocytic environment generated during the frustrated phagocytosis of Candida albicans hypha.

The information stored in glycans is interpreted and read by cell surface-exposed lectin receptors, and with information theory, the formal framework is set for how to analyze such complex single-cell data.

The expression of DECTIN-2 family C-type lectin receptors on macrophages and monocytes is inhibited by the Th2 cytokine IL-4, which suggests a mechanism for inhibition of Th17 responses to MINCLE-dependent vaccination responses by underlying helminth infection.

A genetic screen reveals that two predicted glycosyltransferases promote rosette development and prevent cell clumping in one of the closest living relatives of animals, the choanoflagellate S. rosetta.

A C-type lectin domain protein is an anabolic growth factor that promotes mesenchymal progenitors in the bone marrow to differentiate into bone cells to maintain skeletal bone mass throughout adult life.

Controlled neo-glycosylation of antigens can influence intracellular routing of antigens and the nature and strength of immune response, and should therefore be considered as a major determinant in the design of vaccines against cancer and infectious diseases.