C-type lectin receptor (CLR) (CLR)

C-type lectin receptors (CLRs) are a large and diverse superfamily of proteins characterized by their calcium-dependent carbohydrate-recognition domains (CRDs). They are primarily expressed on myeloid cells, such as dendritic cells and macrophages, where they serve as essential pattern recognition receptors (PRRs) that detect conserved glycan structures on fungi, bacteria, and viruses (Zelensky & Gready, 2005). Beyond their role in innate immunity, CLRs mediate critical processes including cell-cell adhesion, glycoprotein endocytosis, and platelet activation (Drouin et al., 2020). In disease states, CLRs are implicated in the pathogenesis of infectious diseases, chronic inflammatory conditions, and the facilitation of tumor immune evasion (Geijtenbeek & Gringhuis, 2009). Therapeutic interventions targeting specific CLRs include selectin inhibitors for vaso-occlusive crises in sickle cell disease and the use of CLR agonists as vaccine adjuvants to modulate adaptive immune responses (Brown et al., 2018). Because the term C-type lectin encompasses a broad range of proteins with distinct biological roles, it is generally considered a protein class rather than a single specific therapeutic target.

Other names

Calcium-dependent lectinC-type lectin domain-containing proteinCTLD-containing proteinC-type lectin superfamily

Binding to carbohydrate-recognition domains to modulate immune signaling or inhibit cell-cell adhesion.