Classification of C-Type Lectins and Recognition of Pathogens

Abstract

C-type lectins are calcium-dependent glycan-binding proteins that play key roles in the innate immune response by recognizing pathogens. Soluble C-type lectins agglutinate and neutralize pathogens, activate the complement system, and promote pathogen clearance via opsonization. Membrane-bound C-type lectins, also known as C-type lectin receptors (CLRs), internalize pathogens and induce their degradation in lysosomes, presenting pathogen-derived antigens to MHC-II molecules to activate adaptive immunity. CLRs also have signaling capabilities. Some contain the immunoreceptor tyrosine-based activation motif (ITAM), which induces inflammatory responses by activating transcription factors, such as NF-κB and NFAT. Others contain the immunoreceptor tyrosine-based inhibitory motif (ITIM), which suppresses activating signals by activating phosphatases, such as SHP-1. This creates a balance between activation and inhibition. C-type lectins are classified into 17 groups based on their structural domains, with Groups II and V members being particularly important for pathogen recognition. In this review, we present the accumulated and recent information on pathogen recognition by C-type lectins, along with their classification and basic functions.