CD367/CLEC4A Protein, Human (HEK293, His)

CD367/CLEC4A protein functions as a C-type lectin receptor with a preference for binding carbohydrates mannose and fucose, and a weaker interaction with N-acetylglucosamine (GlcNAc) in a Ca(2+)-dependent manner. This receptor plays a crucial role in regulating immune reactivity and, upon antigen triggering, undergoes internalization through clathrin-dependent endocytosis. Consequently, it delivers its antigenic cargo into the antigen presentation pathway, leading to the cross-priming of CD8(+) T cells. Notably, this cross-presentation and cross-priming are augmented by TLR7 and TLR8 agonists, resulting in increased expansion of CD8(+) T cells and heightened production of IFNG and TNF, while reducing levels of IL4, IL5, and IL13. In plasmacytoid dendritic cells, CD367/CLEC4A inhibits TLR9-mediated IFNA and TNF production. Furthermore, it may be involved in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation via its ITIM motif (immunoreceptor tyrosine-based inhibitory motifs). In the context of microbial infection, CD367/CLEC4A is implicated in the interaction between HIV-1 virus and dendritic cells, enhancing HIV-1 binding and virus infection through an ITIM motif-associated signal transduction pathway involving phosphatases PTPN6 and PTPN11, SYK, Src kinases, and MAP kinases.