of some members as follow. DC‑associated C‑type lectin 1 (Dectin1) subfamily includes dectin 1/CLEC7A, DNGR1/CLEC9A, Myeloid C‑type lectin‑like receptor (MICL) (CLEC12A), CLEC2 (also called CLEC1B)- the platelet activation receptor for podoplanin on lymphatic endothelial cells and invading front of some carcinomas, and CLEC12B; while DC immunoreceptor (DCIR) subfamily includes DCIR/CLEC4A, Dectin 2/CLEC6A, Blood DC antigen 2 (BDCA2) ( CLEC4C), and Mincle i.e. macrophage‑inducible C‑type lectin (CLEC4E). The nomenclature (mannose versus asialoglycoprotein) is a bit misleading as these the asialoglycoprotein receptors are not necessarily galactose (one of the commonest outer residues of asialo-glycoprotein) specific receptors and even many of this family members can also bind to mannose after which the other group is named. NOD-like receptors (NLR) For more details, see NOD-like receptor. The NOD-like receptors (NLRs) are cytoplasmic proteins, which recognize bacterial peptidoglycans and mount proinflammatory and antimicrobial immune response. Approximately 20 of these proteins have been found in the mammalian genome and include nucleotide-binding oligomerization domain (NODs), which binds nucleoside triphosphate. Among other proteins the most important are: the MHC Class II transactivator (CIITA), IPAF, BIRC1 etc. The ligands are currently known for NOD1 and NOD2. NOD1 recognizes a molecule called meso-DAP, which is a peptidoglycan constituent only of Gram negative bacteria. NOD2 proteins recognize intracellular MDP (muramyl dipeptide), which is a peptidoglycan constituent of both Gram positive and Gram negative bacteria. When inactive, NODs are in the cytosol in a monomeric state and they undergo conformational change only after ligand recognition, which leads to their activation. NODs transduce signals in the pathway of NF-κB and MAP kinases via the serine-threonine kinase called RIP2. NODs signal via N-terminal CARD domains to activate downstream gene induction events, and interact with microbial molecules by means of a C-terminal leucine-rich repeat (LRR) region. The interaction and cooperation among different types of receptors typical for the innate immune system has been established. An interesting cooperation has been discovered between TLRs and NLRs, particularly between TLR4 and NOD1 in response to Escherichia coli infection. Another proof of the cooperation and integration of the entire immune system has been shown in vivo, when TLR signaling was inhibited or disabled, NOD receptors took over role of TLRs. Like NODs, NLRPs contain C-terminal LRRs, which appear to act as a regulatory domain and may be involved in the recognition of microbial pathogens. Also like NODs, these proteins contain a nucleotide binding site (NBS) for nucleoside triphosphates. Interaction