Immune recognition has always been one of the main points of interest in immunology. It is well appreciated that there are several distinct strategies of immune recognition that operate in the mammalian immune system. These are traditionally grouped as innate and adaptive, based on the use of either germline-encoded or somatically-generated receptors, respectively. Beyond the genetic nature of the receptors involved, however, the distinction between the two types of immune recognition is not always clear-cut. For example, complement receptors, TLRs, and presumably other types of non-clonal "innate" immune receptors can cooperate with B cell receptors in pathogen recognition, and this involves, at least in some cases, co-recognition by the two types of receptors. In addition, the architecture of antigen receptor complexes bears a striking resemblance to a class of innate immune receptor complexes that signal through ITAM-containing adaptor proteins, such as DAP12. In both cases multi-protein receptor complexes are assembled through ionic interactions between charged residues in the transmembrane regions and signal through similar pathways involving ITAM dependent activation of Syk-72 and ZAP-70.Although the classification of immune recognition into innate and adaptive is useful in many ways, it may obscure the heterogeneity of receptors and mechanisms of innate immune recognition. Indeed, the mammalian innate immune system uses several different classes of receptors, including TLRs, NODs, and NALPS, Dectins, RIG-I and MDA-5 and others [1,2]. Some of the receptors are transmembrane proteins (e.g., TLRs and Dectins), some are secreted (e.g., penthaxins and collectins), and some are intracellular cytoplasmic receptors (e.g., RIG-I/MDA-5, NODs).