title: Complementing the inflammasome.
abstract: The innate immune system is an ancient surveillance system able to sense microbial invaders as well as aberrations in normal cell function. No longer viewed as a static and non-specific part of immunity, the innate immune system employs a plethora of specialized pattern recognition sensors to monitor and achieve homeostasis; these include the Toll-like receptors, the retinoic acid-inducible gene-like receptors, the nucleotide-binding oligomerization domain receptors (NLRs), the C-type lectins and the complement system. In order to increase specificity and diversity, innate immunity uses homotypic and heterotypic associations among these different components. Multi-molecular assemblies are formed both on the cell surface and in the cytosol to respond to pathogen and danger signals. Diverse, but tailored, responses to a changing environment are orchestrated depending on the the nature of the challenge and the repertoire of interacting receptors and components available in the sensing cell. It is now emerging that innate immunity operates a system of 'checks and balances' where interaction among the sensors is key in maintaining normal cell function. Complement sits at the heart of this alarm system and it is becoming apparent that it is capable of interacting with all the other pathways to effect a tailored immune response. In this review, we will focus on complement interactions with NLRs, the so-called 'inflammasomes', describing the molecular mechanisms that have been revealed so far and discussing the circumstantial evidence that exists for these interactions in disease states.
authors.affiliation: Institute of Infection and Immunity, School of Medicine, University Hospital of Wales, Cardiff University, Cardiff, UK.
authors.forename: Martha
authors.initials: M
authors.lastname: Triantafilou
authors.affiliation: Institute of Infection and Immunity, School of Medicine, University Hospital of Wales, Cardiff University, Cardiff, UK.
authors.forename: Timothy R
authors.initials: TR
authors.lastname: Hughes
authors.affiliation: Institute of Infection and Immunity, School of Medicine, University Hospital of Wales, Cardiff University, Cardiff, UK.
authors.forename: Bryan Paul
authors.initials: BP
authors.lastname: Morgan
authors.affiliation: Institute of Infection and Immunity, School of Medicine, University Hospital of Wales, Cardiff University, Cardiff, UK.
authors.forename: Kathy
authors.initials: K
authors.lastname: Triantafilou
mesh_terms: D000818:Animals; D000893:Anti-Inflammatory Agents / Q000627:therapeutic use; D003167:Complement Activation / Q000187:drug effects; D003165:Complement System Proteins / Q000276:immunology* / Q000378:metabolism; D006801:Humans; D007113:Immunity, Innate / Q000187:drug effects; D058847:Inflammasomes / Q000187:drug effects / Q000276:immunology* / Q000378:metabolism; D007249:Inflammation / Q000276:immunology* / Q000378:metabolism / Q000517:prevention & control; D018836:Inflammation Mediators / Q000276:immunology / Q000378:metabolism; D008024:Ligands; D011971:Receptors, Immunologic / Q000276:immunology / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D000893:Anti-Inflammatory Agents; D058847:Inflammasomes; D018836:Inflammation Mediators; D008024:Ligands; D011971:Receptors, Immunologic; D003165:Complement System Proteins
keywords: cell surface molecules; complement; inflammasome; inflammation; innate lymphoid cells