title: The immunobiology of Campylobacter jejuni: Innate immunity and autoimmune diseases.
abstract: The Gram-negative bacterium Campylobacter jejuni causes gastroenteritis and Guillain-Barré syndrome in humans. Recent advances in the immunobiology of C. jejuni have been made. This review summarizes C. jejuni-binding innate receptors and highlights the role of innate immunity in autoimmune diseases. This human pathogen produces a variety of glycoconjugates, including human ganglioside-like determinants and multiple activators of Toll-like receptors (TLRs). Furthermore, C. jejuni targets MyD88, NLRP3 inflammasome, TIR-domain-containing adapter-inducing interferon-β (TRIF), sialic acid-binding immunoglobulin-like lectins (Siglecs), macrophage galactose-type lectin (MGL), and immunoglobulin-like receptors (TREM2, LMIR5/CD300b). The roles of these innate receptors and signaling molecules have been extensively studied. MyD88-mediated TLR activation or inflammasome-dependent IL-1β secretion is essential for autoimmune induction. TRIF mediates the production of type I interferons that promote humoral immune responses and immunoglobulin class-switching. Siglec-1 and Siglec-7 interact directly with gangliosides. Siglec-1 activation enhances phagocytosis and inflammatory responses. MGL internalizes GalNAc-containing glycoconjugates. TREM2 is well-known for its role in phagocytosis. LMIR5 recognizes C. jejuni components and endogenous sulfoglycolipids. Several lines of evidence from animal models of autoimmune diseases suggest that simultaneous activation of innate immunity in the presence of autoreactive lymphocytes or antigen mimicry may link C. jejuni to immunopathology.
authors.affiliation: Division of Immunotechnology, MIEDITOR, 5-4-25 Chihaya, Fukuoka 813-0044, Japan. Electronic address: contact@mieditor.com.
authors.forename: Vongsavanh
authors.initials: V
authors.lastname: Phongsisay
mesh_terms: D033942:Adaptor Proteins, Vesicular Transport / Q000235:genetics / Q000276:immunology; D000818:Animals; D002169:Campylobacter Infections / Q000235:genetics / Q000276:immunology* / Q000382:microbiology / Q000473:pathology; D016123:Campylobacter jejuni / Q000276:immunology* / Q000472:pathogenicity; D002352:Carrier Proteins / Q000235:genetics / Q000276:immunology; D005759:Gastroenteritis / Q000235:genetics / Q000276:immunology* / Q000382:microbiology / Q000473:pathology; D005786:Gene Expression Regulation; D006001:Glycoconjugates / Q000276:immunology / Q000378:metabolism; D020275:Guillain-Barre Syndrome / Q000235:genetics / Q000276:immunology* / Q000382:microbiology / Q000473:pathology; D054884:Host-Pathogen Interactions / Q000276:immunology*; D006801:Humans; D007113:Immunity, Innate; D058847:Inflammasomes / Q000276:immunology; D037181:Lectins, C-Type / Q000235:genetics / Q000276:immunology; D008562:Membrane Glycoproteins / Q000235:genetics / Q000276:immunology; D018716:Molecular Mimicry; D053594:Myeloid Differentiation Factor 88 / Q000235:genetics / Q000276:immunology; D000071199:NLR Family, Pyrin Domain-Containing 3 Protein; D011971:Receptors, Immunologic / Q000235:genetics / Q000276:immunology; D063265:Sialic Acid Binding Immunoglobulin-like Lectins / Q000235:genetics / Q000276:immunology
chemical_list: D033942:Adaptor Proteins, Vesicular Transport; C519445:CD300LB protein, human; D002352:Carrier Proteins; D006001:Glycoconjugates; D058847:Inflammasomes; D037181:Lectins, C-Type; C506225:MGL lectin, human; C507779:MYD88 protein, human; D008562:Membrane Glycoproteins; D053594:Myeloid Differentiation Factor 88; D000071199:NLR Family, Pyrin Domain-Containing 3 Protein; C453881:NLRP3 protein, human; D011971:Receptors, Immunologic; D063265:Sialic Acid Binding Immunoglobulin-like Lectins; C470409:TICAM1 protein, human; C498715:TREM2 protein, human
keywords: Autoimmune diseases; Campylobacter jejuni; Innate immunity; Receptor