Alternative titles; symbols
HGNC Approved Gene Symbol: CX3CR1
Cytogenetic location: 3p22.2 Genomic coordinates (GRCh38): 3:39,263,494-39,292,966 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 3p22.2 | {Coronary artery disease, resistance to} | 607339 | 3 | |
| {Macular degeneration, age-related, 12} | 613784 | 3 | ||
| {Rapid progression to AIDS from HIV1 infection} | 609423 | 3 |
Chemokines play pivotal roles in health and disease by controlling migration and tissue localization of specific types of cells expressing their cognate receptors. Humans have at least 45 chemokines, which are grouped into 4 subfamilies (CXC, CC, C, and CX3C) based on the structural motif of their N-terminal conserved cysteine residues. Chemokine receptors, such as CX3CR1, belong to the 7-transmembrane G protein-coupled receptor (GPCR) family and are grouped into 4 subfamilies based on the subfamily of their chemokine ligand. CX3CR1 is the receptor for fractalkine (CX3CL1; 601880) and is mainly expressed by CD16 (FCGR3A; 146740)-high natural killer (NK) cells, terminally differentiated cytotoxic CD8 (see 186910)-positive T cells, and monocytes (summary by Nakayama et al., 2010).
Raport et al. (1995) performed PCR on human genomic DNA with degenerate primers designed using the sequences of the IL8 GPCRs. Several unique PCR products were obtained and used to screen a human peripheral blood mononuclear cell cDNA library. One gene identified in this manner was termed V28. The deduced amino acid sequence of V28 revealed a 355-amino acid polypeptide which displays the features common to other GPCRs, including 7 putative transmembrane domains and a highly conserved 20-amino acid region. Raport et al. (1995) also noted that V28 contains a 7-amino acid sequence that is conserved among chemokine receptors. Raport et al. (1995) found that V28 is 81% identical at the amino acid level to the rat orphan GPCR-encoding gene RBS11 and 39 to 40% identical to several human chemokine GPCRs including chemokine receptor-1 (CMKBR1; 601159). Northern blot analysis on V28 showed a single transcript of 3.2 kb expressed at highest levels in brain, peripheral blood leukocytes, and spleen. The authors also observed high levels of transcript in THP.1 myeloid cells, lower levels in U937 and HL60 myeloid cells, and no expression in lymphoid cell lines.
Garin et al. (2003) identified 2 splice variants of CX3CR1 encoding proteins with N-terminal extensions of 7 and 32 amino acids that did not change the global charge of the protein. Quantitative PCR showed that both variants were expressed in monocytes, NK cells, and CD4 (186940) and CD8 lymphocytes.
Combadiere et al. (2007) analyzed CX3CR1 expression in the eyes of healthy donors and patients with age-related macular degeneration (ARMD; see 603075) and found that all retinal microglial cells expressed CX3CR1.
Analysis of a genomic clone of V28 by Raport et al. (1995) revealed that it does not contain introns.
Raport et al. (1995) used human-mouse somatic cell hybrids to map the V28 (CX3CR1) gene to 3pter-p21, near CMKBR1. Based on the sequence similarity of V28 to several chemokine receptors, its expression in leukocytes, and its chromosomal location near CMKBR1, Raport et al. (1995) speculated that V28 may be a member of the chemokine receptor (CCR) family. By radiation hybrid analysis and organization of BAC contigs by FISH on combed genomic DNA, Maho et al. (1999) localized the CX3CR1 gene within the CCR cluster at 3p21.3.
Leukocyte trafficking at the endothelium requires both cellular adhesion molecules and chemotactic factors. Fractalkine (CX3CL1; 601880), a transmembrane molecule with a CX3C-motif chemokine domain atop a mucin stalk, induces both adhesion and migration of leukocytes. Imai et al. (1997) identified a 7-transmembrane high-affinity receptor for fractalkine and showed that it mediates both the adhesive and migratory functions of fractalkine. The receptor, which the authors termed CX3CR1, requires pertussis toxin-sensitive G protein signaling to induce migration but not to support adhesion, which also occurs without other adhesion molecules but requires the architecture of a chemokine domain atop the mucin stalk. Natural killer cells predominantly express CX3CR1 and respond to fractalkine in both migration and adhesion. Imai et al. (1997) concluded that fractalkine and CX3CR1 represent new types of leukocyte trafficking regulators, performing both adhesive and chemotactic functions.
CX3CR1 is an HIV coreceptor as well as a leukocyte chemotactic/adhesion receptor for fractalkine. Faure et al. (2000) identified 2 single nucleotide polymorphisms in the CX3CR1 gene in Caucasians and demonstrated that HIV-infected patients homozygous for I249/M280 (601470.0001) progressed to AIDS more rapidly than those with other haplotypes (relative risk = 2.13, P = 0.039) (see 609423). Functional CX3CR1 analysis showed that fractalkine binding is reduced among patients homozygous for this particular haplotype. Thus, Faure et al. (2000) concluded that CX3CR1-I249/M280 is a recessive genetic risk factor for HIV/AIDS.
Tripp et al. (2001) showed that the G glycoprotein of respiratory syncytial virus (RSV) shares a heparin-binding domain and a CX3C chemokine motif with CX3CL1. Binding analysis indicated that RSV can use CX3CR1 as a receptor. G glycoprotein binding mimics fractalkine binding and induces leukocyte chemotaxis. Tripp et al. (2001) concluded that RSV G glycoprotein uses its similarities with CX3C to facilitate infection and to modify the immune response.
Garin et al. (2003) found that both CX3CR1 isoforms containing N-terminal extensions bound CX3CL1. CX3CL1 acted as an agonist and induced migration of cells expressing the N-terminally extended CX3CR1 isoforms. HIV-1 fused more readily with the N-terminally extended CX3CR1 isoforms than with the 'classic' form of CX3CR1.
By immunocytochemical analysis, Lucas et al. (2003) investigated the expression of fractalkine and its receptor in human coronary artery plaques. A subset of mononuclear cells expressed high levels of fractalkine in atherosclerotic plaques, and smooth muscle cells within the neointima expressed CX3CR1. There was a positive correlation between the number of fractalkine-expressing cells and the number of CX3CR1-positive cells in 15 plaques (r = 0.70). Cultured vascular smooth muscle cells expressing CX3CR1 underwent chemotaxis toward a fractalkine source, and chemotaxis was inhibited by G-protein inactivation. Lucas et al. (2003) concluded that fractalkine can act as a mediator of smooth muscle cell migration in human atherosclerosis, rather than mediate inflammatory cell recruitment.
Niess et al. (2005) identified a myeloid-derived mucosal dendritic cell in mice, which populates the entire lamina propria of the small intestine. Lamina propria dendritic cells depended on the chemokine receptor CX3CR1 to form transepithelial dendrites which enable the cells to directly sample luminal antigens. CX3CR1 controlled the clearance of enteroinvasive pathogens by dendritic cells. Thus, Niess et al. (2005) concluded that CX3CR1-dependent processes, which control host interactions of specialized dendritic cells with commensal and pathogenic bacteria, may regulate immunologic tolerance and inflammation.
Using chemotaxis and cellular assays, as well as flow cytometry and RT-PCR analysis, Nakayama et al. (2010) demonstrated that CCL26 (604697) is a functional ligand of both CCR3 (601268) and CX3CR1. At relatively high concentrations, human CCL26 induced calcium flux and chemotaxis in mouse cells expressing human CX3CR1, but not mouse Cx3cr1, and competed with CX3CL1 for CX3CR1 binding. Like CX3CL1, CCL26 attracted eosinophils, NK cells, terminally differentiated CD8-positive cytotoxic T lymphocytes, and homeostatic monocytes. Intraperitoneal injection of CCL26 resulted in rapid recruitment of mouse eosinophils and intravenously injected human NK cells to the peritoneal cavity. IL4-stimulated human umbilical vein endothelial cells produced CCL26 and induced adhesion of CX3CR1-expressing cells. Psoriasis (see 177900) and atopic dermatitis (see 603165) lesions both expressed CX3CR1 mRNA, but CX3CL1 was expressed in the former and only sometimes in the latter. In contrast, CCL26 was always expressed in atopic dermatitis lesions. Nakayama et al. (2010) suggested that CCL26 may be partly responsible for the recruitment of cells expressing CX3CR1 in atopic dermatitis lesions when CX3CL1 expression is low. They concluded that CCL26 is another agonist for CX3CR1 and may act in allergic diseases by attracting eosinophils via CCR3 and killer lymphocytes and resident monocytes via CX3CR1.
Leonardi et al. (2018) identified CX3CR1+ mononuclear phagocytes (MNPs) as being essential for the initiation of innate and adaptive immune responses to intestinal fungi. CX3CR1+ MNPs express antifungal receptors and activate antifungal responses in a Syk (600085)-dependent manner. Genetic ablation of CX3CR1+ MNPs in mice led to changes in gut fungal communities and to severe colitis that was rescued by antifungal treatment. In Crohn disease patients, a missense mutation (T280M; see 601470.0001) in the CX3CR1 gene was identified and found to be associated with impaired antifungal responses. Leonardi et al. (2018) concluded that their results unravelled a role of CX3CR1+ MNPs in mediating interactions between intestinal mycobiota and host immunity at steady state and during inflammatory disease.
Small intestinal mononuclear cells that express CX3CR1 regulate immune responses. CX3CR1+ cells take up luminal antigens by protruding their dendrites into lumen. Morita et al. (2019) showed in mice that the bacterial metabolites pyruvic acid and lactic acid induce dendrite protrusion via GPR31 (602043) in CX3CR1+ cells. Mice that lack GPR31, which was highly and selectively expressed in intestinal CX3CR1+ cells, showed defective dendrite protrusions of CX3CR1+ cells in the small intestine. A methanol-soluble fraction of the small intestinal contents of specific-pathogen-free mice, but not germ-free mice, induced dendrite extension of intestinal CX3CR1+ cells in vitro. Morita et al. (2019) purified a GPR31-activating fraction, and identified lactic acid. Both lactic acid and pyruvic acid induced dendrite extension of CX3CR1+ cells of wildtype mice, but not of Gpr31b-null mice. Oral administration of lactate and pyruvate enhanced dendrite protrusion of CX3CR1+ cells in the small intestine of wildtype mice, but not in that of Gpr31b-null mice. Furthermore, wildtype mice treated with lactate or pyruvate showed an enhanced immune response and high resistance to intestinal Salmonella infection. Morita et al. (2019) concluded that their findings demonstrated that lactate and pyruvate, which are produced in the intestinal lumen in a bacteria-dependent manner, contribute to enhanced immune responses by inducing GPR31-mediated dendrite protrusion of intestinal CX3CR1+ cells.
Human Immunodeficiency Virus Type 1, Rapid Progression to AIDS
Among 565 Caucasian HIV-infected individuals, Faure et al. (2000) found an association between more rapid progression to full-blown AIDS (see 609423) and 2 missense mutations in the CX3CR1 gene that were in complete linkage disequilibrium (V249I/T280M; 601470.0001).
Resistance to Coronary Artery Disease
In a study of 151 patients with acute coronary syndromes (see 607339) and 249 healthy controls, Moatti et al. (2001) found an association between the I249 allele (601470.0001) of the CX3CR1 gene and a markedly reduced risk of acute coronary events.
McDermott et al. (2003) analyzed individuals with and without cardiovascular disease from the Offspring Cohort of the Framingham Heart Study and observed an association between CX3CR1-M280 and a lower risk of cardiovascular disease.
Age-Related Macular Degeneration 12
Tuo et al. (2004) found an increased prevalence of CX3CR1 I249/M280 (601470.0001) carriers among cases of age-related macular degeneration (ARMD12; 613784) compared to controls.
Combadiere et al. (2007) observed that homozygosity for the CX3CR1 M280 allele was consistently more frequent in ARMD patients compared to patients with other diseases from previously published studies.
Associations Pending Confirmation
For discussion of a possible association between susceptibility to developmental dysplasia of the hip (DDH2; 615612) and mutation in the CX3CR1 gene, see 601470.0001.
Lesnik et al. (2003) found prominent expression of fractalkine in smooth muscle cells underlying macrophages in atherosclerotic plaques from apoE (107741)-null mice fed a high-fat diet. However, fractalkine was not strongly expressed within the macrophages themselves, indicating that macrophages were not the primary source of the cytokine. Compared to the apoE-null mice, mice doubly null for apoE and the fractalkine receptor Cx3cr1 showed a significant reduction in aortic atherosclerotic plaque lesion formation and lesion progression after being fed a high-fat diet. In addition, there was a significant reduction in numbers of macrophages within the plaques in mice doubly null for apoE and Cx3cr1 compared to apoE-null mice. Lesnik et al. (2003) concluded that fractalkine recruits monocytes and macrophages to the vessel wall and plays a role in the formation of atherosclerotic lesions.
Combadiere et al. (2007) studied Cx3cr1-deficient mice and observed that microglial cells accumulated subretinally with age and albino background and after laser impact preceding retinal degeneration. Drusen-like lipid-laden subretinal microglial cells were seen on funduscopy of senescent Cx3cr1-null mice, and Cx3cr1-dependent microglial cell accumulation was associated with an exacerbation of experimental choroidal neovascularization.
Mionnet et al. (2010) observed reduced lung disease after allergen sensitization and challenge in Cx3cr1-deficient mice and in wildtype mice treated with Cx3cr1-blocking agents. Transfer of wildtype Cd4-positive T cells to Cx3cr1-deficient mice restored asthma features, and Cx3cr1-blocking agents prevented airway inflammation in Cx3cr1-deficient mice injected with wildtype Th2 cells. Flow cytometric analysis demonstrated that Cx3cr1 promoted survival of and resistance to apoptosis in Th2 cells, which were required for airway disease. Further studies showed that Cx3cr1 conferred a survival advantage to both Th1 and Th2 cells in inflamed airways, but not under homeostatic conditions or in inflamed peripheral lymph nodes.
Human Immunodeficiency Virus Type 1, Rapid Progression to AIDS
Faure et al. (2000) used SSCP to screen the CX3CR1 coding sequence for mutations in 78 random French Caucasian blood donors. They found 5 SNPs, all in transmembrane domains of the receptor. Two of them, a G-to-A transition that changed val249 to iso (V249I) and a C-to-T transition that changed thr280 to met (T280M), were quite common, occurring in 25.7% and 13.5%, respectively, of the uninfected population. These 2 mutations were found to be in complete linkage disequilibrium and their respective frequencies among 565 Caucasian HIV-infected individuals were 71.4% homozygous wildtype, 12.4% heterozygous, and 16.2% homozygous mutant. Patients who were homozygous for the mutations had a more rapid progression to full-blown AIDS and probably had increased susceptibility to HIV infection (see 609423).
Resistance to Coronary Artery Disease
When Moatti et al. (2001) analyzed CX3CR1 genotypes in 151 patients with acute coronary syndromes and in 249 healthy controls, they found that I249 heterozygosity was associated with a markedly reduced risk of acute coronary events, independent of established acquired coronary risk factors (e.g., smoking and diabetes). Consistent with this, functional analysis of peripheral blood mononuclear cells showed that CX3CR1 I249 heterozygosity was associated with a significant decrease in the number of fractalkine (CX3CL1; 601880)-binding sites per cell. The results suggested that CX3CR1 may be involved in the pathogenesis of atherosclerotic disease.
McDermott et al. (2003) demonstrated that fractalkine-dependent cell-cell adhesion under conditions of physiologic shear was severely reduced in cells expressing CX3CR1-M280, and this was associated with marked reduction in the kinetics of fractalkine binding as well as reduced fractalkine-induced chemotaxis of primary leukocytes from donors homozygous for CX3CR1-M280. In 204 individuals with cardiovascular disease and 1,655 individuals without cardiovascular disease from the Offspring Cohort of the Framingham Heart Study, they found that CX3CR1-M280 was independently associated with a lower risk of cardiovascular disease (adjusted odds ratio, 0.60; p = 0.008). (McDermott et al. (2003) stated that because M280 always appears in the presence of I249, they referred to the receptor protein bearing both of those variant amino acids as CX3CR1-M280.)
Age-Related Macular Degeneration 12
In a screen of 117 patients with age-related macular degeneration and 276 controls, Tuo et al. (2004) found an increased prevalence, with the highest odds ratio of 3.57, of I249 and M280 carriers among age-related macular degeneration (ARMD12; 613784) cases compared with controls. In archived eye sections, CX3CR1 transcripts were not detectable in the maculae of ARMD eyes bearing T/M280; transcripts were detected in the maculae of normal eyes bearing T/T280 or T/M280 as well as in AMD maculae bearing T/T280. Lower CX3CR1 protein expression was observed in the maculae of AMD eyes bearing T/M280 compared with controls bearing T/T280.
Combadiere et al. (2007) found that homozygosity for the CX3CR1 M280 allele was consistently more frequent in ARMD patients compared to patients with other diseases from previously published studies. They also found that chemotaxis of monocytes from individuals with homozygous I249/M280 genotypes was impaired in the presence of bound CX3CR1.
Developmental Dysplasia of the Hip
In a large 4-generation Utah family segregating autosomal dominant developmental dysplasia of the hip mapping to chromosome 3p22.2 (DDH2; 615612), Feldman et al. (2013) identified heterozygosity for the M280 variant (rs3732378) in 17 affected family members and obligate heterozygotes as well as in 7 family members with fewer signs of DDH, 12 unaffected family members, and 5 unaffected married-in individuals. Noting that M280 is a relatively common variant with an allele frequency of 0.173 among Utah residents with Northern and Western European ancestry, Feldman et al. (2013) suggested that in this family the variant may be necessary but not sufficient by itself to cause the disorder.
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